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Optimization of Virulence Functions Through Glucosylation of Shigella LPS

Authors :
Muriel Delepierre
Nicholas P. West
Philippe J. Sansonetti
Joëlle Mounier
Stéphanie Guadagnini
Ada Prochnicka-Chalufour
Christoph M. Tang
Rachel M. Exley
Myriam Tanguy
Claude Parsot
Marie-Christine Prévost
Centre for Molecular Microbiology and Infection
Faculty of Medicine-Department of Infectious Diseases
Pathogénie Microbienne Moléculaire
Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)
Microscopie électronique (Plate-forme)
Institut Pasteur [Paris]
Résonance Magnétique Nucléaire des Biomolécules
Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)
Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Institut Pasteur [Paris] (IP)
Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)
Source :
Science, Science, American Association for the Advancement of Science, 2005, 307 (5713), pp.1313-7. ⟨10.1126/science.1108472⟩, Science, 2005, 307 (5713), pp.1313-7. ⟨10.1126/science.1108472⟩
Publication Year :
2005
Publisher :
American Association for the Advancement of Science (AAAS), 2005.

Abstract

Shigella , the leading cause of bacillary dysentery, uses a type III secretion system (TTSS) to inject proteins into human cells, leading to bacterial invasion and a vigorous inflammatory response. The bacterium is protected against the response by the O antigen of lipopolysaccharide (LPS) on its surface. We show that bacteriophage-encoded glucosylation of Shigella O antigen, the basis of different serotypes, shortens the LPS molecule by around half. This enhances TTSS function without compromising the protective properties of the LPS. Thus, LPS glucosylation promotes bacterial invasion and evasion of innate immunity, which may have contributed to the emergence of serotype diversity in Shigella .

Details

ISSN :
10959203 and 00368075
Volume :
307
Database :
OpenAIRE
Journal :
Science
Accession number :
edsair.doi.dedup.....758205c8ca8c4134123890bd5a0c4d4e
Full Text :
https://doi.org/10.1126/science.1108472