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Bacterial collagen-binding surface proteins are a specialized class of adhesins, primarily belonging to the Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMM) family, that facilitate the attachment of pathogens to host extracellular matrix components (Speziale et al., 2009, PubMed: 19193271). Prominent examples include the Cna protein of Staphylococcus aureus and the Ace protein of Enterococcus faecalis, which utilize a unique 'collagen hug' mechanism to wrap around and sequester collagen triple helices (Zong et al., 2005, PubMed: 16151463). These proteins are critical virulence factors that enable bacteria to colonize collagen-rich tissues such as heart valves, bone, and cartilage, leading to serious conditions like infective endocarditis, osteomyelitis, and septic arthritis (Nallapareddy et al., 2000, PubMed: 10931141). By mediating the initial stages of infection and promoting biofilm formation, these surface proteins protect bacteria from host immune responses and antibiotic penetration (Herman-Bausier et al., 2016, PubMed: 27551074). As therapeutic targets, they are being investigated for the development of anti-adhesion drugs, monoclonal antibodies, and prophylactic vaccines aimed at preventing the establishment of infection in high-risk patients.
Inhibition of bacterial attachment to host collagen fibers by blocking the MSCRAMM binding domain, thereby preventing tissue colonization and biofilm formation.
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