Summary auto-generated
This study investigated the organizational structure of herpes simplex virus type 1 glycoprotein C (gC) in infected cell membranes using chemical cross-linking methods. Researchers infected human embryonic lung cells with HSV-1 and treated them with cross-linking reagents (EGS and DTBP) to identify protein-protein associations. Analysis by SDS-PAGE and immunoprecipitation revealed that gC forms cross-linked complexes with molecular weights of 150,000 to 260,000 Daltons. Two-dimensional gel electrophoresis with the cleavable cross-linker DTBP demonstrated that these complexes contained only gC molecules linked to themselves, not to other cellular or viral proteins. Western blot analysis confirmed gC presence in the cross-linked complexes. The findings suggest that gC exists as non-covalent homologous multimers or clusters in infected cell membranes, similar to glycoprotein B. However, unlike gB multimers which form stable covalent complexes, gC multimers appear less tightly bound. The clustering of these glycoproteins may facilitate virus attachment and entry into host cells, though the precise mechanism remains to be determined.
Key findings
- HSV-1 glycoprotein C (gC) forms cross-linked complexes of 150,000-260,000 Mr in infected cell membranes
- gC molecules are clustered as homologous multimers linked only to themselves, not to other viral or cellular proteins
- gC multimers are non-covalent associations, unlike the more stable covalent multimers formed by glycoprotein B
- Both gC and gB appear to be organized as homologous multimer clusters in infected cell membranes, potentially facilitating viral attachment and entry
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Abstract
Chemical cross-linking using ethylene glycol succinimidyl 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, immunoprecipitated 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 Mr in the range 150,000 to 260,000. 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 Mr complexes. Immunoelectroblot (Western blot) analyses using polyclonal rabbit antiserum specific for gC verified that the high Mr complexes contained gC. These results indicated that gC molecules may be localized in the infected cell membrane as dimers.