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J. Bacteriol. doi:10.1128/JB.01988-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Evidence for an elongated dimeric structure of heparin-binding haemagglutinin from M. tuberculosis

Carla Esposito, Maxim V. Pethoukov, Dmitri I. Svergun, Alessia Ruggiero, Carlo Pedone, Emilia Pedone*, and Rita Berisio*

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

* To whom correspondence should be addressed. Email: empedone{at}unina.it. rita.berisio{at}unina.it.


   Abstract

Heparin-binding haemagglutinin, HBHA, is a virulence factor of tuberculosis which is responsible for extra-pulmonary dissemination of this disease. A thorough biochemical characterisation of HBHA has provided experimental evidence of a coiled coil nature of HBHA. These data, together with the low resolution structure of both a full-length and a truncated form of HBHA by Small Angle X-ray Scattering have unambiguously indicated that HBHA has a dimeric structure with an elongated shape.







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