Document 0492
 DOCN  M9480492
 TI    Single amino acid changes in the human immunodeficiency virus type 1
       matrix protein block virus particle production.
 DT    9410
 AU    Freed EO; Orenstein JM; Buckler-White AJ; Martin MA; Laboratory of
       Molecular Microbiology, National Institute of; Allergy and Infectious
       Diseases, Bethesda, Maryland 20892.
 SO    J Virol. 1994 Aug;68(8):5311-20. Unique Identifier : AIDSLINE
       MED/94309204
 AB    The matrix protein of human immunodeficiency virus type 1 is encoded by
       the amino-terminal portion of the Gag precursor and is postulated to be
       involved in a variety of functions in the virus life cycle. To define
       domains and specific amino acid residues of the matrix protein that are
       involved in virus particle assembly, we introduced 35 amino acid
       substitution mutations in the human immunodeficiency virus type 1 matrix
       protein. Using reverse transcriptase and radioimmunoprecipitation
       analyses and transmission electron microscopy, we assessed the mutants
       for their ability to form virus particles and to function in the
       infection process. This study has identified several domains of the
       matrix protein in which single amino acid substitutions dramatically
       reduce the efficiency of virus particle production. These domains
       include the six amino-terminal residues of matrix, the region of matrix
       between amino acids 55 and 59, and the region between amino acids 84 and
       95. Single amino acid substitutions in one of these domains (between
       matrix amino acids 84 and 88) result in a redirection of the majority of
       virus particle formation to sites within cytoplasmic vacuoles.
 DE    Amino Acid Sequence  Cell Line  Gene Products, gag/*CHEMISTRY/PHYSIOLOGY
       Hela Cells  Human  HIV Antigens/*CHEMISTRY/PHYSIOLOGY
       HIV-1/CHEMISTRY/*PHYSIOLOGY/ULTRASTRUCTURE  Microscopy, Electron
       Molecular Sequence Data  Mutagenesis, Insertional  Protein
       Precursors/CHEMISTRY  Radioimmunoprecipitation Assay  Virus
       Replication/PHYSIOLOGY  JOURNAL ARTICLE

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