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Lyme borreliosis spirochete Erp proteins, their known host ligands, and potential roles in mammalian infection Brissette CA; Cooley AE; Burns LH; Riley SP; Verma A; Woodman ME; Bykowski T; Stevenson BInt J Med Microbiol 2008[Sep]; 298 Suppl 1 (Suppl 1): 257-67Lyme borreliae naturally maintain numerous distinct DNA elements of the cp32 family, each of which carries a mono- or bicistronic erp locus. The encoded Erp proteins are surface-exposed outer membrane lipoproteins that are produced at high levels during mammalian infection but largely repressed during colonization of vector ticks. Recent studies have revealed that some Erp proteins can serve as bacterial adhesins, binding host proteins such as the complement regulator factor H and the extracellular matrix component laminin. These results suggest that Erp proteins play roles in multiple aspects of mammalian infection.|*Host-Pathogen Interactions[MESH]|Animals[MESH]|Bacterial Outer Membrane Proteins/*metabolism[MESH]|Borrelia burgdorferi/metabolism/*pathogenicity[MESH]|Complement Factor H/*metabolism[MESH]|Humans[MESH]|Laminin/*metabolism[MESH]|Ligands[MESH]|Lipoproteins/*metabolism[MESH]|Lyme Disease/microbiology[MESH] |
