Heparin-binding hemagglutinin HBHA from Mycobacterium tuberculosis affects actin polymerisation (Articolo in rivista)

Type

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

Label

• Heparin-binding hemagglutinin HBHA from Mycobacterium tuberculosis affects actin polymerisation (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

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

• 10.1016/j.bbrc.2011.05.159 (literal)

Alternative label

• Esposito C, Marasco D, Delogu G, Pedone E, Berisio R. (2011)
  Heparin-binding hemagglutinin HBHA from Mycobacterium tuberculosis affects actin polymerisation
  in Biochemical and biophysical research communications (Print)
  (literal)

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

• Esposito C, Marasco D, Delogu G, Pedone E, Berisio R. (literal)

Pagina inizio

• 339 (literal)

Pagina fine

• 344 (literal)

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

• 410 (literal)

Rivista

• Biochemical and biophysical research communications (Rivista)

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

• 6 (literal)

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

• 2 (literal)

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

• Institute of Biostructures and Bioimaging, CNR, Napoli, Italy. (literal)

Titolo

• Heparin-binding hemagglutinin HBHA from Mycobacterium tuberculosis affects actin polymerisation (literal)

Abstract

• HBHA is a mycobacterial cell surface protein that mediates adhesion to epithelial cells and that has been implicated in the dissemination of Mycobacterium tuberculosis (Mtb) from the site of primary infection. In this work, we demonstrate that HBHA is able to bind G-actin whereas its shorter form, deprived of the lysine-rich C-terminal region (HBHA?C), does not bind. Consistently, interaction of actin with HBHA is competitive with heparin binding. Notably, we also observe that HBHA, but not HBHA?C, clearly hampers G-actin polymerisation into F-actin filaments. Since Mtb escapes from the phagosome into the cytosol of host cells, where it can persist and replicate, HBHA is properly localised on the bacterial surface to regulate the dynamic process of cytoskeleton formation driven by actin polymerisation and depolymerisation. (literal)

Prodotto di

• Caratterizzazione strutturale di biomolecole di interesse terapeutico mediante metodologie computazionali (PM.P01.022.002) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• EMILIA MARIA PEDONE (Unità di personale interno)
• RITA BERISIO (Unità di personale interno)
• DANIELA MARASCO (Unità di personale esterno)

Incoming links:

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Caratterizzazione strutturale di biomolecole di interesse terapeutico mediante metodologie computazionali (PM.P01.022.002) (Modulo)

Autore CNR di

• EMILIA MARIA PEDONE (Unità di personale interno)
• RITA BERISIO (Unità di personale interno)
• DANIELA MARASCO (Unità di personale esterno)

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

• Biochemical and biophysical research communications (Rivista)