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Optimization of Virulence Functions Through Glucosylation of Shigella LPS
Nicholas P. West,1*Philippe Sansonetti,2*Joëlle Mounier,2Rachel M. Exley,1Claude Parsot,2Stéphanie Guadagnini,3Marie-Christine Prévost,3Ada Prochnicka-Chalufour,4Muriel Delepierre,4Myriam Tanguy,2Christoph M. Tang1
Shigella, the leading cause of bacillary dysentery, uses a typeIII 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 antigenof lipopolysaccharide (LPS) on its surface. We show that bacteriophage-encodedglucosylation of Shigella O antigen, the basis of differentserotypes, shortens the LPS molecule by around half. This enhancesTTSS function without compromising the protective propertiesof the LPS. Thus, LPS glucosylation promotes bacterial invasionand evasion of innate immunity, which may have contributed tothe emergence of serotype diversity in Shigella.
1 Centre for Molecular Microbiology and Infection, Department of Infectious Diseases, Faculty of Medicine, Flowers Building, Imperial College London, London SW7 2AZ, UK 2 Unité de Pathogénie Microbienne Moléculaire, Unité INSERM 389, Institut Pasteur, 28 rue du Dr. Roux, F-75724 Paris Cédex 15, France. 3 Plate-Forme de Microscopie Electronique, Institut Pasteur, 28 rue du Dr. Roux, F-75724 Paris Cédex 15, France. 4 Unité de Résonance Magnétique Nucléaire des Biomolécules, URA 2185 CNRS; Unité INSERM 389, Institut Pasteur, 28 rue du Dr. Roux, F-75724 Paris Cédex 15, France.
* These authors contributed equally to this work.
Present address: Centenary Institute of Cancer Medicine andCell Biology, Newtown, NSW 2042, Australia.
To whom correspondence should be addressed. E-mail: c.tang{at}imperial.ac.uk
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[DOI: 10.1126/science.1109836] |Summary »|Full Text »|PDF »
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