CSDB: Search results

Taxonomic group: bacteria / Firmicutes (Phylum: Firmicutes)
Associated disease: infection due to Clostridium difficile [ICD11: XN0SE

]

NCBI PubMed ID: 32010066
Publication DOI: 10.3389/fmicb.2019.02909
Journal NLM ID: 101548977
Publisher: Lausanne: Frontiers Research Foundation
Correspondence: Dolores Solis <d.solis

iqfr.csic.es>
Institutions: Instituto de Quimica Fisica Rocasolano, Consejo Superior de Investigaciones Cientificas, Madrid, Spain, Centro de Investigacion Biomedica en Red de Enfermedades Respiratorias, Instituto de Salud Carlos III, Madrid, Spain, UCIBIO, Department of Chemistry, Faculty of Science and Technology, NOVA University of Lisbon, Lisbon, Portuga

Bacterial surfaces are decorated with distinct carbohydrate structures that may substantially differ among species and strains. These structures can be recognized by a variety of glycan-binding proteins, playing an important role in the bacteria cross-talk with the host and invading bacteriophages, and also in the formation of bacterial microcolonies and biofilms. In recent years, different microarray approaches for exploring bacterial surface glycans and their recognition by proteins have been developed. A main advantage of the microarray format is the inherent miniaturization of the method, which allows sensitive and high-throughput analyses with very small amounts of sample. Antibody and lectin microarrays have been used for examining bacterial glycosignatures, enabling bacteria identification and differentiation among strains. In addition, microarrays incorporating bacterial carbohydrate structures have served to evaluate their recognition by diverse host/phage/bacterial glycan-binding proteins, such as lectins, effectors of the immune system, or bacterial and phagic cell wall lysins, and to identify antigenic determinants for vaccine development. The list of samples printed in the arrays includes polysaccharides, lipopoly/lipooligosaccharides, (lipo)teichoic acids, and peptidoglycans, as well as sequence-defined oligosaccharide fragments. Moreover, microarrays of cell wall fragments and entire bacterial cells have been developed, which also allow to study bacterial glycosylation patterns. In this review, examples of the different microarray platforms and applications are presented with a view to give the current state-of-the-art and future prospects in this field.

antibodies, immune system, lectins, vaccine development, microarrays, bacterial glycans, bacterial interactions

Structure type: polymer chemical repeating unit
Location inside paper: fig.5, C. difficile PSI repeating unit
Trivial name: cell-surface polysaccharide, pentaglycosyl phosphate repeating unit cell-surface polysaccharide, rhamnoglucan PSI, PS1, cell-surface polysaccharide PS-I, PSI, PSI repeating unit
Compound class: cell wall polysaccharide, lipoteichoic acid
Contained glycoepitopes: IEDB_136105,IEDB_142488,IEDB_144998,IEDB_145002,IEDB_146664,IEDB_189515,IEDB_189517,IEDB_225177,IEDB_232583,IEDB_232584,IEDB_232585,IEDB_885823,IEDB_983931,SB_192

Comments, role: review

Related record ID(s): 3282, 3283, 3284, 3285, 3286, 3287, 3288, 3289
NCBI Taxonomy refs (TaxIDs): 1496
Reference(s) to other database(s): GTC:G60087JR, GlycomeDB:36857
Show glycosyltransferases

There is only one chemically distinct structure:

*O[C@H]1[C@H](C)O[C@@H](O[C@@H]2[C@@H](O)[C@H](O[C@@H]3[C@@H](CO)O[C@H](O[C@@H]4[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]4OP(*)(=O)O)[C@H](O)[C@H]3O[C@@H]3O[C@@H](C)[C@H](O)[C@@H](O)[C@H]3O)O[C@H](CO)[C@H]2O)[C@H](O)[C@@H]1O

SVG MW SMILES 3D mol Ionize