Bacterial adhesion to animal tissues: protein determinants for recognition of extracellular matrix components

Abstract

SummaryThe extracellular matrix (ECM) is present within all animal tissues and organs. Actually, it surrounds the eukaryotic cells composing the four basic tissue types, i.e. epithelial, muscle, nerve and connective. ECM does not solely refer to connective tissue but composes all tissues where its composition, structure and organization vary from one tissue to another. Constituted of the four main fibrous proteins, i.e. collagen, fibronectin, laminin and elastin, ECM components form a highly structured and functional network via specific interactions. From the basement membrane to interstitial matrix, further heterogeneity exists in the organization of the ECM in various tissues and organs also depending on their physiological state. Back to a molecular level, bacterial proteins represent the most significant part of the microbial surface components recognizing adhesive matrix molecules (MSCRAMM). These cell surface proteins are secreted and localized differently in monoderm and diderm-LPS bacteria. While one collagenbinding domain (CBD) and different fibronectinbinding domains (FBD1 to 8) have been registered in databases, much remains to be learned on specific binding to other ECM proteins via single or supramolecular protein structures. Besides the interaction of bacterial proteins with individual ECM components, this review aims at stressing the importance of fully considering the ECM at supramolecular, cellular, tissue and organ levels. This conceptual view should not be overlooked to rigorously comprehend the physiology of bacterial interaction from commensal to pathogenic species.

Borrelia burgdorferi Protein BBK32 Binds to Soluble Fibronectin via the N-terminal 70-kDa Region, Causing Fibronectin to Undergo Conformational Extension

“…FN was purified from a fibrinogen-rich plasma fraction by heat precipitation (60°C, 5 min) of the fibrinogen followed by chromatography (26). Expression and purification of polyhistidine-tagged monomeric [1][2][3][4][5] FNI, N-3 FNIII, [6][7][8][9] FNI, [7][8][9] FNI, 7 FNI-1 FNIII, [1][2][3][4][5][6][7][8][9][10][11][12][13][14] FNIII, and 2-14 FNIII and dimeric 6 FNI-C, 1 FNIII-C, and 2 FNIII-C were accomplished using recombinant baculovirus and affinity chromatography as described previously (27)(28)(29). Expression and purification of unlabeled [2][3] FNI and 8 -9 FNI, and of uniformly 15 N-labeled 8 -9 FNI, were performed as described previously (13,17).…”

“…Bacterial virulence factors contribute to the invasion and, ultimately, colonization of a host (6). Although patterns of bacterial virulence are organism-and disease-specific, many pathogens utilize FN to adhere to mammalian cells and tissues (7,8); in some cases FN binding results in invasion (9 -11).…”

Temporal upregulation of host surface receptors provides a window of opportunity for bacterial adhesion and disease

“…The ECM, the acellular proteinaceous part of animal connective tissue, provides the anchoring platform for epithelia and also surrounds blood capillaries and neurons [6]. It consists of collagen, elastin, fibrillin, laminin, fibronectin, vitronectin, thrombospondin, proteoglycans and hyaluronic acid.…”

Characterization of DIP0733, a multi-functional virulence factor of Corynebacterium diphtheriae

“…Pathogenic bacteria developed so-called MSCRAMMs, which interact with these proteins (Chagnot et al, 2012). Also for Cor.…”