The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG

Simon Daefler, Marjorie Russel

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94 Scopus citations

Abstract

The secretion of pathogenecity factors by Salmonella typhimurium is mediated by a type III secretion system that includes an outer membrane protein of the secretin family. Related secretins are also required for f1 phage assembly and type II secretion. When the C-terminal 43 amino acids of the S. typhimurium secretin InvG are added to f1 pIV, the chimeric f1 pIV- InvG43 protein becomes dependent on the co-expression of another gene, InvH, for function in phage assembly. [3H]-palmitic acid labelling, globomycin sensitivity and density gradient flotation were used to demonstrate that InvH is an outer membrane lipoprotein that is processed by signal peptidase II. A complex between chimeric f1 pIV-'InvG43 and InvH was demonstrated in vivo. InvH was shown to be required for the proper localization of InvG in the outer membrane and for the secretion of the virulence factor SipC. These results suggest that InvH and InvG are part of the functional outer membrane translocation complex in type III secretion systems.

Original languageEnglish
Pages (from-to)1367-1380
Number of pages14
JournalMolecular Microbiology
Volume28
Issue number6
DOIs
StatePublished - 1998
Externally publishedYes

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