Abstract
Lyme 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.
Original language | English |
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Pages (from-to) | 257-267 |
Number of pages | 11 |
Journal | International Journal of Medical Microbiology |
Volume | 298 |
Issue number | SUPPL. 1 |
DOIs | |
State | Published - Sep 1 2008 |
Bibliographical note
Funding Information:Research on Erp proteins by our laboratory is funded by US National Institutes of Health Grant R01-AI44245. We thank our many colleagues around the world for their helpful scientific discussions and debates.
Keywords
- Adhesin
- Borrelia burgdorferi
- Complement
- Factor H
- Laminin
- Outer surface protein
ASJC Scopus subject areas
- Microbiology
- Microbiology (medical)
- Infectious Diseases