Work

Human immunodeficiency virus type 1 gag-protease fusion proteins are enzymatically active

Year: 1992

Type: article

Abstract: We have introduced mutations into the region of the genome of human immunodeficiency virus type 1 (HIV-1) that encodes the cleavage sites between the viral protease (PR) and the adjacent upstream region of the polyprotein precursor. Segments containing these mutations were introduced into plasmids, and the retroviral proteins were expressed in Escherichia coli. The mutations prevented cleavage between the PR and the adjacent polypeptide; however, other PR cleavage sites in the polyprotein were cleaved normally, showing that the release of free PR is not a prerequisite for the appropriate processing of HIV-1 precursors.

Source: Journal of Virology

DOI: 10.1128/jvi.66.11.6781-6783.1992

Authors: M Kotler, G Arad, S H Hughes

Language: English

Topic: HIV Research and Treatment

Subfield: Virology

Field: Immunology and Microbiology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: National Institutes of Health, National Cancer Institute

Awards: BASIC RESEARCH--CANCER INSTITUTE FREDERICK, G225764842