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A polymeric immunoglobulin receptor-like milk protein with inhibitory activity on human immunodeficiency virus type 1
1Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China.
Insights
A novel bovine milk protein, similar to polymeric immunoglobulin receptor, was isolated. This protein inhibits HIV-1 reverse transcriptase (RT) but lacks ribonuclease activity.
Area of Science:
- Biochemistry
- Molecular Biology
- Immunology
Background:
- Bovine milk contains various proteins with potential biological activities.
- The polymeric immunoglobulin receptor (pIgR) plays a role in mucosal immunity.
- Investigating milk proteins can reveal novel therapeutic or research tools.
Purpose of the Study:
- To isolate and characterize an 85 kDa protein from bovine milk with sequence homology to pIgR.
- To evaluate the protein's inhibitory activity against HIV-1 reverse transcriptase (RT).
- To assess the protein's ribonuclease activity and its effect on cell-free translation.
Main Methods:
- Protein isolation from bovine acid whey using ammonium sulfate precipitation.
- Chromatographic purification including CM-Sepharose and Mono S.
- Enzyme inhibition assays for HIV-1 RT, ribonuclease activity, and cell-free translation.
Main Results:
- An 85 kDa protein with an N-terminal sequence resembling pIgR was successfully isolated.
- The isolated protein demonstrated significant inhibition of HIV-1 RT with an IC(50) of 4.8 microM.
- No ribonuclease activity or inhibition of cell-free translation was observed.
Conclusions:
- A novel bovine milk protein with pIgR-like characteristics was identified.
- This protein exhibits specific inhibitory activity against HIV-1 RT.
- The findings suggest potential applications for this milk protein in antiviral research or therapy.
Abstract:
A protein with a molecular mass of 85 kDa and an N-terminal sequence resembling polymeric immunoglobulin receptor has been isolated from bovine milk. The isolation procedure involved removal of globulin from acid whey by precipitation with 1.8 M (NH(4))(2)SO(4) followed by addition of (NH(4))(2)SO(4) to attain a concentration of 3.6 M. Subsequent steps included chromatography on CM-Sepharose and Mono S and elution of the protein of interest with a linear NaCl concentration gradient. The polymeric immunoglobulin receptor-like milk protein inhibited HIV-1 reverse transcriptase (RT) with an IC(50) of 4.8 microM. However, it did not exhibit ribonuclease activity. Neither did it inhibit translation in a cell-free rabbit reticulocyte lysate system.
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