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Human immunodeficiency virus type 1 KK26-27 matrix mutants display impaired infectivity, circularization and

Abdelkrim Mannioui1, Elisabeth Nelson, Cecile Schiffer

  • 1UMR 7151 Centre National de la Recherche Scientifique-Université Paris 7, 75010 Paris, France. karim.mannioui@chu-stlouis.fr

Virology
|June 21, 2005
PubMed

Insights

Human immunodeficiency virus (HIV)-1 matrix protein (MA) plays a key role in viral replication post-chromatin binding. Mutations in MA

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • The human immunodeficiency virus (HIV)-1 matrix protein (MA) is crucial for viral replication.
  • Understanding the specific roles of MA during different stages of the viral lifecycle is essential for developing effective antiviral strategies.

Purpose of the Study:

  • To investigate the function of the HIV-1 matrix protein (MA) during the afferent phase of viral replication.
  • To determine the role of MA residues 26-27 within the nuclear localization signal (NLS)-1 in HIV-1 infectivity and nuclear import.

Main Methods:

  • Single-round infection of H9 T lymphocytes.
  • Analysis of viral DNA forms, including 2-LTR-circles.
  • Assessment of viral DNA docking to chromatin in interphasic and mitotic cells.

Main Results:

  • Combined mutation of MA Lys residues 26-27 in NLS-1 impaired HIV-1 infectivity.
  • Mutations abrogated 2-LTR-circle formation and significantly reduced viral integration.
  • The mutation did not affect viral DNA docking to chromatin, suggesting MA is not a major determinant of nuclear import.

Conclusions:

  • The HIV-1 matrix protein (MA) plays a previously unreported role in the late, post-chromatin-binding afferent phase of HIV-1 replication.
  • MA's N-terminal basic domain is not a major determinant of HIV-1 nuclear import in T lymphocytes.

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