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• W764522318 abstract "Bacteria express surface-associated adhesion molecules, generally termed adhesins, recognize the eukaryotic cell surface, the extracellular matrix (ECM) protein, or carbohydrate structures. The major structural components of the eukaryotic ECM are collagens that form different types of interstitial or basement membrane networks, including fibril-forming collagens (types I, II, and III) and the two-dimensional collagen type IV network. Due to the tight association of other adhesion proteins, such as fibronectin, vitronectin, von Willebrand factor, laminin, nidogen, and proteoglycans with collagens to form supramolecular aggregates of variable structure and composition, the interaction with host cells or bacteria is not determined solely by the collagen component. Although most characterized interactions with gram-negative bacteria involve recognition of lectins and carbohydrate structures in the host tissue, several types of fimbriae of enterobacteria exhibit specific interactions with fibronectin, laminin, or other adhesion proteins. Importantly, thrombospondin binds Plasmodium falciparum-parasitized erythrocytes and, together with its cell surface receptor, CD36, mediates their adherence to endothelial and other cells. Chlamydia trachomatis expresses a heparan sulfate-like glycan that links the bacterium to host cell heparin-binding proteins, thereby using a trimolecular complex for adherence and invasion. Finally, the epithelial-cell mucosal barriers in the body provide different high-molecular weight mucin glycoproteins (containing 50 to 80% carbohydrate) which exhibit considerable genetic polymorphism among individuals." @default.
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• W764522318 date "2014-04-30" @default.
• W764522318 modified "2023-09-24" @default.
• W764522318 title "Extracellular Matrix and Host Cell Surfaces: Potential Sites of Pathogen Interaction" @default.
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• W764522318 doi "https://doi.org/10.1128/9781555817633.ch4" @default.
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