Document 0785
 DOCN  M9590785
 TI    Identification and characterization of the viral interaction determinant
       of the subgroup A avian leukosis virus receptor.
 DT    9509
 AU    Zingler K; Belanger Ca; Peters R; Agard E; Young JA; Gladstone Institute
       of Virology and Immunology, University of; California School of
       Medicine, San Francisco 94141-9100, USA.
 SO    J Virol. 1995 Jul;69(7):4261-6. Unique Identifier : AIDSLINE
       MED/95287479
 AB    The cellular receptor for subgroup A avian leukosis viruses (ALV-A) has
       a small, 83-amino-acid extracellular domain containing a motif that is
       related in sequence to the ligand binding repeats of the low-density
       lipoprotein receptor. Extensive mutagenesis of the ALV-A receptor has
       identified two acidic amino acids (Asp-46 and Glu-47) and an adjacent
       aromatic amino acid (Trp-48) in the carboxy-terminal portion of this
       low-density lipoprotein receptor-related motif that are crucial for
       efficient viral entry. In addition, a 19-amino-acid peptide derived from
       this region efficiently and specifically blocked subgroup A viral
       infection when oxidized to form a disulfide bond previously predicted to
       form in the native receptor (C. Belanger, K. Zingler, and J. A. T.
       Young, J. Virol. 69:1019-1024, 1995). Thus, the charged and aromatic
       amino acid determinants that are required for viral infection appear to
       lie on a small loop region of the ALV-A receptor. Previously, a single
       aromatic and one or more charged residues on the CD4 receptor for human
       and simian immunodeficiency viruses, and the MCAT receptor for ecotropic
       murine leukemia viruses, were shown to be important for viral entry.
       These results suggest that different retroviruses may recognize related
       determinants on structurally divergent cellular receptors.
 DE    Amino Acid Sequence  Animal  Antigens, CD4/PHYSIOLOGY  Cells, Cultured
       Chick Embryo  Molecular Sequence Data  Mutagenesis, Site-Directed
       Peptide Fragments/PHYSIOLOGY  Receptors, Virus/*PHYSIOLOGY
       Retroviruses, ALV-Related/*PHYSIOLOGY  Structure-Activity Relationship
       Support, Non-U.S. Gov't  Support, U.S. Gov't, P.H.S.  JOURNAL ARTICLE

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