Ion channels and bacterial infection: the case of beta-barrel pore-forming protein toxins of Staphylococcus aureus. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Ion channels and bacterial infection: the case of beta-barrel pore-forming protein toxins of Staphylococcus aureus. (Articolo in rivista) (literal)

Anno

• 2003-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1016/S0014-5793(03)00850-0 (literal)

Alternative label

• Menestrina G., Dalla Serra M., Comai M., Coraiola M., Viero G., Werner S., Colin D.A., Monteil H., Prévost G. (2003)
  Ion channels and bacterial infection: the case of beta-barrel pore-forming protein toxins of Staphylococcus aureus.
  in FEBS letters (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Menestrina G., Dalla Serra M., Comai M., Coraiola M., Viero G., Werner S., Colin D.A., Monteil H., Prévost G. (literal)

Pagina inizio

• 54 (literal)

Pagina fine

• 60 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 552 (literal)

Rivista

• FEBS letters (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• CNR-ITC Istituto di Bio¢sica, Sezione di Trento, Via Sommarive 18, I-38050 Povo, Italy INSERM-U544, Institut de Virologie de la Faculte¤ de Me¤decine, ULP-HUS, 3rue Koeberle¤, F-67000 Strasbourg, France Institut de Bacte¤riologie de la Faculte¤ de Me¤decine, UPRES EA-3432, ULP-HUS, 3 rue Koeberle¤, F-67000 Strasbourg, France (literal)

Titolo

• Ion channels and bacterial infection: the case of beta-barrel pore-forming protein toxins of Staphylococcus aureus. (literal)

Abstract

• Staphylococcus aureus strains causing human pathologies produce several toxins, including a pore-forming protein family formed by the single-component alpha-hemolysin and the bicomponent leukocidins and gamma-hemolysins. The last comprise two protein elements, S and F, that co-operatively form the active toxin. alpha-Hemolysin is always expressed by S. aureus strains, whereas bicomponent leukotoxins are more specifically involved in a few diseases. X-ray crystallography of the alpha-hemolysin pore has shown it is a mushroom-shaped, hollow heptamer, almost entirely consisting of beta-structure. Monomeric F subunits have a very similar core structure, except for the transmembrane stem domain which has to refold during pore formation. Large deletions in this domain abolished activity, whereas shorter deletions sometimes improved it, possibly by removing some of the interactions stabilizing the folded structure. Even before stem extension is completed, the formation of an oligomeric pre-pore can trigger Ca(2+)-mediated activation of some white cells, initiating an inflammatory response. Within the bicomponent toxins, gamma-hemolysins define three proteins (HlgA, HlgB, HlgC) that can generate two toxins: HlgA+HlgB and HlgC+HlgB. Like alpha-hemolysin they form pores in planar bilayers with similar conductance, but opposite selectivity (cation instead of anion) for the presence of negative charges in the ion pathway. gamma-Hemolysin pores seem to be organized as alpha-hemolysin, but should contain an even number of each component, alternating in a 1:1 stoichiometry. (literal)

Prodotto di

• Istituto di biofisica (IBF) (Istituto)

Autore CNR

• MAURO DALLA SERRA (Unità di personale interno)
• GIANFRANCO MENESTRINA (Unità di personale interno)
• GABRIELLA VIERO (Persona)

Incoming links:

Prodotto

• Istituto di biofisica (IBF) (Istituto)

Autore CNR di

• MAURO DALLA SERRA (Unità di personale interno)
• GABRIELLA VIERO (Persona)
• GIANFRANCO MENESTRINA (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• FEBS letters (Rivista)