Open AccessSelective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO
Author(s) -
Evans Lewis D.B.,
Hughes Colin
Publication year - 2009
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2009.01535.x
Subject(s) - chaperone (clinical) , virulence , flagellum , effector , microbiology and biotechnology , secretion , biology , translocon , type three secretion system , transport protein , membrane protein , bacteria , biochemistry , genetics , gene , membrane , medicine , pathology
Bacteria secrete flagella subunits and deliver virulence effectors via type III export systems. During flagellar filament assembly, a chaperone escort mechanism has been proposed to enhance the export of early, minor flagellar filament components by selectively binding and cycling their chaperones. Here we identify virulence orthologues of the flagellar chaperone escort FliJ and show that the orthologues Salmonella InvI and Yersinia YscO are, like FliJ, essential for their type III export pathway and similarly, do not bind export substrates. Like FliJ, they recognize a subset of export chaperones, in particular those of the host membrane translocon components required for subsequent effector delivery.