Efficient support of virus-like particle assembly by the HIV-1 packaging signal
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The principal structural component of a retrovirus particle is the Gag protein. Retroviral genomic RNAs contain a ‘packaging signal’ (‘Ψ%27) and are packaged in virus particles with very high selectivity. However, if no genomic RNA is present, Gag assembles into particles containing cellular mRNA molecules. The mechanism by which genomic RNA is normally selected during virus assembly is not understood. We previously reported (Comas-Garcia et al., 2017) that at physiological ionic strength, recombinant HIV-1 Gag binds with similar affinities to RNAs with or without Ψ, and proposed that genomic RNA is selectively packaged because binding to Ψ initiates particle assembly more efficiently than other RNAs. We now present data directly supporting this hypothesis. We also show that one or more short stretches of unpaired G residues are important elements of Ψ; Ψ may not be localized to a single structural element, but is probably distributed over >100 bases. © Xiong et al.
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The principal structural component of a retrovirus particle is the Gag protein. Retroviral genomic RNAs contain a ‘packaging signal’ (‘Ψ') and are packaged in virus particles with very high selectivity. However, if no genomic RNA is present, Gag assembles into particles containing cellular mRNA molecules. The mechanism by which genomic RNA is normally selected during virus assembly is not understood. We previously reported (Comas-Garcia et al., 2017) that at physiological ionic strength, recombinant HIV-1 Gag binds with similar affinities to RNAs with or without Ψ, and proposed that genomic RNA is selectively packaged because binding to Ψ initiates particle assembly more efficiently than other RNAs. We now present data directly supporting this hypothesis. We also show that one or more short stretches of unpaired G residues are important elements of Ψ; Ψ may not be localized to a single structural element, but is probably distributed over >100 bases. © Xiong et al.
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Gag protein; genomic RNA; Gag protein; virus RNA; Article; binding affinity; binding site; dimerization; DNA packaging; DNA sequence; electron microscopy; Human immunodeficiency virus 1; immunoblotting; ionic strength; nonhuman; RNA binding; RNA sequence; virus assembly; virus like agent; virus nucleocapsid; chemistry; conformation; metabolism; physiology; ultrastructure; virion; virus assembly; gag Gene Products, Human Immunodeficiency Virus; HIV-1; Nucleic Acid Conformation; RNA, Viral; Virion; Virus Assembly
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