Mutation of the zinc-binding metalloprotease motif affects Bacteroides fragilis toxin activity but does not affect propeptide processing

Infect Immun. 2005 Aug;73(8):5273-7. doi: 10.1128/IAI.73.8.5273-5277.2005.

Abstract

To evaluate the role of the zinc-binding metalloprotease in Bacteroides fragilis toxin (BFT) processing and activity, the zinc-binding consensus sequences (H348, E349, H352, G355, H358, and M366) were mutated by site-directed-mutagenesis. Our results indicated that single point mutations in the zinc-binding metalloprotease motif do not affect BFT processing but do reduce or eliminate BFT biologic activity in vitro.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Bacterial Toxins / metabolism*
  • Bacteroides fragilis / enzymology
  • Cadherins / metabolism
  • Immunoblotting
  • Metalloendopeptidases / metabolism*
  • Metalloproteases / genetics*
  • Metalloproteases / metabolism
  • Mutation
  • Peptides / metabolism*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Zinc / metabolism*

Substances

  • Bacterial Toxins
  • Cadherins
  • Peptides
  • Metalloproteases
  • Bacteroides fragilis toxin
  • Metalloendopeptidases
  • Zinc