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. 2024 Feb 1;20(2):e1011937.
doi: 10.1371/journal.ppat.1011937. eCollection 2024 Feb.

The "basics" of HIV-1 assembly

Christopher Sumner  1 , Akira Ono  1
Affiliations

The "basics" of HIV-1 assembly

Christopher Sumner et al. PLoS Pathog. .
No abstract available

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Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Fig 1
Fig 1. The schematic representations of HIV-1 Gag domains and assembly process.
(A) Gag domains and key basic residues or basic residue clusters discussed in this review. Upon cleavage of Pr55Gag, individual domains give rise to mature Gag proteins, MA, CA, p2 (SP1), NC, p1 (SP2), and p6. NTD, N-terminal domain; CTD, C-terminal domain; ZF, zinc finger. (B) Interactions between basic residues in Gag and polyanions play important roles at different steps of virus particle formation and post-assembly processes. In some cases, the basic residues in Gag and the polyanions switch their interaction partners through the transitions from one step to another. PI(4,5)P2, phosphatidylinositol (4,5) bisphosphate; IP6, inositol hexakisphosphate; vRNA, viral genomic RNA.
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References

    1. Freed EO. HIV-1 assembly, release and maturation. Nat Rev Microbiol. 2015;13(8):484–496. Epub 2015/06/29. doi: 10.1038/nrmicro3490 . - DOI - PMC - PubMed
    1. Ono A, Orenstein JM, Freed EO. Role of the Gag matrix domain in targeting human immunodeficiency virus type 1 assembly. J Virol. 2000;74(6):2855–2866. doi: 10.1128/jvi.74.6.2855-2866.2000 ; PubMed Central PMCID: PMC111776. - DOI - PMC - PubMed
    1. Yuan X, Yu X, Lee TH, Essex M. Mutations in the N-terminal region of human immunodeficiency virus type 1 matrix protein block intracellular transport of the Gag precursor. J Virol. 1993;67(11):6387–6394. doi: 10.1128/JVI.67.11.6387-6394.1993 ; PubMed Central PMCID: PMC238073. - DOI - PMC - PubMed
    1. Zhou W, Parent LJ, Wills JW, Resh MD. Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. J Virol. 1994;68(4):2556–2569. doi: 10.1128/JVI.68.4.2556-2569.1994 ; PubMed Central PMCID: PMC236733. - DOI - PMC - PubMed
    1. Hill CP, Worthylake D, Bancroft DP, Christensen AM, Sundquist WI. Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly. Proc Natl Acad Sci U S A. 1996;93(7):3099–3104. doi: 10.1073/pnas.93.7.3099 ; PubMed Central PMCID: PMC39768. - DOI - PMC - PubMed