http://www.cnr.it/ontology/cnr/individuo/prodotto/ID14213
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
- Pagina fine
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- 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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- Autore CNR
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