Lyme borreliosis spirochete Erp proteins, their known host ligands, and potential roles in mammalian infection.

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.

• Authors: Catherine A Brissette, Anne E Cooley, Logan H Burns, Sean P Riley, Ashutosh Verma, Michael E Woodman, Tomasz Bykowski, Brian Stevenson
• Journal: International journal of medical microbiology : IJMM (Int J Med Microbiol) Vol. 298 Suppl 1 Pg. 257-67 (Sep 01 2008) ISSN: 1618-0607 [Electronic] Germany
• PMID: 18248770 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Review)

Chemical References

• Bacterial Outer Membrane Proteins
• Laminin
• Ligands
• Lipoproteins
• Complement Factor H

Topics

• Animals
• Bacterial Outer Membrane Proteins (metabolism)
• Borrelia burgdorferi (metabolism, pathogenicity)
• Complement Factor H (metabolism)
• Host-Pathogen Interactions
• Humans
• Laminin (metabolism)
• Ligands
• Lipoproteins (metabolism)
• Lyme Disease (microbiology)