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• W2990699749 abstract "Molecular chaperones and cochaperones are the most abundant cellular effectors of protein homeostasis, assisting protein folding and preventing aggregation of misfolded proteins. We have previously shown that herpes simplex virus 1 (HSV-1) infection results in the drastic spatial reorganization of the cellular chaperone Hsc70 into nuclear domains called VICE (Virus Induced Chaperone Enriched) domains and that this recruitment is dependent on the viral immediate early protein ICP22. Here, we present several lines of evidence supporting the notion that ICP22 functions as a virally encoded cochaperone (J-protein/Hsp40) functioning together with its Hsc70 partner to recognize and manage aggregated and misfolded proteins. We show that ICP22 results in (i) nuclear sequestration of nonnative proteins, (ii) reduction of cytoplasmic aggresomes in cells expressing aggregation-prone proteins, and (iii) thermoprotection against heat inactivation of firefly luciferase, and (iv) sequence homology analysis indicated that ICP22 contains an N-terminal J domain and a C-terminal substrate binding domain, similar to type II cellular J proteins. ICP22 may thus be functionally similar to J-protein/Hsp40 cochaperones that function together with their HSP70 partners to prevent aggregation of nonnative proteins. This is not the first example of a virus hijacking a function of a cellular chaperone, since simian immunodeficiency virus T antigen was previously shown to contain a J domain; however, this the first known example of the acquisition of a functional J-like protein by a virus and suggests that HSV has taken advantage of the adaptable nature of J proteins to evolve a multifunctional cochaperone that functions with Hsc70 to promote lytic infection.IMPORTANCE Viruses have evolved a variety of strategies to succeed in a hostile environment. The herpes simplex virus 1 (HSV-1) immediate early protein ICP22 plays several roles in the virus life cycle, including downregulation of cellular gene expression, upregulation of late viral gene expression, inhibition of apoptosis, prevention of aggregation of nonnative proteins, and the recruitment of a cellular heat shock protein, Hsc70, to nuclear domains. We present evidence that ICP22 functionally resembles a cellular J-protein/HSP40 family cochaperone, interacting specifically with Hsc70. We suggest that HSV has taken advantage of the adaptable nature of J proteins to evolve a multifunctional cochaperone that functions with Hsc70 to promote lytic infection." @default.
• W2990699749 created "2019-12-05" @default.
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• W2990699749 date "2020-01-31" @default.
• W2990699749 modified "2023-09-26" @default.
• W2990699749 title "The Herpes Simplex Virus 1 Immediate Early Protein ICP22 Is a Functional Mimic of a Cellular J Protein" @default.
• W2990699749 cites W1551656240 @default.
• W2990699749 cites W1724563161 @default.
• W2990699749 cites W1747817694 @default.
• W2990699749 cites W1965754110 @default.
• W2990699749 cites W1969631125 @default.
• W2990699749 cites W1972121275 @default.
• W2990699749 cites W1976564343 @default.
• W2990699749 cites W1988146888 @default.
• W2990699749 cites W1991309644 @default.
• W2990699749 cites W1995112257 @default.
• W2990699749 cites W1995902122 @default.
• W2990699749 cites W2001107002 @default.
• W2990699749 cites W2002431899 @default.
• W2990699749 cites W2002782099 @default.
• W2990699749 cites W2013944211 @default.
• W2990699749 cites W2018395782 @default.
• W2990699749 cites W2021242983 @default.
• W2990699749 cites W2021532580 @default.
• W2990699749 cites W2021919397 @default.
• W2990699749 cites W2030931536 @default.
• W2990699749 cites W2031978571 @default.
• W2990699749 cites W2043433277 @default.
• W2990699749 cites W2043552106 @default.
• W2990699749 cites W2047858670 @default.
• W2990699749 cites W2049057605 @default.
• W2990699749 cites W2051941413 @default.
• W2990699749 cites W2052973965 @default.
• W2990699749 cites W2065031087 @default.
• W2990699749 cites W2069717795 @default.
• W2990699749 cites W2071327617 @default.
• W2990699749 cites W2076250336 @default.
• W2990699749 cites W2080636803 @default.
• W2990699749 cites W2089318493 @default.
• W2990699749 cites W2089400513 @default.
• W2990699749 cites W2090097020 @default.
• W2990699749 cites W2094053167 @default.
• W2990699749 cites W2094400633 @default.
• W2990699749 cites W2096966529 @default.
• W2990699749 cites W2097906368 @default.
• W2990699749 cites W2100680605 @default.
• W2990699749 cites W2104921590 @default.
• W2990699749 cites W2106296270 @default.
• W2990699749 cites W2109350663 @default.
• W2990699749 cites W2110098549 @default.
• W2990699749 cites W2116949284 @default.
• W2990699749 cites W2119714298 @default.
• W2990699749 cites W2124669920 @default.
• W2990699749 cites W2132026043 @default.
• W2990699749 cites W2134656199 @default.
• W2990699749 cites W2138158290 @default.
• W2990699749 cites W2144378803 @default.
• W2990699749 cites W2146223931 @default.
• W2990699749 cites W2147751241 @default.
• W2990699749 cites W2149461582 @default.
• W2990699749 cites W2149761960 @default.
• W2990699749 cites W2156079900 @default.
• W2990699749 cites W2158534684 @default.
• W2990699749 cites W2160076699 @default.
• W2990699749 cites W2160301054 @default.
• W2990699749 cites W2165684456 @default.
• W2990699749 cites W2165988131 @default.
• W2990699749 cites W2170983070 @default.
• W2990699749 cites W2219462594 @default.
• W2990699749 cites W2347047344 @default.
• W2990699749 cites W2410012927 @default.
• W2990699749 cites W2529605438 @default.
• W2990699749 cites W2595886211 @default.
• W2990699749 cites W2595891670 @default.
• W2990699749 cites W2605412739 @default.
• W2990699749 cites W2625805967 @default.
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• W2990699749 doi "https://doi.org/10.1128/jvi.01564-19" @default.
• W2990699749 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6997750" @default.
• W2990699749 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31748398" @default.
• W2990699749 hasPublicationYear "2020" @default.
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