Journal of Cell Science, Vol 114, Issue 1 21-28, Copyright © 2001 by Company of Biologists

JOURNAL ARTICLES

Subversion of integrins by enteropathogenic Yersinia

RR Isberg and P Barnes
Howard Hughes Medical Institute and Dept Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA. ralph.isberg@tufts.edu

Enteropathogenic Yersinia are gram-negative bacterial species that translocate from the lumen of the intestine and are able to grow within deep tissue sites. During the earliest stages of disease, the organism is able to bind integrin receptors that are presented on the apical surface of M cells in the intestine, which allows its internalization and subsequent translocation into regional lymph nodes. The primary integrin substrate is the outer-membrane protein invasin, which binds with extraordinarily high affinity to at least five different integrins that have the (beta)(1) chain. Bacterial uptake into host cells is modulated by the affinity of receptor-substrate interaction, receptor concentration and the ability of the substrate to aggregate target receptors.

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