       Document 0659
 DOCN  M9640659
 TI    Substitution of a single amino acid residue is sufficient to allow the
       human amphotropic murine leukemia virus receptor to also function as a
       gibbon ape leukemia virus receptor.
 DT    9604
 AU    Eiden MV; Farrell KB; Wilson CA; Laboratory of Cell Biology, National
       Institute of Mental Health,; Bethesda, Maryland 20892, USA.
 SO    J Virol. 1996 Feb;70(2):1080-5. Unique Identifier : AIDSLINE
       MED/96135221
 AB    We have previously reported the unique properties of a receptor for
       amphotropic murine leukemia viruses (A-MuLVs) expressed on Chinese
       hamster E36 cells (C.A. Wilson, K.B. Farrell, and M.V. Eiden, J. Virol.
       68:7697-7703, 1994). This receptor, HaPiT2 (formerly designated EAR), in
       contrast to the human form of the A-MuLV receptor (PiT2), functions as a
       receptor not only for A-MuLVs but also for gibbon ape leukemia virus
       (GALV). Comparison of the deduced amino acid sequences of the HaPiT2 and
       PiT2 proteins suggested that differences in the amino acid composition
       of the extracellular region(s) of the hamster and human proteins account
       for their functional differences. We substituted extracellular regions
       of HaPiT2 for those of PiT2 to map the region of the HaPiT2 protein
       required for GALV receptor function. Only those PiT2-HaPiT2 chimeric
       receptors containing the fourth and fifth extracellular regions of
       HaPiT2 functioned as GALV receptors. We have now determined that the
       substitution of a single amino acid residue, glutamic acid, for the
       lysine residue at position 522 in the fourth extracellular region of the
       PiT2 protein is sufficient to render PiT2 functional as a GALV receptor.
 DE    Amino Acid Sequence  Animal  Binding Sites  Cell Line  Cricetulus  CHO
       Cells  Glutamic Acid/*METABOLISM  Hamsters  Human  Leukemia Virus,
       Feline/PATHOGENICITY  Leukemia Virus, Gibbon Ape/*METABOLISM  Leukemia
       Viruses, Murine/*METABOLISM  Lysine/*METABOLISM  Molecular Sequence Data
       Receptors, Virus/CHEMISTRY/*METABOLISM  Structure-Activity Relationship
       JOURNAL ARTICLE

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

