TY - JOUR
T1 - Diverse Lyme disease spirochetes bind integrin α(IIb)β3 on human platelets
AU - Coburn, J.
AU - Barthold, Stephen W
AU - Leong, J. M.
PY - 1994
Y1 - 1994
N2 - Lyme disease is a chronic, multisystemic infection caused by Borrelia burgdorferi sensu lato. An infectious strain of B. burgdorferi was previously shown to bind to human platelets via the integrin α(IIb)β3. In this study, a diverse group of Lyme disease spirochetes was tested for platelet- and α(IIb)β3-binding activity. This collection included representatives of each of the three species that cause Lyme disease, B. burgdorferi (sensu stricto). B. garinii, and B. afzelii. Strains were characterized for infectivity in mouse models or were low-passage isolates from human patients. Each of the 11 infectious strains bound to platelets immobilized in microtiter wells and in suspension. Binding to platelets in suspension was specifically inhibited by a blocking anti-α(IIb)β3 antibody, and representatives of each species bound to purified α(IIb)β3. The strains that did not bind α(IIb)β3 or platelets were all noninfectious. No obvious relationship was observed between binding to platelets and expression of the bacterial outer surface protein OspA, OspB, or OspC, as assessed by immunoblotting. These results demonstrate that integrin α(IIb)β3-binding activity is widespread among the Borrelia species that cause Lyme disease and are consistent with a role for α(IIb)β3 binding in the transmission and/or pathogenesis of Lyme disease.
AB - Lyme disease is a chronic, multisystemic infection caused by Borrelia burgdorferi sensu lato. An infectious strain of B. burgdorferi was previously shown to bind to human platelets via the integrin α(IIb)β3. In this study, a diverse group of Lyme disease spirochetes was tested for platelet- and α(IIb)β3-binding activity. This collection included representatives of each of the three species that cause Lyme disease, B. burgdorferi (sensu stricto). B. garinii, and B. afzelii. Strains were characterized for infectivity in mouse models or were low-passage isolates from human patients. Each of the 11 infectious strains bound to platelets immobilized in microtiter wells and in suspension. Binding to platelets in suspension was specifically inhibited by a blocking anti-α(IIb)β3 antibody, and representatives of each species bound to purified α(IIb)β3. The strains that did not bind α(IIb)β3 or platelets were all noninfectious. No obvious relationship was observed between binding to platelets and expression of the bacterial outer surface protein OspA, OspB, or OspC, as assessed by immunoblotting. These results demonstrate that integrin α(IIb)β3-binding activity is widespread among the Borrelia species that cause Lyme disease and are consistent with a role for α(IIb)β3 binding in the transmission and/or pathogenesis of Lyme disease.
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M3 - Article
C2 - 7525486
AN - SCOPUS:0028062089
VL - 62
SP - 5559
EP - 5567
JO - Infection and Immunity
JF - Infection and Immunity
SN - 0019-9567
IS - 12
ER -