Document 0538
 DOCN  M9460538
 TI    Structure and expression of the human T-cell leukemia virus type 1
       envelope protein.
 DT    9404
 AU    Paine E; Gu R; Ratner L; Department of Medicine, Washington University
       School of Medicine,; St. Louis, Missouri 63110.
 SO    Virology. 1994 Mar;199(2):331-8. Unique Identifier : AIDSLINE
       MED/94167867
 AB    The structure and expression of the HTLV-1 envelope protein was examined
       using T lymphoid cell lines infected with HTLV-1 and recombinant
       vaccinia viruses expressing the HTLV-1 envelope. Pulse-chase experiments
       demonstrated that the envelope precursor, gp62, had a half-life of 7-12
       hr. N-glycosylation of the precursor protein was examined using
       tunicamycin and endoglycosidase H. These studies revealed that at least
       four and possibly five potential N-glycosylation sites were utilized. In
       addition, the envelope precursor was found to sediment on sucrose
       gradients as high-molecular-weight complexes, in positions consistent
       with the formation of dimers and smaller amounts of higher multimeric
       forms. Finally, the recombinant vaccinia system was used to express
       mutants designed to analyze the role in HTLV-1 envelope processing of
       the cytoplasmic tail and the membrane-spanning domain.
 DE    Base Sequence  Biopolymers/BIOSYNTHESIS  Cell Line  Genes, env/GENETICS
       Glycosylation  Human  HTLV-I/*CHEMISTRY  Molecular Sequence Data
       Recombinant Proteins/BIOSYNTHESIS  Support, Non-U.S. Gov't  Support,
       U.S. Gov't, P.H.S.  Vaccinia Virus/METABOLISM  Viral Envelope
       Proteins/*BIOSYNTHESIS/*CHEMISTRY/METABOLISM  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).