Redistribution of Mr 75,000 plasma membrane protein, cytovillin, into newly formed microvilli in herpes simplex and Semliki Forest virus infected human embryonal fibroblasts.

We have previously purified an Mr 75,000 protein from cultured human JEG-3 choriocarcinoma cells and showed that this protein is specifically confined to the cytoplasmic side of JEG-3 microvillar membranes. Recently, the Mr 75,000 protein, designated as cytovillin, was found to be expressed also in several other cultured human cell lines and strains, in which it was detected in microvillus-related structures. We now demonstrate the redistribution of cytovillin in herpes simplex type 1 (HSV-1) and Semliki Forest virus (SFV) infected human embryonal fibroblasts. Virus infection induced rapidly numerous microvilli on the apical cell surfaces, and cytovillin was enriched into these newly formed structures as shown by indirect immunofluorescence and immunoferritin electron microscopy. In mock-infected cells treated with the anti-cytovillin antibodies a small amount of ferritin particles and faint fluorescence was detected along the smooth plasma membrane. Only occasional cell surface protrusions were observed in these cells. The enrichment of the cytovillin was first seen 2 h after infection. The isoelectric point (IP) and the mobility of the cytovillin polypeptide in sodium dodecyl sulfate polyacrylamide gel electrophoresis was not altered after this redistribution, suggesting that the protein was not significantly modified during infection. Five RNA+ SFV mutants (ts-1, ts-2, ts-3, ts-5, ts-7) with temperature-sensitive defects in processing and transport of viral envelope glycoproteins to the plasma membrane induced microvilli at the restrictive temperature (39 degrees C) as the wild type virus.(ABSTRACT TRUNCATED AT 250 WORDS)