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Titolo:
AN ASPARTATE RESIDUE OF THE YERSINIA-PSEUDOTUBERCULOSIS INVASIN PROTEIN THAT IS CRITICAL FOR INTEGRIN BINDING
Autore:
LEONG JM; MORRISSEY PE; MARRA A; ISBERG RR;
Indirizzi:
TUFTS UNIV,SCH MED,HOWARD HUGHES MED INST BOSTON MA 02111 TUFTS UNIV,SCH MED,HOWARD HUGHES MED INST BOSTON MA 02111 TUFTS UNIV,NEW ENGLAND MED CTR,DEPT MED,DIV RHEUMATOL BOSTON MA 02111 TUFTS UNIV,SCH MED,DEPT MOLEC BIOL & MICROBIOL BOSTON MA 02111
Titolo Testata:
EMBO journal
fascicolo: 3, volume: 14, anno: 1995,
pagine: 422 - 431
SICI:
0261-4189(1995)14:3<422:AAROTY>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
CULTURED MAMMALIAN-CELLS; ARG-GLY-ASP; ESCHERICHIA-COLI; FIBRONECTIN RECEPTOR; BACTERIAL ATTACHMENT; SIGNAL-TRANSDUCTION; ADHESION RECEPTORS; ALPHA-SUBUNIT; ENTEROCOLITICA; ACID;
Keywords:
BACTERIAL ENTRY; CELL ADHESION; INTEGRIN; INVASIN; YERSINIA PSEUDOTUBERCULOSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
58
Recensione:
Indirizzi per estratti:
Citazione:
J.M. Leong et al., "AN ASPARTATE RESIDUE OF THE YERSINIA-PSEUDOTUBERCULOSIS INVASIN PROTEIN THAT IS CRITICAL FOR INTEGRIN BINDING", EMBO journal, 14(3), 1995, pp. 422-431

Abstract

The Yersinia pseudotuberculosis invasin protein mediates bacterial entry into mammalian cells by binding multiple beta(1)-chain integrins. Invasin binding to purified alpha(5) beta(1) integrin is inhibited by Arg-Gly-Asp (RGD)-containing peptides, although invasin contains no RGD sequence, Fifteen mutations that diminished binding and bacterial entry were isolated after mutagenesis of the entire inv gene, All of themutations altered residues within the C-terminal 192 amino acids of invasin, previously delineated as the integrin binding domain, and 10 of the mutations fell within an 11 residue region, This small region was subjected to site-directed mutagenesis and almost half of the 35 mutations generated decreased invasin-mediated entry. D911 within this region was the most critical residue, as even a conservative glutamate substitution abolished bacterial penetration, Purified invasin derivatives altered at this residue were defective in promoting cell attachment and this defect was reflected in a 10-fold or greater increase in IC50 for integrin binding, D911 may have a function similar to that of the aspartate residue in RGD-containing sequences.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 14:21:44