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Microbiology 150 (2004), 1079-1084; DOI  10.1099/mic.0.26840-0
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Microbiology 150 (2004), 1079-1084; DOI  10.1099/mic.0.26840-0
© 2004 Society for General Microbiology

The role of the Shigella flexneri yihE gene in LPS synthesis and virulence

Bryn Edwards-Jones1, Paul R. Langford2, J. Simon Kroll2 and Jun Yu1

1 Centre for Molecular Microbiology and Infection, Department of Biological Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK
2 Molecular Infectious Diseases Group, Department of Paediatrics, Faculty of Medicine, Imperial College London, St Mary's Campus, London W2 1PG, UK

Correspondence
Jun Yu
jun.yu{at}imperial.ac.uk

Previously, the authors have shown that inactivation of Shigella flexneri yihE, a gene of unknown function upstream of dsbA, which encodes a periplasmic disulphide catalyst, results in a global change of gene expression. Among the severely down-regulated genes are galETKM, suggesting that the yihE mutant, Sh54, may inefficiently produce the UDP-glucose and UDP-galactose required for LPS synthesis. This paper demonstrates that LPS synthesis in Sh54 is impaired. As a result, Sh54 is unable to polymerize host cell actin, due to aberrant localization of IcsA, or to cause keratoconjunctivitis in guinea pigs. Furthermore, Sh54 is more sensitive to some antimicrobial agents, and exhibits epithelial cytotoxicity characteristic of neither wild-type nor dsbA mutants. Supplying galETK in trans restores LPS synthesis and corrects all the defects. Hence, it is clear that the Shigella yihE gene is important not only in regulating global gene expression, as shown previously, but also in virulence through LPS synthesis via regulating the expression of the galETK operon.

Abbreviations: LDH, lactate dehydrogenase




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