Analysis of Borrelia burgdorferi Surface Proteins as Determinants in
Establishing Host Cell Interactions.
Schmit VL, Patton TG, Gilmore RD Jr
Front Microbiol 2011 07; 2 : 141
Borrelia burgdorferi infection causes Lyme borreliosis in humans, a
condition which can involve a systemic spread of the organism to
colonize various tissues and organs. If the infection is left untreated
by antimicrobials, it can lead to manifestations including, arthritis,
carditis, and/or neurological problems. Identification and
characterization of B. burgdorferi outer membrane proteins that
facilitate cellular attachment and invasion to establish infection
continue to be investigated. In this study, we sought to further define
putative cell binding properties of surface-exposed B. burgdorferi
proteins by observing whether cellular adherence could be blocked by
antibodies. B. burgdorferi mixed separately with monoclonal antibodies
(mAbs) against outer surface protein (Osp) A, OspC, decorin-binding
protein (Dbp) A, BBA64, and RevA antigens were incubated with human
umbilical vein endothelial cells (HUVEC) and human neuroglial cells
(H4). B. burgdorferi treated with anti- OspA, -DbpA, and -BBA64 mAbs
showed a significant decrease in cellular association compared to
controls, whereas B. burgdorferi treated with anti-OspC and anti-RevA
showed no reduction in cellular attachment. Additionally, temporal
transcriptional analyses revealed upregulated expression of bba64, ospA,
and dbpA during coincubation with cells. Together, the data provide
evidence that OspA, DbpA, and BBA64 function in host cell adherence and
infection mechanisms.
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