preprints.org > biology and life sciences > biochemistry and molecular biology > doi: 10.20944/preprints202406.1233.v1

Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

Version 1 : Received: 17 June 2024 / Approved: 18 June 2024 / Online: 18 June 2024 (13:35:41 CEST)

The key factor that enables pathogenic bacteria to establish successful infections lies largely in their ability to escape the host's immune response and adhere to host surfaces. Vitronectin (Vn) is a multi-domain glycoprotein ubiquitously present in blood and extracellular matrix of several tissues, where it plays important roles as regulator of membrane attack complex (MAC) formation and as mediator of cell adhesion. Vn has emerged as intriguing target for several microorganisms. Vn-binding by bacterial receptors confers protection from lysis resulting from MAC deposition. Furthermore, through its Arg-Gly-Asp (RGD) motif, Vn can bind several host cell integrins. Therefore, Vn recruited to the bacterial cell functions as a molecular bridge between bacteria and host surfaces, where it triggers several host signalling events that could promote bacterial internalisation. Each bacterium uses different receptors that recognise specific Vn-domains. In this review, we update the current knowledge of Vn receptors of major bacterial pathogens, emphasising the role they may play in the host upon Vn-binding. Focusing on the structural properties of bacterial proteins, we provide details on the residues involved in their interaction with Vn. Furthermore, we discuss the possible involvement of Vn adsorption on biomaterials in promoting bacterial adhesion on abiotic surfaces.

Vitronectin; bacterial surface proteins; bacterial-host interaction; bacterial adhesion; bacterial immune evasion; human ligands

Biology and Life Sciences, Biochemistry and Molecular Biology

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