» Articles » PMID: 10085058

Beta1-chain Integrins Are Not Essential for Intimin-mediated Host Cell Attachment and Enteropathogenic Escherichia Coli-induced Actin Condensation

Overview
Journal Infect Immun
Date 1999 Mar 20
PMID 10085058
Citations 13
Authors
Affiliations
Soon will be listed here.
Abstract

Intimin is a bacterial outer membrane protein required for intimate attachment of enterohemorrhagic and enteropathogenic Escherichia coli (EHEC and EPEC) to mammalian cells. beta1-chain integrins have been proposed as candidate receptors for intimin. We found that binding of mammalian cells to immobilized intimin was not detectable unless mammalian cells were preinfected with EPEC or EHEC. beta1-chain integrin antagonists or inactivation of the gene encoding the beta1-chain did not affect binding of preinfected mammalian cells to intimin or the actin condensation associated with the attachment of EPEC. The results indicate that beta1-chain integrins are not essential for intimin-mediated cell attachment or EPEC-mediated actin polymerization.

Citing Articles

Staying out or Going in? The Interplay between Type 3 and Type 5 Secretion Systems in Adhesion and Invasion of Enterobacterial Pathogens.

Whelan R, McVicker G, Leo J Int J Mol Sci. 2020; 21(11).

PMID: 32521829 PMC: 7312957. DOI: 10.3390/ijms21114102.


EHEC Adhesins.

McWilliams B, Torres A Microbiol Spectr. 2015; 2(2):EHEC00032013.

PMID: 25635238 PMC: 4307604. DOI: 10.1128/microbiolspec.EHEC-0003-2013.


Actin pedestal formation by enterohemorrhagic Escherichia coli enhances bacterial host cell attachment and concomitant type III translocation.

Battle S, Brady M, Vanaja S, Leong J, Hecht G Infect Immun. 2014; 82(9):3713-22.

PMID: 24958711 PMC: 4187837. DOI: 10.1128/IAI.01523-13.


Enhanced Actin Pedestal Formation by Enterohemorrhagic Escherichia coli O157:H7 Adapted to the Mammalian Host.

Brady M, Radhakrishnan P, Liu H, Magoun L, Murphy K, Mukherjee J Front Microbiol. 2011; 2:226.

PMID: 22102844 PMC: 3219212. DOI: 10.3389/fmicb.2011.00226.


Synapses: sites of cell recognition, adhesion, and functional specification.

Yamada S, Nelson W Annu Rev Biochem. 2007; 76:267-94.

PMID: 17506641 PMC: 3368613. DOI: 10.1146/annurev.biochem.75.103004.142811.


References
1.
Isberg R, Voorhis D, Falkow S . Identification of invasin: a protein that allows enteric bacteria to penetrate cultured mammalian cells. Cell. 1987; 50(5):769-78. DOI: 10.1016/0092-8674(87)90335-7. View

2.
Deibel C, Kramer S, Chakraborty T, Ebel F . EspE, a novel secreted protein of attaching and effacing bacteria, is directly translocated into infected host cells, where it appears as a tyrosine-phosphorylated 90 kDa protein. Mol Microbiol. 1998; 28(3):463-74. DOI: 10.1046/j.1365-2958.1998.00798.x. View

3.
Isberg R, Leong J . Multiple beta 1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells. Cell. 1990; 60(5):861-71. DOI: 10.1016/0092-8674(90)90099-z. View

4.
Leong J, Fournier R, Isberg R . Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein. EMBO J. 1990; 9(6):1979-89. PMC: 551907. DOI: 10.1002/j.1460-2075.1990.tb08326.x. View

5.
Jerse A, Yu J, Tall B, Kaper J . A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells. Proc Natl Acad Sci U S A. 1990; 87(20):7839-43. PMC: 54845. DOI: 10.1073/pnas.87.20.7839. View