BB0761, a MepM homolog, contributes to Borrelia burgdorferi cell division and mammalian infectivity

Christina Thompson, Sierra George, Maria L. White, Prahathees J. Eswara, Zhiming Ouyang

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


M23 family endopeptidases play important roles in cell division and separation in a wide variety of bacteria. Recent studies have suggested that these proteins also contribute to bacterial virulence. However, the biological function of M23 peptidases in pathogenic spirochetes remains unexplored. Here, we describe Borrelia burgdorferi, the bacterial pathogen causing Lyme disease, requires a putative M23 family homolog, BB0761, for spirochete morphology and cell division. Indeed, the inactivation of bb0761 led to an aberrant filamentous phenotype as well as the impairment of B. burgdorferi growth in vitro. These phenotypes were complemented not only with B. burgdorferi bb0761, but also with the mepM gene from E. coli. Moreover, the bb0761 mutant showed a complete loss of infectivity in a murine model of Lyme borreliosis. Resistance of the mutant to osmotic and oxidative stresses was markedly reduced. Our combined results indicate that BB0761 contributes to B. burgdorferi cell division and virulence.

Original languageEnglish (US)
Pages (from-to)1405-1418
Number of pages14
JournalMolecular Microbiology
Issue number6
StatePublished - Jun 2022
Externally publishedYes


  • Borrelia burgdorferi
  • gene regulation
  • lyme disease
  • pathogenesis
  • protease
  • virulence

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology


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