Article ; Online: Mature Rotavirus Particles Contain Equivalent Amounts of
2022 Volume 96, Issue 17, Page(s) e0115122
Abstract: Viruses have evolved different strategies to overcome their recognition by the host innate immune system. The addition of caps at their 5' RNA ends is an efficient mechanism not only to ensure escape from detection by the innate immune system but also to ...
Abstract | Viruses have evolved different strategies to overcome their recognition by the host innate immune system. The addition of caps at their 5' RNA ends is an efficient mechanism not only to ensure escape from detection by the innate immune system but also to ensure the efficient synthesis of viral proteins. Rotavirus mRNAs contain a type 1 cap structure at their 5' end that is added by the viral capping enzyme VP3, which is a multifunctional protein with all the enzymatic activities necessary to add the cap and also functions as an antagonist of the 2'-5'-oligoadenylate synthetase (OAS)/RNase L pathway. Here, the relative abundances of capped and noncapped viral RNAs during the replication cycle of rotavirus were determined. We found that both classes of rotaviral plus-sense RNAs (+RNAs) were encapsidated and that they were present in a 1:1 ratio in the mature infectious particles. The capping of viral +RNAs was dynamic, since different ratios of capped and noncapped RNAs were detected at different times postinfection. Similarly, when the relative amounts of capped and uncapped viral +RNAs produced in an |
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MeSH term(s) | 2',5'-Oligoadenylate Synthetase ; Capsid Proteins/metabolism ; Endoribonucleases/metabolism ; RNA Caps/analysis ; RNA Caps/chemistry ; RNA Caps/metabolism ; RNA, Double-Stranded/genetics ; RNA, Double-Stranded/metabolism ; RNA, Viral/chemistry ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Rotavirus/genetics ; Rotavirus/metabolism ; Virion/genetics ; Virion/metabolism ; Virus Replication |
Chemical Substances | Capsid Proteins ; RNA Caps ; RNA, Double-Stranded ; RNA, Viral ; VP3 protein, Rotavirus ; 2',5'-Oligoadenylate Synthetase (EC 2.7.7.84) ; Endoribonucleases (EC 3.1.-) ; 2-5A-dependent ribonuclease (EC 3.1.26.-) |
Language | English |
Publishing date | 2022-08-24 |
Publishing country | United States |
Document type | Journal Article |
ZDB-ID | 80174-4 |
ISSN | 1098-5514 ; 0022-538X |
ISSN (online) | 1098-5514 |
ISSN | 0022-538X |
DOI | 10.1128/jvi.01151-22 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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