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Titolo:
THE N-TERMINUS OF HEPATITIS-B VIRUS CORE PROTEIN IS NOT EXPOSED ON THE CORE SURFACE
Autore:
KARPENKO LI; RYASANKIN IA; CHIKAEV NA; KOLESNIKOVA LV; ILICHEV AA;
Indirizzi:
VEKTOR RES CTR VIROL & BIOTECHNOL,INST BIOENGN KOLTSOV 633159 NOVOSIBIRSK OBL RUSSIA RUSSIAN ACAD SCI,INST BIOORGAN CHEM NOVOSIBIRSK 630090 RUSSIA
Titolo Testata:
Molecular biology
fascicolo: 5, volume: 31, anno: 1997,
pagine: 785 - 790
SICI:
0026-8933(1997)31:5<785:TNOHVC>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; PARTICLES; ANTIGEN; IMMUNOGENICITY; EPITOPES; DETERMINANTS;
Keywords:
HEPATITIS B VIRUS; EXPRESSION IN ESCHERICHIA COLI; MONOCLONAL ANTIBODIES; ANTIGENIC DETERMINANTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
L.I. Karpenko et al., "THE N-TERMINUS OF HEPATITIS-B VIRUS CORE PROTEIN IS NOT EXPOSED ON THE CORE SURFACE", Molecular biology, 31(5), 1997, pp. 785-790

Abstract

Localization of the N terminus of the hepatitis B virus core antigen (HBcAg) was studied using recombinant HBcAg analogs. The amino acid sequence of the first analog (HBcAgR) was identical with that of the hepatitis B virus core polypeptide. The difference between the second recombinant protein (HBeAgR) and the native one was a 39-amino-acid deletion at the C terminus. The sequence of the third polypeptide (HBe Delta N) was similar to that of HBeAgR except for three N-terminal amino acids replaced with 16 amino acids of beta-galactosidase. The polypeptides were compared in reaction with monoclonal antibodies to the N-terminal linear epitope of hepatitis B virus e-antigen (MAb E1A7). Despitethe fact that all three recombinant proteins assemble into virus-likeparticles, they react differently with MAb E1A7. MAb E1A7 was found to bind to both intact and denatured HBeAgR. No binding with MAb E1A7 was observed for HBe Delta N, whereas HBcAgR reacted only in denatured form. A conclusion was made that the N-terminus of HBcAg is not exposed on the core surface.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 09:33:23