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

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.

• Authors: Carla Esposito, Maxim V Pethoukov, Dmitri I Svergun, Alessia Ruggiero, Carlo Pedone, Emilia Pedone, Rita Berisio
• Journal: Journal of bacteriology (J Bacteriol) Vol. 190 Issue 13 Pg. 4749-53 (Jul 2008) ISSN: 1098-5530 [Electronic] United States
• PMID: 18441065 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Bacterial Proteins
• Lectins
• heparin-binding hemagglutinin

Topics

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