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The actin-based motility defect of a Shigella flexneri rmlD rough LPS mutant is not due to loss of IcsA polarity.

Authors
  • Van den Bosch, Luisa
  • Morona, Renato
Type
Published Article
Journal
Microbial pathogenesis
Publication Date
Jul 01, 2003
Volume
35
Issue
1
Pages
11–18
Identifiers
PMID: 12860454
Source
Medline
License
Unknown

Abstract

Shigella flexneri requires the outer membrane protein IcsA(VirG) and lipopolysaccharide (LPS) for efficient actin-based motility (ABM) within mammalian cells which is essential for virulence. Wild type strains of S. flexneri 2a such as 2457T have smooth LPS whose O antigen (Oag) chains have two modal lengths and IcsA predominantly located at one pole on their cell surface. In contrast, rough LPS mutants lack Oag chains, have IcsA on lateral and polar regions of the cell surface, and are defective for ABM. In this study we directly compared the phenotype of a S. flexneri producing non-IcsP/SopA cleavable IcsA (IcsA*) with that of a rough LPS mutant. IcsA* was located on lateral and polar regions of smooth LPS bacteria, and was fully functional in ABM assays (HeLa cell monolayer plaque and F-actin comet tail formation) which contrasts with the R-LPS phenotype. This indicates that loss of polar IcsA localisation in R-LPS mutants is unrelated to their ABM defect, and suggests that Oag may directly contribute to IcsA-mediated ABM.

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