Crystal structure of Borrelia burgdorferi outer surface protein BBA69 in comparison to the paralogous protein CspA

Publication date: Available online 11 June 2019Source: Ticks and Tick-borne DiseasesAuthor(s): Kalvis Brangulis, Inara Akopjana, Ivars Petrovskis, Andris Kazaks, Kaspars TarsAbstractThe spirochete Borrelia burgdorferi sensu lato is the causative agent of Lyme borreliosis – the most common tick-borne disease in Europe and the United States. Spirochetes are transmitted from infected Ixodes ticks to the mammalian host when the ticks feed. In general, the transfer process of the borreliae is quite complicated, as the environments in the tick and the new mammalian host differs significantly. Therefore, Borrelia changes the expression profile of dozens of proteins, mainly outer surface proteins, to adapt to the new tasks and needs in the new organism. In the transfer process from the tick to the mammalian host, spirochetes that cause Lyme disease show the strongest upregulation of members of paralogous gene family 54 (PFam54). PFam54 members encode 10 proteins, and BBA69 is one of its members. Although several PFam54 members play an important role in the pathogenesis of Lyme disease, the exact function has been determined only for CspA, which binds complement regulator factor H (CFH) and factor H-like protein 1 (FHL-1); thus, CspA is essential to resist the vertebrate host’s immune response. In the current study, we determined the crystal structure of BBA69 at a 2.25 Ǻ resolution. The BBA69 structure revealed a seven α-helical BbCRASP-1 fold previously found only in PFam54 me...
Source: Ticks and Tick borne Diseases - Category: Zoology Source Type: research