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