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Journal of Bacteriology, July 2008, p. 4749-4753, Vol. 190, No. 13
0021-9193/08/$08.00+0     doi:10.1128/JB.01988-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Evidence for an Elongated Dimeric Structure of Heparin-Binding Hemagglutinin from Mycobacterium tuberculosis

Istituto di Biostrutture e Bioimmagini, C.N.R., I-80134, Napoli, Italy,¹ European Molecular Biology Lab, Hamburg, c/o DESY, Notkestrasse 85, 22603 Hamburg, Germany,² Dipartimento delle Scienze Biologiche, Sezione di Biostrutture, Università degli Studi di Napoli Federico II, I-80134, Napoli, Italy³

Received 21 December 2007/ Accepted 13 April 2008

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.

Published ahead of print on 25 April 2008.