Document 3296
 DOCN  M94A3296
 TI    Assembly of human immunodeficiency virus matrix protein.
 DT    9412
 AU    Morikawa Y; Kishi T; Nermut M; Hockley D; Jones I; Kitasato Institute,
       Tokyo, Japan.
 SO    Int Conf AIDS. 1994 Aug 7-12;10(1):109 (abstract no. PA0056). Unique
       Identifier : AIDSLINE ICA10/94369279
 AB    OBJECTIVE: To investigate the oligomeric state of p17 matrix protein
       following expression in E. coli and recombinant baculoviruses. To
       identify the residues involved in oligomerisation and gag assembly.
       METHODS: p17 protein was expressed in E. coli and its oligomeric state
       was examined in vitro. Site-directed mutagenesis was used to modify
       cysteine residues in p17 and the mutant forms were similarly expressed
       and characterised. p17 mutations were also expressed in baculoviruses
       and their ability to assemble and secret antigen was assessed. RESULTS:
       Wild type p17 protein was found as monomer to hexamer forms on
       non-reducing SDS-PAGE. Mutations in either Cys57 to Ser or Cys87 to Ser
       led to the production of only monomers and dimers. Mutations in both
       residues prevented any oligomerisation. Expression of p17 in
       baculoviruses also showed oligomeric assembly to hexamers and was
       secreted. Cys mutations expressed in this system did not secret gag
       antigen. DISCUSSION AND CONCLUSIONS: p17 protein assembles to hexameric
       form via inter-subunit disulfide bond. The hexameric form may be the
       basic unit of gag assembly that leads to virion formation.
 DE    Baculoviridae/GENETICS  Escherichia coli/GENETICS  Gene Expression  Gene
       Products, gag/CHEMISTRY/GENETICS/*METABOLISM  Human  HIV/GROWTH &
       DEVELOPMENT/GENETICS/*METABOLISM  HIV
       Antigens/CHEMISTRY/GENETICS/*METABOLISM  In Vitro  Mutagenesis,
       Site-Directed  Protein Conformation  Viral Matrix
       Proteins/CHEMISTRY/GENETICS/*METABOLISM  MEETING ABSTRACT

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