Characterization of Glycoprotein H and L of Human Herpesvirus 7
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- Mukai Tetsu
- Department of Virology, Research Institute for Microbial Diseases, Osaka University Medical School
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- Hata Atsuko
- Department of Virology, Research Institute for Microbial Diseases, Osaka University Medical School
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- Isegawa Yuji
- Department of Virology, Research Institute for Microbial Diseases, Osaka University Medical School
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- Yamanishi Koichi
- Department of Virology, Research Institute for Microbial Diseases, Osaka University Medical School
抄録
The genes encoding the glycoproteins H (gH) and L (gL) of human herpesvirus 7 (HHV-7) have been identified. The gH open reading frame (ORF) was 2, 070 base pairs in length and encoded a predicted 690 amino-acid protein. The gH contained characteristics of a transmembrane glycoprotein including 10 consensus N-linked glycosylation sites, 12 cysteine residues, a potential amino-terminal signal sequence and a predicted transmembrane segment located near the carboxyl terminus. The gL ORF was 738 base pairs in length and encoded a predicted 246 amino-acid protein. Four possible N-glycosylation sites and 6 cysteine residues existed within gL. The predicted amino-acid sequences of the HHV-7 gH and human herpesvirus 6 variant A (HHV 6A) gH gene products exhibited 23.6% identity to each other, and those of the gL gene products had 26.0% identity. Upon in vitro translation of the gL gene, the addition of microsomal membranes resulted in two modified products with molecular weights of 32kDa and 35kDa from the unmodified initial translation product of 26kDa. An amino-terminal portion of gH and the full length of gL were expressed as glutathione S-transferase fusion proteins, and these proteins were used to raise immune sera in mice. Lysates of cells infected with HHV-7 were subjected to immunoprecipitation analysis. Approximate molecular weights of 33, 37, 80 and 90kDa polypeptides were immunoprecipitated with antibodies against the gH protein. Antibodies against the gL protein polypeptides with the same molecular weights were also precipitated, and were observed with the antibodies against the gH protein. These results suggest that HHV-7 gH and gL may form a heterodimeric complex with each other in HHV 7 infected cells, as has been reported for other herpesviruses.
収録刊行物
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- MICROBIOLOGY and IMMUNOLOGY
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MICROBIOLOGY and IMMUNOLOGY 41 (1), 43-50, 1997
Center For Academic Publications Japan
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詳細情報 詳細情報について
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- CRID
- 1571980078011891584
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- NII論文ID
- 130003484429
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- ISSN
- 03855600
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- 本文言語コード
- en
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- データソース種別
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- CiNii Articles