Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
GroEL (Hsp60) of Clostridium difficile is involved in cell adherence
Autore:
Hennequin, C; Porcheray, F; Waligora-Dupriet, AJ; Collignon, A; Bare, MC; Bourlioux, P; Karjalainen, T;
Indirizzi:
Univ Paris Sud, Fac Pharm, Dept Microbiol, F-92296 Chatenay Malabry, France Univ Paris Sud Chatenay Malabry France F-92296 Chatenay Malabry, France
Titolo Testata:
MICROBIOLOGY-UK
, volume: 147, anno: 2001,
parte:, 1
pagine: 87 - 96
SICI:
1350-0872(200101)147:<87:G(OCDI>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEAT-SHOCK-PROTEIN; HELICOBACTER-PYLORI UREASE; LEGIONELLA-PNEUMOPHILA; BACILLUS-SUBTILIS; HAEMOPHILUS-DUCREYI; SECONDARY-STRUCTURE; ESCHERICHIA-COLI; EPITHELIAL-CELLS; SURFACE; LOCALIZATION;
Keywords:
Clostridium difficile; adherence; pathogenesis; GroEL; heat shock;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Karjalainen, T Univ Paris Sud, Fac Pharm, Dept Microbiol, 5 Rue JB Clement, F-92296 Chatenay Malabry, France Univ Paris Sud 5 Rue JB Clement ChatenayMalabry France F-92296
Citazione:
C. Hennequin et al., "GroEL (Hsp60) of Clostridium difficile is involved in cell adherence", MICROBIO-UK, 147, 2001, pp. 87-96

Abstract

Previous results have demonstrated that adherence of Clostridium difficileto tissue culture cells is augmented by various stresses; this study focussed on whether the GroEL heat shock protein is implicated in this process. The 1940 bp groESL operon of C. difficile was isolated by PCR. The 1623 bp groEL gene is highly conserved between Various C. difficile isolates as determined by RFLP-PCR and DNA sequencing, and the operon is present in one copy on the bacterial chromosome. The 58 kDa GroEL protein was expressed in Escherichia coli in fusion with glutathione S-transferase and the fusion protein was purified from IPTG-induced bacterial lysates by affinity chromatography on glutathione-Sepharose. A polyclonal, monospecific antiserum was obtained for GroEL which established by immunoelectron microscopy, indirect immunofluorescence and immunoblot analysis that GroEL is released extracellularly after heat shock and can be surface associated. Cell fractionation experiments suggest that GroEL is predominantly cytoplasmic and membrane bound. GroEL-specific antibodies as well as the purified protein partially inhibited C. difficile cell attachment and expression of the protein was induced by cell contact. suggesting a role for GroEL in cell adherence.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 07:21:20