Borrelia burgdorferi resistance to a major skin antimicrobial peptide is independent of outer surface lipoprotein content.
We hypothesize a potential role for Borrelia burgdorferi OspC in innate immune evasion at the initial stage of mammalian infection. We demonstrate that B. burgdorferi is resistant to high levels (>200 microg/ml) of cathelicidin and that this antimicrobial peptide exhibits limited binding to the spirochetal outer membrane, irrespective of OspC or other abundant surface lipoproteins. We conclude that the essential role of OspC is unrelated to resistance to this component of innate immunity.
Sarkar
Amit
A
Laboratory of Zoonotic Pathogens, Rocky Mountain Laboratories, NIAID, NIH, 903 S. 4th Street, Hamilton, MT 59840, USA. sarkara@niaid.nih.gov
Tilly
Kit
K
Stewart
Philip
P
Bestor
Aaron
A
Battisti
James M
JM
Rosa
Patricia A
PA
D000890:Anti-Infective Agents / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology*; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000502:physiology*; D025065:Borrelia burgdorferi / Q000187:drug effects* / Q000235:genetics; D024881:Drug Resistance, Bacterial / Q000235:genetics; D007113:Immunity, Innate / Q000235:genetics; D008074:Lipoproteins / Q000235:genetics / Q000502:physiology*; D054804:Cathelicidins
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D001425:Bacterial Outer Membrane Proteins; D008074:Lipoproteins; D054804:Cathelicidins