Type-4 pilus-structure: outside to inside and top to bottom--a minireview

Gene. 1997 Jun 11;192(1):165-9. doi: 10.1016/s0378-1119(97)00008-5.


We have recently proposed a computational model of the N. gonorrhoeae pilus fiber based on the high resolution X-ray crystal structure of the component protein pilin, combined with available biophysical and genetic data [Parge et al. (1995) Nature 378, 32-38]. In parallel, we have used anti-peptide antibodies to distinguish buried and exposed regions of pilin within the assembled fiber [Forest et al. (1996) Infect. Immun. 64, 644-652]. This mini-review addresses the properties of the current pilus model and the locations of end-exposed epitopes. The fiber forms a three-layered structure of coiled conserved alpha helices surrounded by beta-sheet, with the hypervariable region as the most highly exposed portion. Overall the pilus model developed from diffraction and antibody mapping is expected to be representative of type-4 pili with general implications for type-4 assembly, function, and interactions with other proteins and cell membranes.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / chemistry*
  • Conserved Sequence
  • Crystallography, X-Ray
  • Fimbriae Proteins
  • Fimbriae, Bacterial / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Neisseria gonorrhoeae / chemistry*
  • Protein Conformation
  • Protein Structure, Secondary


  • Bacterial Outer Membrane Proteins
  • Fimbriae Proteins