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NLM AIDSLINE

A truncated HTLV-I envelope protein, lacking the hydrophobic membrane anchor domain, is associated with cellular membranes and virions.




 

Virology. 1994 Jul;202(1):61-9. Unique Identifier : AIDSLINE

The HTLV-I producer cell line C10/MJ2 does not induce syncytium formation with HTLV-I receptor expressing cells. Here we show that this cell line produces a truncated envelope protein, which, because of a premature stop codon, lacks the hydrophobic membrane anchor domain of the transmembrane protein (TM). Despite lacking a membrane anchor this envelope protein is expressed on the cell surface and associated with released virions. However, its incorporation into virions seems less efficient than that of a full-length envelope glycoprotein and some of its released into the cell culture supernatant as soluble surface glycoprotein (SU)-TM complexes. Small amounts of such a truncated envelope glycoprotein were also found in the fusion-competent HTLV-I producer cell line MT2. Premature truncation of HTLV-I envelope proteins in producer cell lines may result from in vitro selection for a less fusogenic phenotype. The association of truncated HTLV-I envelope proteins with virions and cell surfaces may reflect interactions between the SU domain and cellular membranes, possibly with the cellular receptor for HTLV-I.

Amino Acid Sequence Base Sequence Cell Line Cell Membrane/*MICROBIOLOGY Codon DNA, Viral Genes, env Giant Cells/MICROBIOLOGY Human HTLV-I/IMMUNOLOGY/*METABOLISM Molecular Sequence Data Peptide Fragments/METABOLISM Support, Non-U.S. Gov't T-Lymphocytes/MICROBIOLOGY Viral Envelope Proteins/CHEMISTRY/*METABOLISM *Virion JOURNAL ARTICLE



 




Information in this article was accurate in September 30, 1994. The state of the art may have changed since the publication date. This material is designed to support, not replace, the relationship that exists between you and your doctor. Always discuss treatment options with a doctor who specializes in treating HIV.