Hydrogen as an energy source for the human pathogen Bilophila wadsworthia

Antonie Van Leeuwenhoek. 2008 May;93(4):381-90. doi: 10.1007/s10482-007-9215-x. Epub 2007 Dec 9.


The gram-negative anaerobic gut bacterium Bilophila wadsworthia is the third most common isolate in perforated and gangrenous appendicitis, being also found in a variety of other infections. This organism performs a unique kind of anaerobic respiration in which taurine, a major organic solute in mammals, is used as a source of sulphite that serves as terminal acceptor for the electron transport chain. We show here that molecular hydrogen, one of the major products of fermentative bacteria in the colon, is an excellent growth substrate for B. wadsworthia. We have quantified the enzymatic activities associated with the oxidation of H(2), formate and pyruvate for cells obtained in different growth conditions. The cell extracts present high levels of hydrogenase activity, and up to five different hydrogenases can be expressed by this organism. One of the hydrogenases appears to be constitutive, whereas the others show differential expression in different growth conditions. Two of the hydrogenases are soluble and are recognised by antibodies against a [FeFe] hydrogenase of a sulphate reducing bacterium. One of these hydrogenases is specifically induced during fermentative growth on pyruvate. Another two hydrogenases are membrane-bound and show increased expression in cells grown with hydrogen. Further work should be carried out to reveal whether oxidation of hydrogen contributes to the virulence of B. wadsworthia.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bilophila / enzymology
  • Bilophila / growth & development
  • Bilophila / metabolism*
  • Desulfovibrionaceae Infections / microbiology*
  • Formate Dehydrogenases / analysis
  • Formate Dehydrogenases / metabolism
  • Humans
  • Hydrogen / metabolism*
  • Hydrogenase / analysis
  • Hydrogenase / metabolism
  • Isoenzymes / analysis
  • Isoenzymes / metabolism
  • Pyruvate Synthase / analysis
  • Pyruvate Synthase / metabolism


  • Isoenzymes
  • Hydrogen
  • Hydrogenase
  • Formate Dehydrogenases
  • Pyruvate Synthase