Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis

J Bacteriol. 2008 Jul;190(13):4749-53. doi: 10.1128/JB.01988-07. Epub 2008 Apr 25.

Abstract

Heparin-binding hemagglutinin (HBHA) is a virulence factor of tuberculosis which is responsible for extrapulmonary dissemination of this disease. A thorough biochemical characterization of HBHA has provided experimental evidence of a coiled-coil nature of HBHA. These data, together with the low-resolution structures of a full-length form and a truncated form of HBHA obtained by small-angle X-ray scattering, have unambiguously indicated that HBHA has a dimeric structure with an elongated shape.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Circular Dichroism
  • Dimerization
  • Lectins / chemistry*
  • Lectins / metabolism
  • Models, Molecular
  • Mycobacterium tuberculosis / metabolism*
  • Scattering, Radiation
  • Synchrotrons
  • X-Rays

Substances

  • Bacterial Proteins
  • Lectins
  • heparin-binding hemagglutinin