Characterization of Glycoprotein H and L of Human Herpesvirus 7

作者: Tetsu Mukai , Atsuko Hata , Yuji Isegawa , Koichi Yamanishi

DOI: 10.1111/J.1348-0421.1997.TB01171.X

关键词: Signal peptideTransmembrane domainBiologyImmunoprecipitationOpen reading frameGlycoproteinFusion proteinMolecular biologyGeneGlycosylationImmunologyMicrobiologyVirology

摘要: The genes encoding the glycoproteins H (gH) and L (gL) of human herpesvirus 7 (HHV-7) have been identified. gH open reading frame (ORF) was 2,070 base pairs in length encoded a predicted 690 amino-acid protein. contained characteristics transmembrane glycoprotein including 10 consensus N-linked glycosylation sites, 12 cysteine residues, potential amino-terminal signal sequence segment located near carboxyl terminus. gL ORF 738 246 Four possible N-glycosylation sites 6 residues existed within gL. sequences HHV-7 variant A (HHV-6A) gene products exhibited 23.6% identity to each other, those had 26.0% identity. Upon vitro translation gene, addition microsomal membranes resulted two modified with molecular weights 32 kDa 35 from unmodified initial product 26 kDa. An portion full were expressed as glutathione S-transferase fusion proteins, these proteins used raise immune sera mice. Lysates cells infected subjected immunoprecipitation analysis. Approximate 33, 37, 80 90 polypeptides immunoprecipitated antibodies against Antibodies protein same also precipitated, observed These results suggest that may form heterodimeric complex other cells, has reported for herpesviruses.

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