Literature DB >> 1693247

Epitope-specific antibody response to the surface antigen of duck hepatitis B virus in infected ducks.

R C Cheung1, D E Trujillo, W S Robinson, H B Greenberg, P L Marion.   

Abstract

In order to investigate the immune response to duck hepatitis B virus (DHBV) infection, newly hatched DHBV DNA negative ducklings were injected with infectious serum of sufficiently low DHBV-DNA titer to allow clearance of viremia. Of 20 injected ducklings, 13 (65%) became viremic. Of these, 6 (46%) cleared virus from the serum 3 to 22 weeks postinjection. The convalescent sera of these 6 animals were tested for an epitope-specific antibody response in a highly specific competitive inhibition assay using a panel of monoclonal antibodies against duck hepatitis B surface antigen (DHBsAg) that had been well-characterized. All 6 animals recovering from DHBV infection developed antibodies to epitopes on the preS and S proteins of DHBV. Antibody responses were highly variable with marked differences between animals in the extent and specificity of the antibody response. The humoral response to DHBsAg was prolonged in some animals but transient in others. No antibody to preS or S was detected in either preimmune sera or sera of control animals from an uninfected flock. Infected animals that did not clear viremia also remained antibody negative. The humoral responses to neutralizing preS epitopes III and V were weak but antibodies to two immunodominant epitopes on the preS region (II and B) were present in all 6 animals. The humoral response to the two epitopes in the S region was transient and of lower titer when compared to the two immunodominant preS epitopes. The two immunodominant preS epitopes may play an important role in clearance of DHBV infection in ducks.

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Year:  1990        PMID: 1693247     DOI: 10.1016/0042-6822(90)90025-m

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  6 in total

1.  The pre-S domain of the large viral envelope protein determines host range in avian hepatitis B viruses.

Authors:  T Ishikawa; D Ganem
Journal:  Proc Natl Acad Sci U S A       Date:  1995-07-03       Impact factor: 11.205

2.  Residues critical for duck hepatitis B virus neutralization are involved in host cell interaction.

Authors:  C Sunyach; C Rollier; M Robaczewska; C Borel; L Barraud; A Kay; C Trépo; H Will; L Cova
Journal:  J Virol       Date:  1999-04       Impact factor: 5.103

3.  Protective efficacy of DNA vaccines against duck hepatitis B virus infection.

Authors:  M Triyatni; A R Jilbert; M Qiao; D S Miller; C J Burrell
Journal:  J Virol       Date:  1998-01       Impact factor: 5.103

4.  Naturally occurring point mutation in the C terminus of the polymerase gene prevents duck hepatitis B virus RNA packaging.

Authors:  Y Chen; W S Robinson; P L Marion
Journal:  J Virol       Date:  1992-02       Impact factor: 5.103

5.  A cell surface protein that binds avian hepatitis B virus particles.

Authors:  K Kuroki; R Cheung; P L Marion; D Ganem
Journal:  J Virol       Date:  1994-04       Impact factor: 5.103

6.  Spread of hepatitis B viruses in vitro requires extracellular progeny and may be codetermined by polarized egress.

Authors:  A Funk; H Hohenberg; M Mhamdi; H Will; H Sirma
Journal:  J Virol       Date:  2004-04       Impact factor: 5.103

  6 in total

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