Bordetella pertussis binds human C1 esterase inhibitor during the virulent phase, to evade complement-mediated killing

J Infect Dis. 2007 Feb 15;195(4):585-8. doi: 10.1086/510913. Epub 2007 Jan 10.

Abstract

C1 esterase inhibitor (C1inh) is a major inhibitor of several pathways of inflammation in humans. In this study, we show that virulent-phase cultures of Bordetella pertussis, the etiological agent for whooping cough, but not other Bordetella species specifically recruit C1inh from human serum. Using a spontaneous mutant of B. pertussis that was deficient in C1inh binding, we demonstrate that the ability of B. pertussis to acquire high levels of human C1inh and wild-type levels of serum resistance are well correlated, suggesting that, in addition to and independent of BrkA expression, acquisition of C1inh is vital to B. pertussis resistance to complement-mediated killing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bordetella pertussis / genetics
  • Bordetella pertussis / immunology*
  • Bordetella pertussis / metabolism
  • Bordetella pertussis / pathogenicity*
  • Complement C1 Inactivator Proteins / metabolism*
  • Complement System Proteins / immunology*
  • Humans
  • Mutation
  • Protein Binding
  • Virulence

Substances

  • Complement C1 Inactivator Proteins
  • Complement System Proteins