Document 0201
 DOCN  M9440201
 TI    Role of the matrix protein in the virion association of the human
       immunodeficiency virus type 1 envelope glycoprotein.
 DT    9404
 AU    Dorfman T; Mammano F; Haseltine WA; Gottlinger HG; Division of Human
       Retrovirology, Dana-Farber Cancer Institute,; Boston, Massachusetts
       02115.
 SO    J Virol. 1994 Mar;68(3):1689-96. Unique Identifier : AIDSLINE
       MED/94149861
 AB    The matrix (MA) protein of human immunodeficiency virus type 1 (HIV-1)
       forms an inner coat directly underneath the lipid envelope of the
       virion. The outer surface of the lipid envelope surrounding the capsid
       is coated by the viral Env glycoproteins. We report here that the HIV-1
       capsid-Env glycoprotein association is very sensitive to minor
       alterations in the MA protein. The results indicate that most of the MA
       domain of the Gag precursor, except for its carboxy terminus, is
       essential for this association. Viral particles produced by proviruses
       with small missense or deletion mutations in the region coding for the
       amino-terminal 100 amino acids of the MA protein lacked both the surface
       glycoprotein gp120 and the transmembrane glycoprotein gp41, indicating a
       defect at the level of Env glycoprotein incorporation. Alterations at
       the carboxy terminus of the MA domain had no significant effect on the
       levels of particle-associated Env glycoprotein or on virus replication.
       The presence of HIV-1 MA protein sequences was sufficient for the stable
       association of HIV-1 Env glycoprotein with hybrid particles that contain
       the capsid (CA) and nucleocapsid (NC) proteins of visna virus. The
       association of HIV-1 Env glycoprotein with the hybrid particles was
       dependent upon the presence of the HIV-1 MA protein domain, as HIV-1 Env
       glycoprotein was not efficiently recruited into virus particles when
       coexpressed with authentic visna virus Gag proteins.
 DE    Cells, Cultured  DNA Mutational Analysis  Gene Products, env/*METABOLISM
       Human  HIV-1/*GROWTH & DEVELOPMENT/GENETICS/ULTRASTRUCTURE
       Morphogenesis  Protein Binding  RNA, Viral/METABOLISM
       Structure-Activity Relationship  Support, Non-U.S. Gov't  Support, U.S.
       Gov't, P.H.S.  Viral Matrix Proteins/GENETICS/*METABOLISM
       Virion/*GROWTH & DEVELOPMENT/GENETICS/ULTRASTRUCTURE  JOURNAL ARTICLE

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