By Michael Wilson
Adhesion is the the most important first degree in any infectious affliction. it really is for that reason very important to completely comprehend the mechanisms underlying bacterial adhesion in order that we are able to enhance equipment of conserving our basic (protective) microflora, and of forestalling pathogenic micro organism from starting up an infectious procedure. This e-book describes the bacterial constructions liable for adhesion and the molecular mechanisms underlying the adhesion method. a distinct characteristic is that it additionally bargains with the implications of adhesion for either the adherent bacterium and the host cell/tissue to which it has adhered.
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Additional resources for Bacterial Adhesion to Host Tissues: Mechanisms and Consequences (Advances in Molecular and Cellular Microbiology)
The Yersinia protein invasin possesses features that enable it to interact with several ␤1 integrins with aªnity that is higher than that of the natural ligand, allowing eªcient competition with extracellular matrix proteins to which ␤1 integrins may be engaged. The result is ‘zippering’ – a process by which the host cell forms a series of contacts over the surface of the microbe leading to uptake (Isberg, 1991; Isberg and Tran Van Nhieu, 1994). , 1990). Additionally, receptor clustering achieved by cross-linking of ligands was also a requirement for the signal leading to uptake (Isberg and Tran Van Nhieu, 1994).
Of the four domains (loops 1–4) predicted to be exposed on the bacterial surface, only loop 4 (the most proximal to the C-terminus) is conserved. 5). Opa proteins undergo antigenic and phase variation at a high frequency. , 1986). , 1991). Opc is phase variable but structurally it is largely invariant. , 1995a), which suggests that pili are selected for in vivo. , 1983). , 2000). One consequence of pilus-mediated adhesion to endothelial cells is increased cellular damage, which is mediated primarily by LPS (Fig.
It can be quantitatively released from cells by treatment with LiCl and is thus not covalently anchored. The Map protein comprises six repeats of a 110 amino acid residue motif with a central portion composed of a subdomain with high homology to the peptide-binding groove of mammalian major histocompatibility complex class II (MHCII) molecules. Map is capable of interacting with a variety of proteins and peptides, including many ECM proteins of the host. , 1999). , 1981). Bioﬁlms comprise multiple layers of cells embedded in an amorphous extracellular glycocalyx.