A Borrelia burgdorferi Surface-Exposed Transmembrane Protein Lacking Detectable Immune Responses Supports Pathogen Persistence and Constitutes a Vaccine Target


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Kung F., Kaur S., Smith A. A., Yang X., Wilder C. N., Sharma K., ...More

JOURNAL OF INFECTIOUS DISEASES, vol.213, no.11, pp.1786-1795, 2016 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 213 Issue: 11
  • Publication Date: 2016
  • Doi Number: 10.1093/infdis/jiw013
  • Journal Name: JOURNAL OF INFECTIOUS DISEASES
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1786-1795
  • Keywords: Borrelia burgdorferi, BB0405, pathogen persistence, transmission-blocking, vaccine, LYME-DISEASE SPIROCHETE, OUTER-MEMBRANE PROTEINS, WHOLE-GENOME SEQUENCES, GENE-EXPRESSION, TICKS, TRANSMISSION, MICE, LIPOPROTEIN, ARTHRITIS, VECTOR
  • Ondokuz Mayıs University Affiliated: Yes

Abstract

Borrelia burgdorferi harbors a limited set of transmembrane surface proteins, most of which constitute key targets of humoral immune responses. Here we show that BB0405, a conserved membrane-spanning protein of unknown function, fails to evoke detectable antibody responses despite its extracellular exposure. bb0405 is a member of an operon and ubiquitously expressed throughout the rodent-tick infection cycle. The gene product serves an essential function in vivo, as bb0405-deletion mutants are unable to transmit from ticks and establish infection in mammalian hosts. Despite the lack of BB0405-specific immunoglobulin M or immunoglobulin G antibodies during natural infection, mice immunized with a recombinant version of the protein elicited high-titer and remarkably long-lasting antibody responses, conferring significant host protection against tick-borne infection. Taken together, these studies highlight the essential role of an apparently immune-invisible borrelial transmembrane protein in facilitating infection and its usefulness as a target of protective host immunity blocking the transmission of B. burgdorferi.