Antibodies to ospB prevent infection of C3H mice challenged with Borrelia burgdorferi isolates expressing truncated OspB antigens

William Scott Probert, Melissa Crawford, Rance B. LeFebvre

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Truncation of outer surface protein B (OspB) of the Lyme disease agent, Borrelia burgdorferi, may allow the organism to escape immunological destruction and render an OspB-based vaccine ineffective. To investigate this possibility, we have identified two isolates, 297 and CA4, which predominantly express a truncated form of the OspB antigen. In each case, nucleic acid sequencing revealed that truncation of the OspB antigen resulted from a nonsense mutation within the 3' end of the ospB gene. Growth inhibition and protection studies demonstrated that both isolates were neutralized by an anti-OspB serum. Our results indicate that truncated forms of the OspB antigen possess epitopes that may represent important targets for neutralizing antibodies and thus, support the inclusion of OspB as a component of a subunit vaccine.

Original languageEnglish (US)
Pages (from-to)15-19
Number of pages5
JournalVaccine
Volume15
Issue number1
DOIs
StatePublished - Jan 1997
Externally publishedYes

Keywords

  • Borrelia burgdorferi
  • outer surface protein
  • vaccine

ASJC Scopus subject areas

  • Immunology
  • Microbiology
  • Virology
  • Infectious Diseases
  • Public Health, Environmental and Occupational Health
  • veterinary(all)

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