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A truncated HTLV-I envelope protein, lacking the hydrophobic membrane anchor domain, is associated with cellular membranes and virions.
Carrington CV; Weiss RA; Schulz TF; Chester Beatty Laboratories,
September 30, 1994
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