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Titolo:
TRYPSIN-RESISTANT PROTEASE ACTIVATION MUTANTS OF AN INFLUENZA-VIRUS
Autore:
ORLICH M; LINDER D; ROTT R;
Indirizzi:
UNIV GIESSEN,INST VIROL,FRANKFURTER STR 107 D-35392 GIESSEN GERMANY UNIV GIESSEN,INST VIROL D-35392 GIESSEN GERMANY UNIV GIESSEN,ZENTRUM BIOCHEM D-35392 GIESSEN GERMANY
Titolo Testata:
Journal of General Virology
, volume: 76, anno: 1995,
parte:, 3
pagine: 625 - 633
SICI:
0022-1317(1995)76:<625:TPAMOA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
CLEAVAGE SITE; SENDAI VIRUS; FUSION PROTEIN; MEMBRANE-FUSION; CHICK-EMBRYO; FACTOR-X; A-VIRUS; HEMAGGLUTININ; DETERMINANT; PATHOGENICITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
M. Orlich et al., "TRYPSIN-RESISTANT PROTEASE ACTIVATION MUTANTS OF AN INFLUENZA-VIRUS", Journal of General Virology, 76, 1995, pp. 625-633

Abstract

New classes of mutants of influenza virus A/seal/Mass/1/80 are described in which the haemagglutinins (HA) have lost their protease cleavability by trypsin, but can be activated by elastase, chymotrypsin or thermolysin in different cell types. The same proteases that were required for activation of infectivity of the mutants also activated haemolysis and cell-fusing properties. The protease activation (pal-mutants were nonpathogenic for chickens, but induced a protective immune response against a highly pathogenic challenge virus. The failure of the mutants to be activated by trypsin, but instead to be activated by the other proteases employed, was related to amino acid exchanges around theHA cleavage site. The cleavability of the chymotrypsin and elastase pa-mutants is most likely determined by replacement of Arg-1 by neutralamino acids such as Ile, Thr, Met or Leu, depending on the substrate specificity of the activating proteases. Cleavage activation of the thermolysin pa-mutants, on the other hand, became possible by insertion of a single Leu residue at position 4 of the HA(2) polypeptide, which compensates for the loss of the Gly residue at the N terminus of the fusion peptide due to thermolysin cleavage. The correction of the mutations in revertants confirmed the conclusions drawn from sequence analyses of the pa-mutants.

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Documento generato il 27/01/20 alle ore 17:06:11