Identification and functional analysis of an immunoreactive DsbA-like thio-disulfide oxidoreductase of Ehrlichia spp

Infect Immun. 2002 May;70(5):2700-3. doi: 10.1128/IAI.70.5.2700-2703.2002.

Abstract

Novel homologous DsbA-like disulfide bond formation (Dsb) proteins of Ehrlichia chaffeensis and Ehrlichia canis were identified which restored DsbA activity in complemented Escherichia coli dsbA mutants. Recombinant Ehrlichia Dsb (eDsb) proteins were recognized by sera from E. canis-infected dogs but not from E. chaffeensis-infected patients. The eDsb proteins were observed primarily in the periplasm of E. chaffeensis and E. canis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Base Sequence
  • Dogs
  • Ehrlichia / enzymology*
  • Humans
  • Molecular Sequence Data
  • Protein Disulfide-Isomerases / analysis*
  • Protein Disulfide-Isomerases / genetics
  • Protein Disulfide-Isomerases / physiology

Substances

  • Protein Disulfide-Isomerases