Functional Equivalence of OspA and OspB, but Not OspC, in Tick Colonization by Borrelia burgdorferi
| Autor: | Patricia A. Rosa, Aaron Bestor, Kit Tilly |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Lipoproteins 030106 microbiology Immunology Gene Expression Mice SCID Tick Microbiology complex mixtures Bacterial genetics 03 medical and health sciences Mice Lyme disease Ticks Antigen parasitic diseases medicine Animals Borrelia burgdorferi Recombination Genetic Antigens Bacterial biology fungi biology.organism_classification medicine.disease bacterial infections and mycoses Virology Antibodies Bacterial Molecular Pathogenesis Bacterial vaccine Bacterial adhesin 030104 developmental biology Infectious Diseases Antigens Surface Bacterial Vaccines biology.protein Parasitology lipids (amino acids peptides and proteins) Antibody Gene Deletion Bacterial Outer Membrane Proteins |
| Zdroj: | Infection and immunity. 84(5) |
| ISSN: | 1098-5522 |
| Popis: | Borrelia burgdorferi , a Lyme disease agent, makes different major outer surface lipoproteins at different stages of its mouse–tick infectious cycle. Outer surface protein A (OspA) coats the spirochetes from the time they enter ticks until they are transmitted to a mammal. OspA is required for normal tick colonization and has been shown to bind a tick midgut protein, indicating that OspA may serve as a tick midgut adhesin. Tick colonization by spirochetes lacking OspA is increased when the infecting blood meal is derived from mice that do not produce antibody, indicating that OspA may protect the spirochetes from host antibody, which will not recognize tick-specific proteins such as OspA. To further study the importance of OspA during tick colonization, we constructed a form of B. burgdorferi in which the ospA open reading frame, on lp54, was replaced with the ospC gene or the ospB gene, encoding a mammal-specific or tick-specific lipoprotein, respectively. These fusions yielded a strain that produces OspC within a tick (from the fusion gene) and during early mammalian infection (from the normal ospC locus) and a strain that produces OspB in place of OspA within ticks. Here we show that the related, tick-specific protein OspB can fully substitute for OspA, whereas the unrelated, mammal-specific protein OspC cannot. These data were derived from three different methods of infecting ticks, and they confirm and extend previous studies indicating that OspA both protects spirochetes within ticks from mammalian antibody and serves an additional role during tick colonization. |
| Databáze: | OpenAIRE |
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