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Titolo:
IDENTIFICATION AND ANALYSES OF GLYCOPROTEIN-B OF HUMAN HERPESVIRUS-7
Autore:
HATA A; MUKAI T; ISEGAWA Y; YAMANISHI K;
Indirizzi:
OSAKA UNIV,MICROBIAL DIS RES INST,DEPT VIROL,3-1 YAMADA OKA SUITA OSAKA 565 JAPAN OSAKA UNIV,MICROBIAL DIS RES INST,DEPT VIROL SUITA OSAKA 565 JAPAN OSAKA UNIV,SCH MED,DEPT MICROBIOL SUITA OSAKA 565 JAPAN
Titolo Testata:
Virus research
fascicolo: 1-2, volume: 46, anno: 1996,
pagine: 125 - 137
SICI:
0168-1702(1996)46:1-2<125:IAAOGO>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
SIMPLEX VIRUS TYPE-1; MONOCLONAL-ANTIBODIES; NEUTRALIZING ANTIBODIES; SYNCYTIUM FORMATION; FREQUENT ISOLATION; STRAIN TOWNE; T-CELLS; CYTOMEGALOVIRUS; GENE; SALIVA;
Keywords:
GLYCOPROTEIN B; GST FUSION PROTEIN; HUMAN HERPESVIRUS 7; IMMUNOPRECIPITATION; MONOSPECIFIC ANTISERA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
A. Hata et al., "IDENTIFICATION AND ANALYSES OF GLYCOPROTEIN-B OF HUMAN HERPESVIRUS-7", Virus research, 46(1-2), 1996, pp. 125-137

Abstract

The gene for the human herpes virus 7 (HHV-7) glycoprotein B (gB) hasbeen identified by sequencing a molecularly cloned HHV-7 DNA fragment. A 2.5-kb open reading frame (ORF) encoded a protein of 822 amino acids with characteristics of a transmembrane glycoprotein, and showed the strongest similarity (56.5%) with the human herpesvirus 6 (HHV-6) gB. The genes for the transport/capsid assembly protein (tp/cap) and theDNA polymerase (pol) existed upstream and downstream of the gB gene, respectively. This arrangement was the same as that of HHV-6. Antiserawere generated by immunizing mice with a glutathione S-transferase-carboxy terminal gB fusion protein. Immunofluorescent tests demonstratedthat the antisera reacted specifically with HHV-7 antigens in cytoplasm of infected cells. The antisera immunoprecipitated proteins with apparent molecular masses of 51, 63 and 112 kDa from HHV-7 infected cells by pulse-chase analysis. In the presence of tunicamycin, the proteinwith a molecular mass of 112 kDa was replaced by a protein with a molecular mass of 88 kDa, and this size was consistent with the predictedsize of the primary translation product of the HHV-7 gB gene. These results suggested that the protein with a molecular mass of 112 kDa wasa glycoprotein synthesized by addition of N-linked oligosaccharides to a non-glycosylated precursor of the protein with a molecular mass of88 kDa and then cleaved into the proteins with molecular masses of 51and 63 kDa in HHV-7 infected cells. Copyright (C) 1996 Elsevier Science B.V.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 15:55:28