期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 23, 期 14, 页码 -出版社
MDPI
DOI: 10.3390/ijms23147569
关键词
Gag molecular structure; p17 Gag; p24 Gag; p7 Gag; p6 Gag; p2 and p1 Gag
资金
- Poliomyelitis Research Foundation [16/67]
- University of KwaZulu-Natal's College of Health Sciences Ph.D. grant
- South African Medical Research Council (SIR grant)
The HIV-1 Gag polyprotein, originally believed to only contribute to the physical nature of the virus, has been found to have multiple roles in viral replication and functionality. It can mediate its own trafficking, interact with host factors, and aid in viral genome packaging. It has also been associated with drug resistance and treatment failure.
Once merely thought of as the protein responsible for the overall physical nature of the human immunodeficiency virus type 1 (HIV-1), the Gag polyprotein has since been elucidated to have several roles in viral replication and functionality. Over the years, extensive research into the polyproteins' structure has revealed that Gag can mediate its own trafficking to the plasma membrane, it can interact with several host factors and can even aid in viral genome packaging. Not surprisingly, Gag has also been associated with HIV-1 drug resistance and even treatment failure. Therefore, this review provides an extensive overview of the structural and functional roles of the HIV-1 Gag domains in virion integrity, functionality and infectivity.
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