Ontology highlight
ABSTRACT:
SUBMITTER: Yang XF
PROVIDER: S-EPMC2213294 | biostudies-literature | 2004 Mar
REPOSITORIES: biostudies-literature
Yang Xiaofeng F XF Pal Utpal U Alani Sophie M SM Fikrig Erol E Norgard Michael V MV
The Journal of experimental medicine 20040223 5
The molecular basis of how Borrelia burgdorferi (Bb), the Lyme disease spirochete, maintains itself in nature via a complex life cycle in ticks and mammals is poorly understood. Outer surface (lipo)protein A (OspA) of Bb has been the most intensively studied of all borrelial molecular constituents, and hence, much has been speculated about the potential role(s) of OspA in the life cycle of Bb. However, the precise function of OspA (along with that of its close relative and operonic partner, oute ...[more]