title: Functional Equivalence of OspA and OspB, but Not OspC, in Tick Colonization by Borrelia burgdorferi.
abstract: 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.
authors.affiliation: Laboratory of Zoonotic Pathogens, Rocky Mountain Laboratories, NIAID, NIH, Hamilton, Montana, USA ktilly@niaid.nih.gov prosa@niaid.nih.gov.
authors.forename: Kit
authors.initials: K
authors.lastname: Tilly
authors.affiliation: Laboratory of Zoonotic Pathogens, Rocky Mountain Laboratories, NIAID, NIH, Hamilton, Montana, USA.
authors.forename: Aaron
authors.initials: A
authors.lastname: Bestor
authors.affiliation: Laboratory of Zoonotic Pathogens, Rocky Mountain Laboratories, NIAID, NIH, Hamilton, Montana, USA ktilly@niaid.nih.gov prosa@niaid.nih.gov.
authors.forename: Patricia A
authors.initials: PA
authors.lastname: Rosa
mesh_terms: D000818:Animals; D000907:Antibodies, Bacterial / Q000276:immunology; D000942:Antigens, Bacterial / Q000235:genetics / Q000378:metabolism*; D000954:Antigens, Surface / Q000235:genetics / Q000378:metabolism*; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D001428:Bacterial Vaccines / Q000235:genetics / Q000378:metabolism*; D025065:Borrelia burgdorferi / Q000254:growth & development* / Q000276:immunology; D017353:Gene Deletion; D015870:Gene Expression; D008074:Lipoproteins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D016513:Mice, SCID; D011995:Recombination, Genetic; D013987:Ticks / Q000382:microbiology*
chemical_list: D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D000954:Antigens, Surface; D001425:Bacterial Outer Membrane Proteins; D001428:Bacterial Vaccines; D008074:Lipoproteins; C072045:OspA protein; C079616:OspC protein; C077030:OspB protein, Borrelia burgdorferi