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Immunologic and proteolytic analysis of HIV-1 reverse transcriptase structure.

A L Ferris1, A Hizi, S D Showalter

  • 1BRI-Basic Research Program, NCI-Frederick Cancer Research Facility, Maryland 21701.

Virology
|April 1, 1990
PubMed
Summary

The HIV-1 viral protease precisely cleaves the 66-kDa reverse transcriptase to the 51-kDa form, generating the active enzyme found in virions. This specific cleavage avoids further degradation, highlighting its biological significance.

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Area of Science:

  • Biochemistry
  • Virology
  • Molecular Biology

Background:

  • Human Immunodeficiency Virus type 1 (HIV-1) virions contain two key reverse transcriptase (RT) polypeptides: a 66-kDa precursor and a 51-kDa product.
  • The 51-kDa RT form is a truncated version of the 66-kDa form, lacking carboxy-terminal sequences and is thought to result from proteolytic processing.

Purpose of the Study:

  • To investigate the proteolytic processing of the 66-kDa HIV-1 reverse transcriptase.
  • To identify which proteases can generate the 51-kDa form and to map the cleavage sites recognized by specific monoclonal antibodies.

Main Methods:

  • Purified 66-kDa HIV-1 reverse transcriptase was treated with various viral and nonviral proteases.
  • Digestion products were analyzed using monoclonal antibodies targeting specific segments of the RT.

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  • Antibody binding to truncated RT forms helped map antibody recognition sites.

    • Main Results:

    • The viral protease was uniquely capable of cleaving the 66-kDa RT to the 51-kDa form without generating additional cleavage products.
    • Monoclonal antibody mapping revealed that recognized segments are not uniformly distributed and likely reside on the surface of the folded RT.

    Conclusions:

    • HIV-1 viral protease is responsible for producing the 51-kDa reverse transcriptase in virions through specific cleavage of the 66-kDa precursor.
    • The specific and limited cleavage by the viral protease suggests a controlled maturation process within the virion.