Found 2 structures.
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1. Compound ID: 1015
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-5)-b-D-Araf-(1-2)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf |
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Structure type: fragment of a bigger structure
Trivial name: nonreducing terminal epitope of lipoarabinomannan
Contained glycoepitopes: IEDB_130701,IEDB_1309625,IEDB_136104,IEDB_140116,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_857718,IEDB_857722,IEDB_857726,IEDB_857728,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 303
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: 16653
b-D-Araf-(1-2)-a-D-Araf-(1-3)-+
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a-D-Araf-(1-4)-a-D-Manp-(1-2)-a-D-Manp-(1-5)-b-D-Araf-(1-2)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-5)-b-D-Araf-(1-2)-a-D-Araf-(1-3)-+ |
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-5)-b-D-Araf-(1-2)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-{{{-a-D-Araf-(1-5)-}}}/n=13/-a-D-Araf-(1--/mannan core-phoshatidyl-inositol/
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Suc-(1-2)-+ |
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Structure type: oligomer
Aglycon: mannan core-phoshatidyl-inositol
Trivial name: mannose-capped lipoarabinomannan (MtLAM)
Contained glycoepitopes: IEDB_130701,IEDB_1309625,IEDB_134619,IEDB_136104,IEDB_140116,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_857717,IEDB_857718,IEDB_857720,IEDB_857722,IEDB_857723,IEDB_857726,IEDB_857727,IEDB_857728,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 6463
Shimokawa M, Ishiwata A, Kashima T, Nakashima C, Li J, Fukushima R, Sawai N, Nakamori M, Tanaka Y, Kudo A, Morikami S, Iwanaga N, Akai G, Shimizu N, Arakawa T, Yamada C, Kitahara K, Tanaka K, Ito Y, Fushinobu S, Fujita K "Identification and characterization of endo-α-, exo-α-, and exo-β-D-arabinofuranosidases degrading lipoarabinomannan and arabinogalactan of mycobacteria" -
Nature Communications 14(1) (2023) 5803
The cell walls of pathogenic and acidophilic bacteria, such as Mycobacterium tuberculosis and Mycobacterium leprae, contain lipoarabinomannan and arabinogalactan. These components are composed of D-arabinose, the enantiomer of the typical L-arabinose found in plants. The unique glycan structures of mycobacteria contribute to their ability to evade mammalian immune responses. In this study, we identified four enzymes (two GH183 endo-D-arabinanases, GH172 exo-α-D-arabinofuranosidase, and GH116 exo-β-D-arabinofuranosidase) from Microbacterium arabinogalactanolyticum. These enzymes completely degraded the complex D-arabinan core structure of lipoarabinomannan and arabinogalactan in a concerted manner. Furthermore, through biochemical characterization using synthetic substrates and X-ray crystallography, we elucidated the mechanisms of substrate recognition and anomer-retaining hydrolysis for the α- and β-D-arabinofuranosidic bonds in both endo- and exo-mode reactions. The discovery of these D-arabinan-degrading enzymes, along with the understanding of their structural basis for substrate specificity, provides valuable resources for investigating the intricate glycan architecture of mycobacterial cell wall polysaccharides and their contribution to pathogenicity.
characterization, enzyme, Mycobacteria, arabinogalactan, lipoarabinomannan, arabinofuranosidase
NCBI PubMed ID: 37726269Publication DOI: 10.1038/s41467-023-41431-2Journal NLM ID: 101528555Publisher: London: Nature Publishing Group
Correspondence: S. Fushinobu
; K. Fujita
Institutions: Faculty of Agriculture, Kagoshima University, Kagoshima, 890-0065, Japan, Cluster for Pioneering Research, RIKEN, Saitama, 351-0198, Japan, Department of Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo, 113-8657, Japan, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki, 305-0801, Japan, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Noda, Chiba, 278-8510, Japan, School of Agriculture, Meiji University, Kawasaki, Kanagawa, 214-8571, Japan, Department of Chemical Science and Engineering, Tokyo Institute of Technology, Meguro-ku, Tokyo, 152-8552, Japan, Graduate School of Science, Osaka University, Osaka, 560-0043, Japan, CRIIM, The University of Tokyo, Bunkyo-ku, Tokyo, 113-8657, Japan
Methods: 1H NMR, SDS-PAGE, DNA techniques, TLC, enzymatic degradation, HPLC, electron microscopy, crystallography, enzyme assay, HPAEC-PAD, ESI-TOF-MS, genome sequencing, qPCR RT, SEC-MALS/RI, SEC-SAXS
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