Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: implications for bacterial agglutination (Articolo in rivista)

Type
Label
  • Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: implications for bacterial agglutination (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.febslet.2010.02.044 (literal)
Alternative label
  • Esposito C, Carullo C, Pedone E, Graziano G, Del Vecchio P, Berisio R (2010)
    Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: implications for bacterial agglutination
    in FEBS letters (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Esposito C, Carullo C, Pedone E, Graziano G, Del Vecchio P, Berisio R (literal)
Pagina inizio
  • 1091 (literal)
Pagina fine
  • 1096 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 584 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • a Istitute of Biostructures and Bioimaging, C.N.R., I-80134 - Naples, Italy b Department of Chemistry ''Paolo Corradini\", University of Naples Federico II, Complesso Universitario Monte S. Angelo, I-80126, Naples, Italy c Department of Biological and Environmental Sciences, University of Sannio, I-82100 Benevento, Italy (literal)
Titolo
  • Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: implications for bacterial agglutination (literal)
Abstract
  • Heparin Binding Hemagglutinin A (HBHA) is hitherto the sole virulence factor associated with tuberculosis dissemination from the lungs, the site of primary infection, to epithelial cells. We have previously reported the solution structure of HBHA, a dimeric and elongated molecule. Since oligomerisation of HBHA is associated with its ability to induce bacterial agglutination, we investigated this process using experimental and modelling techniques. We here identified a short segment of HBHA whose presence is mandatory for the stability of folded conformation, whose denaturation is a reversible two-state process. Our data suggest that agglutination-driven cell-cell interactions do not occur via association of HBHA monomers, nor via association of HBHA dimers and open the scenario to a possible trans-dimerisation process. (literal)
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