PMID: 8982360Dec 15, 1996Paper

Human antibodies responsible for binding inhibition and polymerization inhibition of human immunodeficiency virus type 1 reverse transcriptase

Journal of Immunological Methods
F OdawaraM Nakai

Abstract

Using a solid-phase non-radioisotopic (non-RI) reverse transcriptase (RT) assay, antibodies inhibiting human immunodeficiency virus type 1 (HIV-1) RT activity (RTI antibody) were investigated for their ability to inhibit binding of RT to a template-primer and DNA polymerization. The RTI antibody inhibited the binding of RT to the template-primer (BI antibody), and directly reacted with the RT-template-primer complex and inhibited enzymatic activity (PI antibody). The RTI antibody interfered with formation of the RT-template-primer complex suggesting that it recognized the antigenic site involved in template-primer binding of RT molecules. Since deoxynucleotide triphosphates (dNTPs) blocked inhibition of the RT activity by the PI antibody, the antigenic site recognized by the PI antibody may be closely related to the dNTP binding site. The seropositivities of the BI and PI antibodies were 84.6% and 91.2%, respectively, in HIV-1-infected individuals; healthy individuals, HTLV-I-positive individuals, autoimmune disease patients and leukemia patients were all seronegative. No significant correlation of residual RT activities was observed when BI and PI antibodies were compared (r = 0.688). It is possible that the epitopes recognize...Continue Reading

References

Feb 1, 1988·AIDS Research and Human Retroviruses·A L DeVicoM G Sarngadharan
May 1, 1995·Journal of Acquired Immune Deficiency Syndromes and Human Retrovirology : Official Publication of the International Retrovirology Association·B Grimison, J Laurence

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Citations

Oct 9, 2002·Journal of Virological Methods·Fumitomo OdawaraKouichi Sano
Mar 30, 2017·Antimicrobial Agents and Chemotherapy·Christine Cruz-OliveiraAndrea T Da Poian
May 8, 2014·The Journal of Biological Chemistry·Jordan D DimitrovSébastien Lacroix-Desmazes

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