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Collagen-binding adhesins

Nummelin, H., Merckel, M. C., Leo, J. C., Lankinen, H., Skurnik, M., and Goldman, A. (2004). The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll. EMBOJ. 23, 701-711. [Pg.95]

At least some adhesins bind to more than one receptor. Intimin might not only bind to Tir but also to pi containing integrins as well as to nucleolin [65], The Dr adhesin recognizes not just the short consensus repeat domain as all members of the Dr family of adhesins but also type IV collagen, which is a critical step in renal persistence [66],... [Pg.117]

The lipase GehD is secreted by S. epidermidis and specifically binds collagen [59], Like AtlE, it displays not only enzymatic activity but also functions as an adhesin. The factor(s) responsible for S. epidermidis binding to thrombospondin have yet to be identified. [Pg.161]

The extracellular domains of integrins interact with a variety of profeins of the extracellular matrix. These include fibronectin, fibrinogen, vifronecfin, collagen, and entacfin. Other large cell surface adhesins include laminin and osteopontin (Chapfer 8), thrombospondin, von Willebrand factor, and related proteins. These adhesins appear to depend upon the sequence Arg-Gly-Asp (RGD), which binds nonco-valently to integrins, which act as cell-surface receptors. See also Chapter 12, Section C,9. [Pg.971]


See other pages where Collagen-binding adhesins is mentioned: [Pg.95]    [Pg.170]    [Pg.109]    [Pg.511]    [Pg.1884]    [Pg.48]    [Pg.114]    [Pg.160]    [Pg.161]    [Pg.950]   
See also in sourсe #XX -- [ Pg.113 , Pg.115 , Pg.117 ]




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