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• W2167680425 endingPage "13472" @default.
• W2167680425 startingPage "13463" @default.
• W2167680425 abstract "ABSTRACT The retroviral structural protein, Gag, is capable of independently assembling into virus-like particles (VLPs) in living cells and in vitro. Immature VLPs of human immunodeficiency virus type 1 (HIV-1) and of Rous sarcoma virus (RSV) are morphologically distinct when viewed by transmission electron microscopy (TEM). To better understand the nature of the Gag-Gag interactions leading to these distinctions, we constructed vectors encoding several RSV/HIV-1 chimeric Gag proteins for expression in either insect cells or vertebrate cells. We used TEM, confocal fluorescence microscopy, and a novel correlative scanning EM (SEM)-confocal microscopy technique to study the assembly properties of these proteins. Most chimeric proteins assembled into regular VLPs, with the capsid (CA) domain being the primary determinant of overall particle diameter and morphology. The presence of domains between matrix and CA also influenced particle morphology by increasing the spacing between the inner electron-dense ring and the VLP membrane. Fluorescently tagged versions of wild-type RSV, HIV-1, or murine leukemia virus Gag did not colocalize in cells. However, wild-type Gag proteins colocalized extensively with chimeric Gag proteins bearing the same CA domain, implying that Gag interactions are mediated by CA. A dramatic example of this phenomenon was provided by a nuclear export-deficient chimera of RSV Gag carrying the HIV-1 CA domain, which by itself localized to the nucleus but relocalized to the cytoplasm in the presence of wild type HIV-1 Gag. Wild-type and chimeric Gag proteins were capable of coassembly into a single VLP as viewed by correlative fluorescence SEM if, and only if, the CA domain was derived from the same virus. These results imply that the primary selectivity of Gag-Gag interactions is determined by the CA domain." @default.
• W2167680425 created "2016-06-24" @default.
• W2167680425 creator A5002859125 @default.
• W2167680425 creator A5063066850 @default.
• W2167680425 creator A5088660634 @default.
• W2167680425 date "2005-11-01" @default.
• W2167680425 modified "2023-10-17" @default.
• W2167680425 title "The Retroviral Capsid Domain Dictates Virion Size, Morphology, and Coassembly of Gag into Virus-Like Particles" @default.
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• W2167680425 doi "https://doi.org/10.1128/jvi.79.21.13463-13472.2005" @default.
• W2167680425 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1262573" @default.
• W2167680425 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16227267" @default.
• W2167680425 hasPublicationYear "2005" @default.
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