Subversion of integrins by enteropathogenic Yersinia
Open Access
- 1 January 2001
- journal article
- review article
- Published by The Company of Biologists in Journal of Cell Science
- Vol. 114 (1) , 21-28
- https://doi.org/10.1242/jcs.114.1.21
Abstract
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.Keywords
This publication has 76 references indexed in Scilit:
- Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification of eight NSVAIG – S motifs in the amino‐terminal half of the protein involved in collagen bindingMolecular Microbiology, 2000
- Defining Fibronectin's Cell Adhesion Synergy Site by Site-Directed MutagenesisThe Journal of cell biology, 2000
- Solution structure and dynamics of linked cell attachment modules of mouse fibronectin containing the RGD and synergy regions: comparison with the human fibronectin crystal structureJournal of Molecular Biology, 1998
- Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificityJournal of Molecular Biology, 1997
- A Region of the Invasin Protein That Contributes to High Affinity Binding to Integrin ReceptorsPublished by Elsevier ,1996
- Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes.Journal of Clinical Investigation, 1996
- 2.0 Å Crystal Structure of a Four-Domain Segment of Human Fibronectin Encompassing the RGD Loop and Synergy RegionCell, 1996
- Cooperative signaling by alpha 5 beta 1 and alpha 4 beta 1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin.The Journal of cell biology, 1995
- Bordetella pertussis filamentous hemagglutinin interacts with a leukocyte signal transduction complex and stimulates bacterial adherence to monocyte CR3 (CD11b/CD18).The Journal of Experimental Medicine, 1994
- A point mutation of integrin beta 1 subunit blocks binding of alpha 5 beta 1 to fibronectin and invasin but not recruitment to adhesion plaques.The Journal of cell biology, 1992