Abstract
Collagens are the primary structural components of mammalian extracellular matrices. In addition, collagens regulate tissue development, regeneration and host defense through interaction with specific cellular receptors. Their unique triple helix structure, which requires a glycine residue every third amino acid, is the defining structural feature of collagens. There are 28 genetically distinct collagens in humans. In addition, several other unrelated human proteins contain a collagen domain. Gram-positive bacteria of the genera Staphylococcus, Streptococcus, Enterococcus, and Bacillus express cell surface proteins that bind to collagen. These proteins of Gram-positive pathogens are modular proteins that can be classified into different structural families. This review will focus on the different structural families of collagen binding proteins of Gram-positive pathogen. We will describe how these proteins interact with the triple helix in collagens and other host proteins containing a collagenous domain and discuss how these interactions can contribute to the pathogenic processes.
Highlights
Collagen is the most abundant protein in the human body and an integral component of the extracellular matrix (ECM) (Shoulders and Raines, 2009)
We have identified three emerging families of collagen-binding proteins where, one or more than one family member binds to collagen, a clear picture of how these proteins bind to collagen is not yet available
Gram-positive pathogens utilize their interactions with the ECM for tissue colonization and to establish infections in the host
Summary
Collagen is the most abundant protein in the human body and an integral component of the extracellular matrix (ECM) (Shoulders and Raines, 2009). All members of the CNA-like MSCRAMM family appear to bind collagen by a collagen hug mechanism, the proteins show differences in affinity (Table 2) and mechanistic details because of structural variations.
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