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Titolo:
VACCINIA VIRUS-ENCODED CYTOKINE RECEPTOR BINDS AND NEUTRALIZES CHICKEN INTERFERON-GAMMA
Autore:
PUEHLER F; WEINING KC; SYMONS JA; SMITH GL; STAEHELI P;
Indirizzi:
UNIV FREIBURG,DEPT VIROL,INST MED MIKROBIOL & HYG,HERMANN HERDER STR 11 D-79008 FREIBURG GERMANY UNIV FREIBURG,DEPT VIROL,INST MED MIKROBIOL & HYG D-79008 FREIBURG GERMANY UNIV OXFORD,SIR WILLIAM DUNN SCH PATHOL OXFORD OX1 3RE ENGLAND
Titolo Testata:
Virology (New York, N.Y. Print)
fascicolo: 2, volume: 248, anno: 1998,
pagine: 231 - 240
SICI:
0042-6822(1998)248:2<231:VVCRBA>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
BROAD SPECIES-SPECIFICITY; IFN-GAMMA; NUCLEOTIDE-SEQUENCE; HOST RESPONSE; NITRIC-OXIDE; C-TERMINUS; PROTEIN; GENE; BIOLOGY; CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
F. Puehler et al., "VACCINIA VIRUS-ENCODED CYTOKINE RECEPTOR BINDS AND NEUTRALIZES CHICKEN INTERFERON-GAMMA", Virology (New York, N.Y. Print), 248(2), 1998, pp. 231-240

Abstract

To counteract the host immune response, poxviruses have evolved secreted factors that bind cytokines and thereby neutralize their biological activities. The vaccinia virus B8R gene encodes a protein that neutralizes interferon-gamma (IFN-gamma) from several mammals including man, cow, rat, and rabbit but not mice. we now report that the activity of the B8R gene product is not restricted to cytokines of mammals: it also efficiently neutralized chicken IFN-gamma. B8R blocked chicken IFN-gamma-mediated induction of guanylate binding protein RNP, in the chicken fibroblast cell line CEC-32 and secretion of nitric oxide in HD-11 cells. Radiolabeled baculovirus-expressed B8R efficiently bound to immobilized recombinant chicken IFN-gamma. Scatchard analysis revealed a binding constant of chicken IFN-gamma to B8R of approximately 0.5 nM. A mutant form of chicken IFN-gamma which lacks the 18 C-terminal amino acids and which has lost more than 99% of its biological activity was able to block the IFN-gamma-neutralizing effect of B8R. Binding studies showed that the mutant protein bound radiolabeled B8R only about threefold less well than wild-type chicken IFN-gamma but failed to compete with wild-type chicken IFN-gamma for binding to the cellular receptor. These results suggest that the extreme C terminus of chicken IFN-gamma is crucial for binding to its cellular receptor but less important for recognition by the viral cytokine receptor. (C) 1998 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/01/20 alle ore 19:57:28