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Bacterial collagen-binding proteins are surface-expressed adhesins found in numerous Gram-positive pathogens (e.g., *Streptococcus* spp., *Staphylococcus aureus*, *Arcanobacterium pyogenes*, *Enterococcus* spp.), and also certain Gram-negative bacteria. They typically contain specialized domains (such as von Willebrand factor type A (vWA) domains or T-shaped helical bundles) that recognize and bind with high specificity and affinity to the triple-helical structure of host collagen fibers[1][3][4][5][6][7]. This interaction promotes bacterial attachment to tissues rich in collagen (e.g., heart valves, joints, skin), enabling colonization, biofilm formation, and evasion of host immunity, and often contributes to the pathogenesis of infections such as endocarditis and soft tissue infections[4][5][6]. Collagen-binding proteins are considered attractive targets for new therapies aimed at inhibiting bacterial colonization and virulence rather than directly killing bacteria[4][5]. Individual proteins in this family, such as CbpA (*Arcanobacterium pyogenes*), CNA (*Staphylococcus aureus*), and various MSCRAMMs, have been structurally and functionally characterized; antibodies against these adhesins can block their function, offering a potential avenue for antivirulence therapy[4][7]. Note: “Bacterial collagen-binding protein” is a family designation; for specific drug targeting or biomarker use, individual protein identities (e.g., CNA, CbpA) are often required.
Competitive inhibition of collagen binding (by antibodies or peptides); Disruption of bacterial adhesion
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