The major secreted product of the whipworm, Trichuris, is a pore-forming protein

Proc Biol Sci. 1994 Sep 22;257(1350):255-61. doi: 10.1098/rspb.1994.0123.


The data presented here describe the first unequivocable characterization of a pore-forming protein in any helminth parasite. The excretory/secretory (E/S) material of the human whipworm T. trichiura contains a highly abundant protein of molecular mass 47 kDa (TT47); the murine model parasite, T. muris, contains a similarly abundant protein of molecular mass 43 kDa (TM43). When purified to homogeneity, these proteins induce ion-conducting pores in lipid bilayers. Antibodies raised against TM43 abolish channel activity. Pore formation in epithelial cell membranes may facilitate invasion of the host gut by Trichuris and enable the parasite to maintain its syncytial environment in the caecal epithelium. The observation that this activity may be inhibited by antibody opens a possible avenue for drug and vaccine development.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies
  • Cell Membrane / physiology
  • Electrophoresis, Polyacrylamide Gel
  • Helminth Proteins / isolation & purification*
  • Helminth Proteins / physiology
  • Humans
  • Lipid Bilayers
  • Membrane Proteins / isolation & purification*
  • Membrane Proteins / physiology
  • Mice
  • Molecular Weight
  • Phosphatidylcholines
  • Trichuris / chemistry
  • Trichuris / physiology*


  • Antibodies
  • Helminth Proteins
  • Lipid Bilayers
  • Membrane Proteins
  • Phosphatidylcholines
  • 1,2-diphytanoylphosphatidylcholine