@article{mbs:/content/journal/jgv/10.1099/0022-1317-71-2-455, author = "Kikuchi, Gary E. and Glorioso, Joseph C. and Nairn, Roderick", title = "Cross-linking studies show that herpes simplex virus type 1 glycoprotein C molecules are clustered in the membrane of infected cells", journal= "Journal of General Virology", year = "1990", volume = "71", number = "2", pages = "455-458", doi = "https://doi.org/10.1099/0022-1317-71-2-455", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-71-2-455", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "Chemical cross-linking using ethylene glycol succinimi- dyl succinate (EGS) and dithiobispropionimidate (DTBP) was performed to determine the association of herpes simplex virus type 1 glycoprotein C (HSV-1 gC) with its nearest neighbours. Human embryonic lung (HEL) cells were infected with HSV-1 strain KOS, treated with EGS, lysed with Nonidet P40, immuno- precipitated with monoclonal antibodies specific for gC, and analysed by SDS-PAGE. These analyses demonstrated the presence of cross-linked complexes that migrated with an apparent M r in the range 150000 to 260000. Two-dimensional SDS-PAGE (non-reduced and then reduced) analyses of HSV-1-infected HEL cells treated with the cleavable cross-linker DTBP demonstrated that molecules that comigrated with gC were the only components of these high M r complexes. Immunoelectroblot (Western blot) analyses using polyclonal rabbit antiserum specific for gC verified that the high M r complexes contained gC. These results indicated that gC molecules may be localized in the infected cell membrane as dimers.", }