Document 0584
 DOCN  M9550584
 TI    Virion incorporation of envelope glycoproteins with long but not short
       cytoplasmic tails is blocked by specific, single amino acid
       substitutions in the human immunodeficiency virus type 1 matrix.
 DT    9505
 AU    Freed EO; Martin MA; Laboratory of Molecular Microbiology, National
       Institute of; Allergy and Infectious Diseases, Bethesda, Maryland
       20892-0460.
 SO    J Virol. 1995 Mar;69(3):1984-9. Unique Identifier : AIDSLINE
       MED/95156639
 AB    Incorporation of envelope glycoproteins into a budding retrovirus is an
       essential step in the formation of an infectious virus particle. By
       using site-directed mutagenesis, we identified specific amino acid
       residues in the matrix domain of the human immunodeficiency virus type 1
       (HIV-1) Gag protein that are critical to the incorporation of HIV-1
       envelope glycoproteins into virus particles. Pseudotyping analyses were
       used to demonstrate that two heterologous envelope glycoproteins with
       short cytoplasmic tails (the envelope of the amphotropic murine leukemia
       virus and a naturally truncated HIV-2 envelope) are efficiently
       incorporated into HIV-1 particles bearing the matrix mutations.
       Furthermore, deletion of the cytoplasmic tail of HIV-1 transmembrane
       envelope glycoprotein gp41 from 150 to 7 or 47 residues reversed the
       incorporation block imposed by the matrix mutations. These results
       suggest the existence of a specific functional interaction between the
       HIV-1 matrix and the gp41 cytoplasmic tail.
 DE    Cytoplasm  Gene Products, gag/*METABOLISM  Hela Cells  Human  HIV
       Envelope Protein gp41/METABOLISM  HIV-1/*ULTRASTRUCTURE
       HIV-2/ULTRASTRUCTURE  Leukemia Viruses, Murine/ULTRASTRUCTURE
       Morphogenesis  Mutagenesis, Site-Directed  Sequence Deletion
       Structure-Activity Relationship  Viral Envelope Proteins/*METABOLISM
       Virion/METABOLISM  Virus Replication  JOURNAL ARTICLE

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