Infection and Immunity, August 2000, p. 4637-4646, Vol. 68, No. 8
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
from Enterohemorrhagic
Escherichia coli in Citrobacter
rodentium

Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AZ,1 Department of Paediatric Gastroenterology, St. Bartholomew's and the Royal London School of Medicine and Dentistry, St. Bartholomew's Hospital, London EC1A 7BE,2 and University Department of Paediatric Gastroenterology, Royal Free Hospital, London NW3 2QG,3 United Kingdom
Received 10 February 2000/Returned for modification 18 April 2000/Accepted 17 May 2000
The carboxy-terminal 280 amino acids (Int280) of the bacterial
adhesion molecule intimin include the receptor-binding
domain. At least five different types of Int280, designated
,
,
,
, and
, have been described based on sequence variation in
this region. Importantly, the intimin types are associated with
different evolutionary branches and contribute to distinct
tissue tropism of intimin-positive bacterial pathogens. In this study
we engineered a strain of Citrobacter rodentium, which
normally displays intimin
, to express intimin
from
enterohemorrhagic Escherichia coli. We show that intimin
binds to the translocated intimin receptor (Tir) from C. rodentium and has the ability to produce attaching and effacing
lesions on HEp-2 cells. However, C. rodentium
expressing intimin
could not colonize orally infected mice or
induce mouse colonic hyperplasia. These results suggest that intimin
may contribute to host specificity, possibly through its interaction
with a receptor on the host cell surface.
Present address: Institute of Microbiology and Genetics, University
of Vienna, A-1030 Vienna, Austria.
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