P. BhattarakosolC. YoosookA. CrossMahidol UniversityMedical Research Council2018-06-142018-06-141990-03-01Archives of Virology. Vol.115, No.1-2 (1990), 89-10014328798030486082-s2.0-0025002145https://repository.li.mahidol.ac.th/handle/20.500.14594/15958Monoclonal antibodies (MAbs) to herpes simplex virus (HSV) glycoproteins gD, gG, gB, and gE were used to analyze antigenic variations of 128 genital HSV-2 isolates by an indirect enzyme-linked immunosorbent assay (ELISA). Isolates were considered significantly different from the standard HSV-2 strain 186 when their optical density (OD) in ELISA was less than half that of strain 186. This criterion gave 30 patterns of reactivity among the genital HSV-2 isolates. The MAbs to gB, gG, and 2 of the gD antibodies reacted with more than 90% of the isolates, suggesting that these MAbs recognized highly conserved epitopes. However, the gE MAb reacted with only 47% of the isolates, and one of the gD antibodies with only 39%. Thus, HSV-2 can readily tolerate modifications in some parts of the gD and gE molecules while remaining infectious. © 1990 Springer-Verlag.Mahidol UniversityImmunology and MicrobiologyArticleSCOPUS10.1007/BF01310625