The nucleotide sequence of the glycoprotein E gene of herpes simplex virus type 2 and its structural characteristics in comparison with the gE of herpes simplex virus type 1
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- The nucleotide sequence of the glycoprotein E gene of herpes simplex virus type 2 and its structural characteristics in comparison with the gE of herpes simplex virus type 1
- See Young Choi; Young Rim Seong; Eun Kyung Lee; Seung Ki Chon; Wangdon Yoo; Chong-Kyo Lee; Dong Soo Im
- Bibliographic Citation
- Molecules and Cells, vol. 6, no. 2, pp. 145-152
- Publication Year
- The nucleotide sequence of a 1.88-kb DNA cloned from the region of the herpes simplex virus type 2 (HSV-2) genome which maps colinearly with the HSV-1 glycoprotein E (gE1) gene has been determined. Contained within this sequence is a major open reading frame of 548 amino acids for the glycoprotein E of HSV-2 (gE2). The gE2 protein has an amino acid sequence homology of 74% with the cognate gE1 protein. In particular, the carboxy-terminal region of the gE2 protein shows a high degree of sequence homology to the gE1. Two putative N-linked glycosylation sites, a Fc binding motif, a phosphorylation site, and two clusters of cysteine residues are perfectly conserved in both the gE1 and gE2 proteins, suggesting that they may serve similar important functions in the life cycle of the herpesviruses in nature. An amino acid region, which is distinct from that of the gE1 protein in terms of amino acid composition, was found between amino acids 180 and 211 in the gE2 protein. That region, which appears to reside on the outer surface of the gE2 protein, may be an epitope to elicit a HSV-type specific antibody. In addition, a hydropathic analysis of the HSV-2 gE sequence demonstrates that the gE2 protein contains structures characteristic of membrane-bound glycoproteins, including an amino-terminal signal sequence and carboxy-terminal hydrophobic transmembrane domain.
- Korea Soc-Assoc-Inst
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