Computer predictions of antigenic domains in herpes simplex virus types 1 and 2 glycoprotein D as compared with experimentally proven domains.
The primary amino-acid sequence of the glycoprotein D (gD) of herpes simplex virus types 1 and 2 (HSV-1, HSV-2) was analyzed by computer programs that provided values for hydrophilicity, surface probability, flexibility, and antigenicity, as well as the secondary structure conformation. Putative antigenic domains with a high hydrophilicity, surface probability, and antigenicity index were determined and compared with the reported antigenic domains in HSV-1 and HSV-2 gD protein based on experimental data. The major experimentally proven antigenic domains were detected by the computer analyses. Additional putative antigenic domains with potential for the synthesis of antigenic viral peptides were determined.
Becker
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Department of Molecular Virology, Faculty of Medicine, Hebrew University of Jerusalem, Israel.
D000595:Amino Acid Sequence; D000956:Antigens, Viral / Q000276:immunology*; D000939:Epitopes / Q000276:immunology; D008969:Molecular Sequence Data; D011487:Protein Conformation; D018139:Simplexvirus / Q000737:chemistry / Q000276:immunology*; D012984:Software; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000276:immunology*
D000956:Antigens, Viral; D000939:Epitopes; D014759:Viral Envelope Proteins; C039447:glycoprotein D, Human herpesvirus 1; C040570:glycoprotein D-herpes simplex virus type 2