Localization of epitopes of herpes simplex virus type 1 glycoprotein D.

作者: R J Eisenberg , D Long , M Ponce de Leon , J T Matthews , P G Spear

DOI: 10.1128/JVI.53.2.634-644.1985

关键词: AntibodyGlycoproteinProtein secondary structureAmino acidBiologyProtein structureLinear epitopeMolecular biologyEpitopeMonoclonal antibody

摘要: We previously defined eight groups of monoclonal antibodies which react with distinct epitopes herpes simplex virus glycoprotein D (gD). One these, group VII antibody, was shown to a type-common continuous epitope within residues 11 19 the mature (residues 36 44 predicted sequence gD). In current investigation, we have localized sites binding two additional antibody recognize gD. The use truncated forms gD as well computer predictions secondary structure and hydrophilicity were instrumental in locating these choosing synthetic peptides mimic their reactivity. Group II antibodies, are type common, an 268 287 293 312 sequence). V gD-1 specific, 340 356 protein 365 381 Four appear discontinuous gD-1, since reactivity lost when denatured by reduction alkylation. Truncated used localize four first 260 amino acids protein. Competition experiments assess relative positions various pairs antibodies. several cases, one bound, there no interference from another group, indicating that distinct. However, other competition, might share some common acids.

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