RNase Inhibition of Human Immunodeficiency Virus Infection of H9 Cells

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 91; no. 13; pp. 6012 - 6016
• Main Authors: Youle, Richard J., Wu, You-Neng, Mikulski, Stanislaw M., Shogen, Kuslima, Hamilton, Rebecca S., Newton, Dianne, D'Alessio, Giuseppe, Gravell, Maneth
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 21.06.1994; National Acad Sciences; National Academy of Sciences
• Subjects: Animals; Antigens; Antineoplastic Agents - toxicity; Antiviral Agents - toxicity; Antivirals; Cattle; Cell aggregates; Cell culture techniques; Cell Line; Cell lines; Cell Survival - drug effects; Cellular biology; Dose-Response Relationship, Drug; Egg Proteins - toxicity; HIV; HIV 1; HIV-1 - drug effects; HIV-1 - physiology; Human immunodeficiency virus; Humans; Infections; Kinetics; Leukemia; Male; Medical research; Neurons; Ribonuclease, Pancreatic - toxicity; Ribonucleases - toxicity; Semen - enzymology; Time Factors; Tumor Cells, Cultured; Ungulates; Virus Replication - drug effects
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.91.13.6012

Onconase and bovine seminal RNase, two members of the RNase A superfamily, inhibit human immunodeficiency virus type 1 replication in H9 leukemia cells 90-99.9% over a 4-day incubation at concentrations not toxic to uninfected H9 cells. Two other members of the same protein family, bovine pancreatic RNase A and human eosinophil-derived neurotoxin, have no detectable antiviral activity, demonstrating a strikingly selective antiviral activity among homologous ribonucleases. The antiviral RNases do not appear to affect viral particles directly but inhibit replication in host cell cultures. Onconase, already in clinical trials for cancer therapy, and bovine seminal RNase have potential as antiviral therapeutics.