期刊
JOURNAL OF EXPERIMENTAL MEDICINE
卷 199, 期 5, 页码 641-648出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1084/jem.20031960
关键词
Lyme disease; OspA; lipoprotein; arthropod vector; Borrelia burgdorferi
资金
- NIAID NIH HHS [AI-49200, R01 AI032947, R37 AI049200, R01 AI049200, R01 AI045538, AI-45538, AI-32947] Funding Source: Medline
- NIAMS NIH HHS [R03 AR047640, R03-AR-47640] Funding Source: Medline
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 surf-ice (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, outer surface [lipo]protein B [OspB]) heretofore has not been directly determined, due primarily to the inability to generate an OspA/B-deficient mutant from a virulent strain of Bb. In this study, we created an OspA/B-deficient mutant of an infectious human isolate of Bb (strain 297) and found that OspA/B function was not required for either Bb infection of mice or accompanying tissue pathology. However, OspA/B function was essential for Bb colonization of and survival within tick midguts, events crucial for sustaining Bb in its natural enzootic life cycle.
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