Human immunodeficiency virus type-1 envelope glycoprotein gp120 induces expression of fusion regulatory protein (FRP)-1/CD98 on CD4+ T cells: a possible ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-04

AUTHORS

Shigeru Suga, Masato Tsurudome, Masahiro Ito, Shinji Ohgimoto, Nobutada Tabata, Machiko Nishio, Mitsuo Kawano, Hiroshi Komada, Morihiro Ito, Minoru Sakurai, Y. Ito

ABSTRACT

Syncytium formation is one of major cytopathic effects of human immunodeficiency virus (HIV) infection, and requires the interaction of CD4 molecules on uninfected cells with HIV envelope glycoprotein gp120 expressed on HIV-infected cells. Recent evidence suggests chemokine receptors function as fusion cofactors. We have recently found that fusion regulatory protein (FRP)-1/ CD98 is involved in syncytium formation of HIV gp160-expressing U2ME-7 cells and TALL-1 cells persistently infected with HIV. However, resting lymphocytes were found to express no FRP-1 molecule. In this study, we demonstrated that recombinant gp120 (rpg120) has the ability to induce expression of FRP-1 on peripheral blood mononuclear cells (PBMC). Three-color flow cytometric analysis showed that rgp120-induced FRP-1 was expressed selectively on CD4+ T cells in a dose-dependent manner. FRP-1 expression level was maximum 3 days after addition of rgp120. Anti-CD4 and anti-gp120 antibodies blocked rgp120-induced FRP-1 expression. Co-cultivation of PBMC with HIV-1 gp160-expressing HeLa cells also resulted in the increased expression of FRP-1 on T cells. These results suggest that FRP-1 molecules are induced on CD4+ T cells via CD4-gp120 interaction and may play an important role in regulation of HIV-induced syncytium formation. More... »

PAGES

237-243

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s004300050036

DOI

http://dx.doi.org/10.1007/s004300050036

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005549211

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9138296


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