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Antigenicity of a candidate varicella-zoster virus glycoprotein subunit vaccine.

作者信息

Vafai A

机构信息

Department of Biomedical Sciences, University of Illinois, College of Medicine, Rockford 61107-1897.

出版信息

Vaccine. 1993;11(9):937-40. doi: 10.1016/0264-410x(93)90382-8.

DOI:10.1016/0264-410x(93)90382-8
PMID:8212841
Abstract

A 1642 bp DNA fragment, encoding the N-terminal region and 511 amino acid residues of varicella-zoster virus (VZV) glI gene, was inserted into vaccinia virus genome. The expression of recombinant vaccinia virus (designated VVTgpI-511) yielded the synthesis of a 60 kDa protein species which was processed to a secretory 76 kDa polypeptide (designated TgpI-511). The antigenicity of this protein was examined by subcutaneous inoculation of one rabbit with 100 micrograms purified TgpI-511 in the Ribi adjuvant system. The animal was boosted 3 weeks after the initial inoculation and antisera were tested 7 days after the last injection by immunoprecipitation and neutralization tests. The results showed that rabbit antibodies to TgpI-511 (RAnti-TgpI-511) were reactive with purified TgpI-511 as well as native gpI in VZV-infected cells. In addition, TgpI-511 was capable of eliciting complement-dependent VZV neutralizing antibodies. These results suggested that the purified preparation of TgpI-511 may have the potential to be used as a candidate VZV subunit vaccine.

摘要

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