Document 0146
 DOCN  M9480146
 TI    Identification of functional sites on bovine leukemia virus envelope
       glycoproteins using structural and immunological data.
 DT    9410
 AU    Callebaut I; Portetelle D; Burny A; Mornon JP; Departement des
       Macromolecules Biologiques--Laboratoire de;
       Mineralogie-Cristallographie, CNRS URA09, Universites Paris,; France.
 SO    Eur J Biochem. 1994 Jun 1;222(2):405-14. Unique Identifier : AIDSLINE
       MED/94291634
 AB    Sequence analysis using the sensitive hydrophobic cluster analysis
       method shows that the bovine leukemia virus envelope glycoproteins
       conserve the general organization of the influenza hemagglutinin into a
       'stem', containing the external part of the transmembrane glycoprotein
       and the N-terminal and C-terminal parts of the external glycoprotein,
       and a 'head', containing only external glycoprotein residues. However,
       our analysis suggests, for the first time, that the bovine leukemia
       virus envelope head will not adopt the typical 'jelly-roll' fold of the
       influenza A hemagglutinin head, but most likely folds into another type
       of 'Greek-key' structure corresponding to the overall topology of
       constant immunoglobulin domains. We constructed a three-dimensional
       model for the bovine leukemia virus envelope head by homology modeling
       using the crystal structure of the human histocompatibility antigen
       HLA-A2 alpha 3 domain. Furthermore, we propose a general model for the
       oligomeric organization of this head, based on the hemagglutinin trimer.
       The proposed structural organization of bovine leukemia virus external
       glycoprotein is further supported by antipeptide and monoclonal antibody
       reactivities. Our modeling study suggests that the loops of the two
       neutralizing peptides located in the head are adjacent at the top of the
       domain and define a potential interaction site of the external
       glycoprotein with its cellular receptor. This site is topologically
       similar to the binding site of hemagglutinin with its cellular receptor,
       sialic acid. The other neutralizing peptides are located within a small
       domain linking the head to the stem. These data are of interest for
       defining other oncoviral glycoproteins heads and receptor-binding sites.
 DE    Amino Acid Sequence  Comparative Study  Glycoproteins/*CHEMISTRY  Human
       HLA-A2 Antigen/CHEMISTRY  HTLV-I/CHEMISTRY  Lentivirus/CHEMISTRY
       Leukemia Virus, Bovine/*CHEMISTRY  Models, Structural  Molecular
       Sequence Data  Orthomyxoviruses Type A/CHEMISTRY  *Protein Conformation
       *Protein Structure, Secondary  Retroviridae/*CHEMISTRY  Sequence
       Homology, Amino Acid  Support, Non-U.S. Gov't  Viral Envelope
       Proteins/*CHEMISTRY  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
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