HtrA chaperone activity contributes to host cell binding in Campylobacter jejuni

TY - JOUR

T1 - HtrA chaperone activity contributes to host cell binding in Campylobacter jejuni

AU - Bæk, Kristoffer Torbjørn

AU - Vegge, Christina Skovgaard

AU - Brøndsted, Lone

PY - 2011

Y1 - 2011

N2 - Background: Acute gastroenteritis caused by the food-borne pathogen Campylobacter jejuni is associated with attachment of bacteria to the intestinal epithelium and subsequent invasion of epithelial cells. In C. jejuni, the periplasmic protein HtrA is required for efficient binding to epithelial cells. HtrA has both protease and chaperone activity, and is important for virulence of several bacterial pathogens. Results: The aim of this study was to determine the role of the dual activities of HtrA in host cell interaction of C. jejuni by comparing an htrA mutant lacking protease activity, but retaining chaperone activity, with a htrA mutant and the wild type strain. Binding of C. jejuni to both epithelial cells and macrophages was facilitated mainly by HtrA chaperone activity that may be involved in folding of outer membrane adhesins. In contrast, HtrA protease activity played only a minor role in interaction with host cells. Conclusion: We show that HtrA protease and chaperone activities contribute differently to C. jejuni's interaction with mammalian host cells, with the chaperone activity playing the major role in host cell binding.

AB - Background: Acute gastroenteritis caused by the food-borne pathogen Campylobacter jejuni is associated with attachment of bacteria to the intestinal epithelium and subsequent invasion of epithelial cells. In C. jejuni, the periplasmic protein HtrA is required for efficient binding to epithelial cells. HtrA has both protease and chaperone activity, and is important for virulence of several bacterial pathogens. Results: The aim of this study was to determine the role of the dual activities of HtrA in host cell interaction of C. jejuni by comparing an htrA mutant lacking protease activity, but retaining chaperone activity, with a htrA mutant and the wild type strain. Binding of C. jejuni to both epithelial cells and macrophages was facilitated mainly by HtrA chaperone activity that may be involved in folding of outer membrane adhesins. In contrast, HtrA protease activity played only a minor role in interaction with host cells. Conclusion: We show that HtrA protease and chaperone activities contribute differently to C. jejuni's interaction with mammalian host cells, with the chaperone activity playing the major role in host cell binding.

KW - Former LIFE faculty

KW - HtrA

KW - chaperone

KW - protease

KW - Campylobacter jejuni

KW - INT-407

KW - Phagocytosis

KW - Virulence

U2 - 10.1186/1757-4749-3-13

DO - 10.1186/1757-4749-3-13

M3 - Journal article

SN - 1757-4749

VL - 3

JO - Gut Pathogens

JF - Gut Pathogens

IS - 13

ER -