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(K15R M52E) aprotinin is a weak Kunitz-type inhibitor of HIV-1 replication in H9 cells

E A Auerswald1, A Schubert, M Dolinar

  • 1Abteilung für Klinische Chemie, Universität München, FRG.

Biomedica Biochimica Acta
|January 1, 1991
PubMed

Insights

A novel recombinant aprotinin variant, (K15R M52E), effectively inhibits serine proteinases and reduces human immunodeficiency virus type 1 (HIV-1) replication in cell cultures.

Area of Science:

  • Biochemistry
  • Virology
  • Molecular Biology

Background:

  • Native aprotinin is a serine proteinase inhibitor.
  • Recombinant protein engineering can enhance inhibitor properties.
  • Human immunodeficiency virus type 1 (HIV-1) replication is a target for therapeutic intervention.

Purpose of the Study:

  • To characterize a recombinant aprotinin variant, (K15R M52E).
  • To assess the efficacy of (K15R M52E) aprotinin in inhibiting HIV-1 replication.

Main Methods:

  • Production and purification of recombinant (K15R M52E) aprotinin in E. coli.
  • Enzyme-linked immunosorbent assay (ELISA) to quantify HIV-1 core protein p24.
  • In vitro testing of (K15R M52E) aprotinin on HIV-1 replication in H9 cells.

Main Results:

  • The recombinant (K15R M52E) aprotinin demonstrated a broader inhibition spectrum and higher affinity for certain serine proteinases compared to native aprotinin.
  • A concentration of 50 microM of (K15R M52E) aprotinin significantly reduced HIV-1 replication.
  • HIV-1 core protein p24 levels were decreased, indicating reduced viral load.

Conclusions:

  • The engineered (K15R M52E) aprotinin variant shows promising potential as an antiviral agent.
  • This recombinant aprotinin effectively inhibits HIV-1 replication in vitro.
  • Further research into (K15R M52E) aprotinin as an anti-HIV therapeutic is warranted.

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