Li. Karpenko et al., LOCALIZATION OF THE AMINO-TERMINUS OF THE HEPATITIS-B VIRUS CORE ANTIGEN WITHIN THE CORE PARTICLE, Virus research, 52(1), 1997, pp. 15-23
The position of the amino terminus of the hepatitis B virus core antig
en (HBcAg) within the core particle was studied. For this purpose, thr
ee recombinant analogs of HBcAg were designed. One analog, HBcAgR, was
identical in amino acid sequences to the core polypeptide of the hepa
titis B virus; the second, HBeAgR, differed from the authentic protein
in deletion of 39 carboxy-terminal amino acids. The amino acid sequen
ces of the third polypeptide, HBe Delta N and of HBeAgR were similar,
HBe Delta N differed from HBeAgR only in replacement of 3 N-terminal a
mino acids by 16 amino acids of beta-galactosidase. The HBcAg analogs
were compared with respect to their reaction with monoclonal antibody
(mAb E1A7) to the amino-terminal linear epitope of hepatitis B virus e
antigen. Although able to assemble into virus-like particles, the thr
ee analogs of HBcAg, reacted differently with mAb E1A7. It was demonst
rated that mAb E1A7 reacted with both native and denatured HBeAgR. HBe
Delta N was not recognized by mAb E1A7. In contrast, HBcAgR reacted w
ith mAb E1A7 only when denatured. Native HBcAgR did not react with mAb
E1A7 when assembled into particles. Thus evidence was obtained that t
he amino terminus of HBcAg is not exposed on the particle surface. (C)
1997 Elsevier Science B.V.