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Pietri GP, Bertuzzi S, Karnicar K, Unione L, Lisnic B, Malic S, Miklic K, Novak M, Calloni I, Santini L, Usenik A, Romano MR, Adamo R, Jonjic S, Turk D, Jiménez-Barbero J, Lenac Rovis T
Antigenic determinants driving serogroup-specific antibody response to Neisseria meningitidis C, W, and Y capsular polysaccharides: Insights for rational vaccine design
Carbohydrate Polymers 341 (2024)
ID 122349
Neisseria meningitidis C
(NCBI TaxID 135720,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
NCBI PubMed ID: 38876728Publication DOI: 10.1016/j.carbpol.2024.122349Journal NLM ID: 8307156Publisher: Elsevier
Correspondence: Jiménez-Barbero J <jbarbero
cicbiogune.es>; Lenac Rovis T <tihana.lenac
uniri.hr>
Institutions: IKERBASQUE, Basque Foundation for Science, Bilbao, Spain, GSK, Siena, Italy, Center for Proteomics, Faculty of Medicine, University of Rijeka, Rijeka, Croatia, CICbioGUNE, Basque Research & Technology Alliance (BRTA), Bizkaia Technology Park, Building 800, Derio, Spain, Jožef Stefan Institute, Department of Biochemistry and Molecular and Structural Biology, Ljubljana, Slovenia, Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins (CIPKeBiP), Ljubljana, Slovenia, Department of Organic and Inorganic Chemistry, Faculty of Science and Technology, University of the Basque Country, Leioa, Spain, Centro de Investigaciґon Biomґedica En Red de Enfermedades Respiratorias, Madrid, Spain
Meningococcal glycoconjugate vaccines sourced from capsular polysaccharides (CPSs) of pathogenic Neisseria meningitidis strains are well-established measures to prevent meningococcal disease. However, the exact structural factors responsible for antibody recognition are not known. CPSs of Neisseria meningitidis serogroups Y and W differ by a single stereochemical center, yet they evoke specific immune responses. Herein, we developed specific monoclonal antibodies (mAbs) targeting serogroups C, Y, and W and evaluated their ability to kill bacteria. We then used these mAbs to dissect structural elements responsible for carbohydrate-protein interactions. First, Men oligosaccharides were screened against the mAbs using ELISA to select putative lengths representing the minimal antigenic determinant. Next, molecular interaction features between the mAbs and serogroup-specific sugar fragments were elucidated using STD-NMR. Moreover, X-ray diffraction data with the anti-MenW CPS mAb enabled the elucidation of the sugar-antibody binding mode. Our findings revealed common traits in the epitopes of all three sialylated serogroups. The minimal binding epitopes typically comprise five to six repeating units. Moreover, the O-acetylation of the neuraminic acid moieties was fundamental for mAb binding. These insights hold promise for the rational design of optimized meningococcal oligosaccharides, opening new avenues for novel production methods, including chemical or enzymatic approaches
Structure type: polymer chemical repeating unit
Location inside paper: pg. 5, Fig. 4, Fig. 5, MenC
Compound class: polysaccharide, O-epitope
Methods: 13C NMR, 1H NMR, NMR-2D, DNA sequencing, X-ray, DNA techniques, ELISA, Western blotting, biological assays, cloning, gene expression
3D data: molecular dynamics
Related record ID(s): 15682, 15683
NCBI Taxonomy refs (TaxIDs): 135720
Show glycosyltransferases
1H NMR data: present in publication
|
13C NMR data: present in publication
|
There is only one chemically distinct structure:
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Pietri GP, Bertuzzi S, Karnicar K, Unione L, Lisnic B, Malic S, Miklic K, Novak M, Calloni I, Santini L, Usenik A, Romano MR, Adamo R, Jonjic S, Turk D, Jiménez-Barbero J, Lenac Rovis T
Antigenic determinants driving serogroup-specific antibody response to Neisseria meningitidis C, W, and Y capsular polysaccharides: Insights for rational vaccine design
Carbohydrate Polymers 341 (2024)
ID 122349
Neisseria meningitidis W
(Ancestor NCBI TaxID 487,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
NCBI PubMed ID: 38876728Publication DOI: 10.1016/j.carbpol.2024.122349Journal NLM ID: 8307156Publisher: Elsevier
Correspondence: Jiménez-Barbero J <jbarbero
cicbiogune.es>; Lenac Rovis T <tihana.lenac
uniri.hr>
Institutions: IKERBASQUE, Basque Foundation for Science, Bilbao, Spain, GSK, Siena, Italy, Center for Proteomics, Faculty of Medicine, University of Rijeka, Rijeka, Croatia, CICbioGUNE, Basque Research & Technology Alliance (BRTA), Bizkaia Technology Park, Building 800, Derio, Spain, Jožef Stefan Institute, Department of Biochemistry and Molecular and Structural Biology, Ljubljana, Slovenia, Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins (CIPKeBiP), Ljubljana, Slovenia, Department of Organic and Inorganic Chemistry, Faculty of Science and Technology, University of the Basque Country, Leioa, Spain, Centro de Investigaciґon Biomґedica En Red de Enfermedades Respiratorias, Madrid, Spain
Meningococcal glycoconjugate vaccines sourced from capsular polysaccharides (CPSs) of pathogenic Neisseria meningitidis strains are well-established measures to prevent meningococcal disease. However, the exact structural factors responsible for antibody recognition are not known. CPSs of Neisseria meningitidis serogroups Y and W differ by a single stereochemical center, yet they evoke specific immune responses. Herein, we developed specific monoclonal antibodies (mAbs) targeting serogroups C, Y, and W and evaluated their ability to kill bacteria. We then used these mAbs to dissect structural elements responsible for carbohydrate-protein interactions. First, Men oligosaccharides were screened against the mAbs using ELISA to select putative lengths representing the minimal antigenic determinant. Next, molecular interaction features between the mAbs and serogroup-specific sugar fragments were elucidated using STD-NMR. Moreover, X-ray diffraction data with the anti-MenW CPS mAb enabled the elucidation of the sugar-antibody binding mode. Our findings revealed common traits in the epitopes of all three sialylated serogroups. The minimal binding epitopes typically comprise five to six repeating units. Moreover, the O-acetylation of the neuraminic acid moieties was fundamental for mAb binding. These insights hold promise for the rational design of optimized meningococcal oligosaccharides, opening new avenues for novel production methods, including chemical or enzymatic approaches
Structure type: polymer chemical repeating unit
Location inside paper: pg. 5, Fig. 4, Fig. 5, MenW
Compound class: polysaccharide, O-epitope
Contained glycoepitopes: IEDB_142488,IEDB_144998,IEDB_146664,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, NMR-2D, DNA sequencing, X-ray, DNA techniques, ELISA, Western blotting, biological assays, cloning, gene expression
3D data: molecular dynamics
Related record ID(s): 15681, 15683
NCBI Taxonomy refs (TaxIDs): 487
Show glycosyltransferases
1H NMR data: present in publication
|
13C NMR data: present in publication
|
There is only one chemically distinct structure:
Expand this record
Collapse this record
Pietri GP, Bertuzzi S, Karnicar K, Unione L, Lisnic B, Malic S, Miklic K, Novak M, Calloni I, Santini L, Usenik A, Romano MR, Adamo R, Jonjic S, Turk D, Jiménez-Barbero J, Lenac Rovis T
Antigenic determinants driving serogroup-specific antibody response to Neisseria meningitidis C, W, and Y capsular polysaccharides: Insights for rational vaccine design
Carbohydrate Polymers 341 (2024)
ID 122349
Neisseria meningitidis Y
(NCBI TaxID 648194,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
NCBI PubMed ID: 38876728Publication DOI: 10.1016/j.carbpol.2024.122349Journal NLM ID: 8307156Publisher: Elsevier
Correspondence: Jiménez-Barbero J <jbarbero
cicbiogune.es>; Lenac Rovis T <tihana.lenac
uniri.hr>
Institutions: IKERBASQUE, Basque Foundation for Science, Bilbao, Spain, GSK, Siena, Italy, Center for Proteomics, Faculty of Medicine, University of Rijeka, Rijeka, Croatia, CICbioGUNE, Basque Research & Technology Alliance (BRTA), Bizkaia Technology Park, Building 800, Derio, Spain, Jožef Stefan Institute, Department of Biochemistry and Molecular and Structural Biology, Ljubljana, Slovenia, Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins (CIPKeBiP), Ljubljana, Slovenia, Department of Organic and Inorganic Chemistry, Faculty of Science and Technology, University of the Basque Country, Leioa, Spain, Centro de Investigaciґon Biomґedica En Red de Enfermedades Respiratorias, Madrid, Spain
Meningococcal glycoconjugate vaccines sourced from capsular polysaccharides (CPSs) of pathogenic Neisseria meningitidis strains are well-established measures to prevent meningococcal disease. However, the exact structural factors responsible for antibody recognition are not known. CPSs of Neisseria meningitidis serogroups Y and W differ by a single stereochemical center, yet they evoke specific immune responses. Herein, we developed specific monoclonal antibodies (mAbs) targeting serogroups C, Y, and W and evaluated their ability to kill bacteria. We then used these mAbs to dissect structural elements responsible for carbohydrate-protein interactions. First, Men oligosaccharides were screened against the mAbs using ELISA to select putative lengths representing the minimal antigenic determinant. Next, molecular interaction features between the mAbs and serogroup-specific sugar fragments were elucidated using STD-NMR. Moreover, X-ray diffraction data with the anti-MenW CPS mAb enabled the elucidation of the sugar-antibody binding mode. Our findings revealed common traits in the epitopes of all three sialylated serogroups. The minimal binding epitopes typically comprise five to six repeating units. Moreover, the O-acetylation of the neuraminic acid moieties was fundamental for mAb binding. These insights hold promise for the rational design of optimized meningococcal oligosaccharides, opening new avenues for novel production methods, including chemical or enzymatic approaches
Structure type: polymer chemical repeating unit
Location inside paper: pg. 5, Fig. 4, Fig. 5, MenY
Compound class: polysaccharide, O-epitope
Contained glycoepitopes: IEDB_136906,IEDB_137472,IEDB_141794,IEDB_151528,IEDB_190606,SB_7
Methods: 13C NMR, 1H NMR, NMR-2D, DNA sequencing, X-ray, DNA techniques, ELISA, Western blotting, biological assays, cloning, gene expression
3D data: molecular dynamics
Related record ID(s): 15681, 15682
NCBI Taxonomy refs (TaxIDs): 648194
Show glycosyltransferases
1H NMR data: present in publication
|
13C NMR data: present in publication
|
There is only one chemically distinct structure:
Expand this record
Collapse this record
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