FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2019564765> ?p ?o ?g. }

• W2019564765 abstract "ABSTRACT Viruses require the host translational apparatus to synthesize viral proteins. Host stress response mechanisms that suppress translation, therefore, represent a significant obstacle that viruses must overcome. Here, we report a strategy whereby the mammalian orthoreoviruses compartmentalize the translational machinery within virus-induced inclusions known as viral factories (VF). VF are the sites of reovirus replication and assembly but were thought not to contain ribosomes. It was assumed viral mRNAs exited the VF to undergo translation by the cellular machinery, and proteins reentered the factory to participate in assembly. Here, we used ribopuromycylation to visualize active translation in infected cells. These studies revealed that active translation occurs within VF and that ribosomal subunits and proteins required for translation initiation, elongation, termination, and recycling localize to the factory. Interestingly, we observed components of the 43S preinitiation complex (PIC) concentrating primarily at factory margins, suggesting a spatial and/or dynamic organization of translation within the VF. Similarly, the viral single-stranded RNA binding protein σNS localized to the factory margins and had a tubulovesicular staining pattern that extended a short distance from the margins of the factories and colocalized with endoplasmic reticulum (ER) markers. Consistent with these colocalization studies, σNS was found to associate with both eukaryotic translation initiation factor 3 subunit A (eIF3A) and the ribosomal subunit pS6R. Together, these findings indicate that σNS functions to recruit 43S PIC machinery to the primary site of viral translation within the viral factory. Pathogen-mediated compartmentalization of the translational apparatus provides a novel mechanism by which viruses might avoid host translational suppression. IMPORTANCE Viruses lack biosynthetic capabilities and depend upon the host for protein synthesis. This dependence requires viruses to evolve mechanisms to coerce the host translational machinery into synthesizing viral proteins in the face of ongoing cellular stress responses that suppress global protein synthesis. Reoviruses replicate and assemble within cytoplasmic inclusions called viral factories. However, synthesis of viral proteins was thought to occur in the cytosol. To identify the site(s) of viral translation, we undertook a microscopy-based approach using ribopuromycylation to detect active translation. Here, we report that active translation occurs within viral factories and that translational factors are compartmentalized within factories. Furthermore, we find that the reovirus nonstructural protein σNS associates with 43S preinitiation complexes at the factory margins, suggesting a role for σNS in translation. Together, virus-induced compartmentalization of the host translational machinery represents a strategy for viruses to spatiotemporally couple viral protein synthesis with viral replication and assembly." @default.
• W2019564765 created "2016-06-24" @default.
• W2019564765 creator A5008844142 @default.
• W2019564765 creator A5070846124 @default.
• W2019564765 creator A5089399007 @default.
• W2019564765 date "2014-10-31" @default.
• W2019564765 modified "2023-10-10" @default.
• W2019564765 title "Virus-Mediated Compartmentalization of the Host Translational Machinery" @default.
• W2019564765 cites W1509188202 @default.
• W2019564765 cites W1565097993 @default.
• W2019564765 cites W1622101525 @default.
• W2019564765 cites W1799953230 @default.
• W2019564765 cites W1964317873 @default.
• W2019564765 cites W1966455695 @default.
• W2019564765 cites W1967986998 @default.
• W2019564765 cites W1969264016 @default.
• W2019564765 cites W1969533384 @default.
• W2019564765 cites W1970561614 @default.
• W2019564765 cites W1972160946 @default.
• W2019564765 cites W1978396569 @default.
• W2019564765 cites W1985346742 @default.
• W2019564765 cites W1986991567 @default.
• W2019564765 cites W1990640355 @default.
• W2019564765 cites W1991140361 @default.
• W2019564765 cites W1991743074 @default.
• W2019564765 cites W1992261249 @default.
• W2019564765 cites W1994360005 @default.
• W2019564765 cites W1996550262 @default.
• W2019564765 cites W2000085886 @default.
• W2019564765 cites W2003702834 @default.
• W2019564765 cites W2005132603 @default.
• W2019564765 cites W2008410413 @default.
• W2019564765 cites W2010538519 @default.
• W2019564765 cites W2022636631 @default.
• W2019564765 cites W2022712238 @default.
• W2019564765 cites W2030785017 @default.
• W2019564765 cites W2031495818 @default.
• W2019564765 cites W2031757923 @default.
• W2019564765 cites W2032148650 @default.
• W2019564765 cites W2035205542 @default.
• W2019564765 cites W2037313242 @default.
• W2019564765 cites W2037483660 @default.
• W2019564765 cites W2053293904 @default.
• W2019564765 cites W2053885170 @default.
• W2019564765 cites W2056836205 @default.
• W2019564765 cites W2057710061 @default.
• W2019564765 cites W2060261905 @default.
• W2019564765 cites W2070985249 @default.
• W2019564765 cites W2071207834 @default.
• W2019564765 cites W2072963880 @default.
• W2019564765 cites W2075107227 @default.
• W2019564765 cites W2076353383 @default.
• W2019564765 cites W2082378699 @default.
• W2019564765 cites W2088412411 @default.
• W2019564765 cites W2091617778 @default.
• W2019564765 cites W2097102109 @default.
• W2019564765 cites W2097453900 @default.
• W2019564765 cites W2101990520 @default.
• W2019564765 cites W2103816676 @default.
• W2019564765 cites W2110811665 @default.
• W2019564765 cites W2113363982 @default.
• W2019564765 cites W2115102378 @default.
• W2019564765 cites W2123716335 @default.
• W2019564765 cites W2125170324 @default.
• W2019564765 cites W2142160102 @default.
• W2019564765 cites W2143339100 @default.
• W2019564765 cites W2150135205 @default.
• W2019564765 cites W2150249493 @default.
• W2019564765 cites W2167214317 @default.
• W2019564765 cites W2171184872 @default.
• W2019564765 cites W2171566201 @default.
• W2019564765 cites W2141002765 @default.
• W2019564765 doi "https://doi.org/10.1128/mbio.01463-14" @default.
• W2019564765 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4172071" @default.
• W2019564765 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25227463" @default.
• W2019564765 hasPublicationYear "2014" @default.
• W2019564765 type Work @default.
• W2019564765 sameAs 2019564765 @default.
• W2019564765 citedByCount "62" @default.
• W2019564765 countsByYear W20195647652014 @default.
• W2019564765 countsByYear W20195647652015 @default.
• W2019564765 countsByYear W20195647652016 @default.
• W2019564765 countsByYear W20195647652017 @default.
• W2019564765 countsByYear W20195647652018 @default.
• W2019564765 countsByYear W20195647652019 @default.
• W2019564765 countsByYear W20195647652020 @default.
• W2019564765 countsByYear W20195647652021 @default.
• W2019564765 countsByYear W20195647652022 @default.
• W2019564765 countsByYear W20195647652023 @default.
• W2019564765 crossrefType "journal-article" @default.
• W2019564765 hasAuthorship W2019564765A5008844142 @default.
• W2019564765 hasAuthorship W2019564765A5070846124 @default.
• W2019564765 hasAuthorship W2019564765A5089399007 @default.
• W2019564765 hasBestOaLocation W20195647651 @default.
• W2019564765 hasConcept C104292427 @default.
• W2019564765 hasConcept C104317684 @default.
• W2019564765 hasConcept C105580179 @default.
• W2019564765 hasConcept C110455231 @default.
• W2019564765 hasConcept C140704245 @default.
• W2019564765 hasConcept C149364088 @default.

• next