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1. Compound ID: 1014
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b-D-GlcpNAc-(1-4)-+
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D-Ala-(2-1)-mPmN2-(2-5)-D-Glu-(2-1)-L-Ala-(2-8)-b-Murp
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Gc-(1-2)-+ |
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Structure type: oligomer
Trivial name: peptidoglycan monomer
Compound class: peptidoglycan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 302
Lee RE, Brennan PJ, Besra GS "Mycobacterium tuberculosis cell envelope" -
Book: Tuberculosis (series: Current Topics in Microbiology and Immunology) (1996) Vol. 215, 1-27
The mycobacterial cell wall is a complex and intriguing mixture of components which sets Mycobacterium tuberculosis apart from all other known bacterial species (Goodfellow and Minnikin 1984). To understand the M. tuberculosis cell wall, one must first consider the biology of the tubercle bacillus. Tuberculosis has long been known as a cause of morbidity and mortality worldwide. Indeed it is believed that one third of the word’s population is infected with M. tuberculosis (Sudre et al. 1992). Evidence of tuberculosis-like infections date back many thousands of years, and it is very likely that tuberculosis-related infections have plagued humankind since the dawn of civilization. M. tuberculosis is primarily an intracellular pathogen which resides within the phagolysosomes of alveolar macrophages. Perhaps as a consequence of this intracellular environment, the highly intricate features of the tubercle bacilli cell wall have undergone extensive evolutionary changes.
lipid, Mycobacteria, membrane, arabinogalactan, cell envelope, lipoarabinomannan, Mycobacterium tuberculosis, peptidoglycan
Publication DOI: 10.1007/978-3-642-80166-2_1Publisher: Berlin, Heidelberg: Springer.
Editors: Shinnick TM
Institutions: Department of Microbiology, Colorado State University, Fort Collins, CO, 80523, USA
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2. Compound ID: 1877
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D-Ala-(?-?)-mPmN2-(?-?)-D-Glu-(2-1)-L-Ala-(2-8)-+
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-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1- |
Show graphically |
Structure type: polymer chemical repeating unit
; 943.5 [M+H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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3. Compound ID: 1992
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mPmN2-(?-?)-D-Glu-(?-1)-L-Ala-(2-8)-+
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-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1- |
Show graphically |
Structure type: polymer chemical repeating unit
; 870.4 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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4. Compound ID: 1993
Structure type: polymer chemical repeating unit
; 568.6 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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5. Compound ID: 1994
|
D-Ala-(?-?)-mPmN2-(?-?)-D-Glu-(2-1)-L-Ala-(2-8)-+
|
-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1-
Mur-lactam = muramic acid δ-lactam (open form) |
Show graphically |
Structure type: polymer chemical repeating unit
; 1378.3 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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6. Compound ID: 1995
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D-Ala-(?-?)-mPmN2-(?-?)-D-Glu-(2-1)-L-Ala-(2-8)-+
|
-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1-
Mur-lactam = muramic acid δ-lactam (reduced form) |
Show graphically |
Structure type: polymer chemical repeating unit
; 1346.0 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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7. Compound ID: 1996
|
D-Ala-(?-?)-mPmN2-(?-?)-D-Glu-(2-1)-L-Ala-(2-8)-+
|
-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1-
Mur-lactam = muramic acid δ-lactam |
Show graphically |
Structure type: polymer chemical repeating unit
; 1361.2 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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8. Compound ID: 1997
|
L-Ala-(2-8)-+
|
-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1-
Mur-lactam = muramic acid δ-lactam (open form) |
Show graphically |
Structure type: polymer chemical repeating unit
; 1005.6 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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9. Compound ID: 1998
|
L-Ala-(2-8)-+
|
-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1-
Mur-lactam = muramic acid δ-lactam (reduced form) |
Show graphically |
Structure type: polymer chemical repeating unit
; 973.5 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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10. Compound ID: 1999
|
L-Ala-(2-8)-+
|
-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1-
Mur-lactam = muramic acid δ-lactam |
Show graphically |
Structure type: polymer chemical repeating unit
; 987.6 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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11. Compound ID: 2000
|
D-Ala-(?-?)-mPmN2-(?-?)-D-Glu-(2-1)-L-Ala-(2-8)-+
|
-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1-
Mur-lactam = muramic acid δ-lactam (one of them reduced) |
Show graphically |
Structure type: polymer chemical repeating unit
; 1764.2 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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12. Compound ID: 2001
|
D-Ala-(?-?)-mPmN2-(?-?)-D-Glu-(2-1)-L-Ala-(2-8)-+
|
-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1-
Mur-lactam = muramic acid δ-lactam |
Show graphically |
Structure type: polymer chemical repeating unit
; 1778.2 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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13. Compound ID: 2002
|
L-Ala-(2-8)-+
|
-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1-
Mur-lactam = muramic acid δ-lactam (one of them reduced) |
Show graphically |
Structure type: polymer chemical repeating unit
; 1391.4 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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14. Compound ID: 2003
|
L-Ala-(2-8)-+
|
-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp-lactam-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1-
Mur-lactam = muramic acid δ-lactam |
Show graphically |
Structure type: polymer chemical repeating unit
; 1406.1 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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15. Compound ID: 2004
|
D-Ala-(?-?)-mPmN2-(?-?)-D-Glu-(2-1)-L-Ala-(2-8)-+
|
-4)-b-D-GlcpNAc-(1-4)-b-Murp-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp-(1-4)-b-D-GlcpNAc-(1-4)-b-Murp2Ac-(1- |
Show graphically |
Structure type: polymer chemical repeating unit
; 2194.6 [M-H]+
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
The structure is contained in the following publication(s):
- Article ID: 616
Atrih A, Zollner P, Allmaier G, Foster SJ "Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation" -
Journal of Bacteriology 178(21) (1996) 6173-6183
The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.
role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation
NCBI PubMed ID: 8892816Publication DOI: 10.1128/jb.178.21.6173-6183.1996Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: s.foster@sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria
Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
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