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Journal of Clinical Microbiology, January 2000, p. 382-388, Vol. 38, No. 1
Laboratory of Human Bacterial Pathogenesis,
Rocky Mountain Laboratories, National Institute of Allergy and
Infectious Diseases, National Institutes of Health, Hamilton, Montana
59840,1 and Division of Vector-Borne
Infectious Diseases, National Center for Infectious Diseases, Centers
for Disease Control and Prevention, Fort Collins, Colorado
805222
Received 12 July 1999/Returned for modification 14 September
1999/Accepted 5 October 1999
The Lyme disease-associated spirochete, Borrelia
burgdorferi, is maintained in enzootic cycles involving
Ixodes ticks and small mammals. Previous studies
demonstrated that B. burgdorferi expresses outer surface
protein A (OspA) but not OspC when residing in the midgut of unfed
ticks. However, after ticks feed on blood, some spirochetes stop making
OspA and express OspC. Our current work examined the timing and
frequency of OspA and OspC expression by B. burgdorferi in
infected Ixodes scapularis nymphs as they fed on uninfected
mice and in uninfected I. scapularis larvae and nymphs as
they first acquired spirochetes from infected mice. Smears of midguts
from previously infected ticks were prepared at 12- or 24-h intervals
following attachment through repletion at 96 h, and spirochetes
were stained for immunofluorescence for detection of antibodies to OspA
and OspC. As shown previously, prior to feeding spirochetes in nymphs
expressed OspA but not OspC. During nymphal feeding, however, the
proportion of spirochetes expressing OspA decreased, while spirochetes
expressing OspC became detectable. In fact, spirochetes rapidly began
to express OspC, with the greatest proportion of spirochetes having
this protein at 48 h of attachment and then with the proportion
decreasing significantly by the time that the ticks had completed
feeding. In vitro cultivation of the spirochete at different
temperatures showed OspC to be most abundant when the spirochetes were
grown at 37°C. Yet, the synthesis of this protein waned with
continuous passage at this temperature. Immunofluorescence staining of
spirochetes in smears of midguts from larvae and nymphs still attached
or having completed feeding on infected mice demonstrated that OspA but
not OspC was produced by these spirochetes recently acquired from mice.
Therefore, the temporal synthesis of OspC by spirochetes only in
feeding ticks that were infected prior to the blood meal suggests that
this surface protein is involved in transmission from tick to mammal
but not from mammal to tick.
0095-1137/0/$04.00+0
Temporal Changes in Outer Surface Proteins A and C
of the Lyme Disease-Associated Spirochete, Borrelia
burgdorferi, during the Chain of Infection in Ticks and
Mice
*
Corresponding author. Mailing address: Rocky Mountain
Laboratories, 903 S. Fourth St., Hamilton, MT. Phone: (406) 363-9250. Fax: (406) 363-9371. E-mail: tom_schwan{at}nih.gov.
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