Formation and working mechanism of the picornavirus VPg uridylylation complex

doi:10.1016/j.coviro.2014.09.003

Review

. 2014 Dec:9:24-30.

doi: 10.1016/j.coviro.2014.09.003. Epub 2014 Sep 19.

Formation and working mechanism of the picornavirus VPg uridylylation complex

Yuna Sun¹, Yu Guo², Zhiyong Lou³

Affiliations

¹ National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China; School of Medicine and MOE Key Laboratory of Protein Sciences, Tsinghua University, Beijing 100084, China.
² College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300071, China.
³ School of Medicine and MOE Key Laboratory of Protein Sciences, Tsinghua University, Beijing 100084, China; Collaborative Innovation Center for Biotherapy, Tsinghua University, Beijing 100084, China; Collaborative Innovation Center for Biotherapy, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, West China Medical School, Sichuan University, Chengdu, China. Electronic address: louzy@mail.tsinghua.edu.cn.

PMID: 25240314
DOI: 10.1016/j.coviro.2014.09.003

Review

Formation and working mechanism of the picornavirus VPg uridylylation complex

Yuna Sun et al. Curr Opin Virol. 2014 Dec.

. 2014 Dec:9:24-30.

doi: 10.1016/j.coviro.2014.09.003. Epub 2014 Sep 19.

Authors

Yuna Sun¹, Yu Guo², Zhiyong Lou³

Affiliations

¹ National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China; School of Medicine and MOE Key Laboratory of Protein Sciences, Tsinghua University, Beijing 100084, China.
² College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300071, China.
³ School of Medicine and MOE Key Laboratory of Protein Sciences, Tsinghua University, Beijing 100084, China; Collaborative Innovation Center for Biotherapy, Tsinghua University, Beijing 100084, China; Collaborative Innovation Center for Biotherapy, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, West China Medical School, Sichuan University, Chengdu, China. Electronic address: louzy@mail.tsinghua.edu.cn.

PMID: 25240314
DOI: 10.1016/j.coviro.2014.09.003

Abstract

The initiation of picornavirus replication is featured by the uridylylation of viral protein genome-linked (VPg). In this process, viral RNA-dependent RNA polymerase (RdRp) catalyzes two uridine monophosphate (UMP) molecules to the hydroxyl group of the third tyrosine residue of VPg. Subsequently, the uridylylated VPg (VPg-pUpU) functions as the protein primer to initiate the replication of the viral genome. Although a large body of functional and structural works has been performed to define individual snapshots for particular stages of the VPg uridylylation process, the formation, dynamics and mechanism of the whole VPg uridylylation complex still requires further elucidation. We would like to provide an overview of the current knowledge of the picornaviral VPg uridylylation complex in this paper.

PubMed Disclaimer

Cited by

Biochemical characterization of recombinant Enterovirus 71 3C protease with fluorogenic model peptide substrates and development of a biochemical assay.
Shang L, Zhang S, Yang X, Sun J, Li L, Cui Z, He Q, Guo Y, Sun Y, Yin Z. Shang L, et al. Antimicrob Agents Chemother. 2015 Apr;59(4):1827-36. doi: 10.1128/AAC.04698-14. Epub 2014 Nov 24. Antimicrob Agents Chemother. 2015. PMID: 25421478 Free PMC article.
Picornavirus RNA polyadenylation by 3D(pol), the viral RNA-dependent RNA polymerase.
Kempf BJ, Barton DJ. Kempf BJ, et al. Virus Res. 2015 Aug 3;206:3-11. doi: 10.1016/j.virusres.2014.12.030. Epub 2015 Jan 3. Virus Res. 2015. PMID: 25559071 Free PMC article. Review.
Picornavirus 2C proteins: structure-function relationships and interactions with host factors.
Yin C, Zhao H, Xia X, Pan Z, Li D, Zhang L. Yin C, et al. Front Cell Infect Microbiol. 2024 Feb 23;14:1347615. doi: 10.3389/fcimb.2024.1347615. eCollection 2024. Front Cell Infect Microbiol. 2024. PMID: 38465233 Free PMC article. Review.
Studies on Inhibition of Proliferation of Enterovirus-71 by Compound YZ-LY-0.
Yang Q, Jie Q, Shaw N, Li L, Rao Z, Yin Z, Lou Z. Yang Q, et al. Int J Biol Sci. 2015 Nov 1;11(11):1337-47. doi: 10.7150/ijbs.12996. eCollection 2015. Int J Biol Sci. 2015. PMID: 26640412 Free PMC article.
Peptidyl aldehyde NK-1.8k suppresses enterovirus 71 and enterovirus 68 infection by targeting protease 3C.
Wang Y, Yang B, Zhai Y, Yin Z, Sun Y, Rao Z. Wang Y, et al. Antimicrob Agents Chemother. 2015 May;59(5):2636-46. doi: 10.1128/AAC.00049-15. Epub 2015 Feb 17. Antimicrob Agents Chemother. 2015. PMID: 25691647 Free PMC article.

See all "Cited by" articles

Publication types

Actions
Actions

MeSH terms

Actions
Actions
Actions
Actions
Actions
Actions
Actions

Substances

Actions
Actions
Actions

LinkOut - more resources

Full Text Sources
- Elsevier Science
Other Literature Sources
- scite Smart Citations
Research Materials
- NCI CPTC Antibody Characterization Program

Save citation to file

Email citation

Add to Collections

Add to My Bibliography

Your saved search

Create a file for external citation management software

Your RSS Feed

Formation and working mechanism of the picornavirus VPg uridylylation complex

Affiliations

Formation and working mechanism of the picornavirus VPg uridylylation complex

Authors

Affiliations

Abstract

Similar articles

Cited by

Publication types

MeSH terms

Substances

LinkOut - more resources

Full Text Sources

Other Literature Sources

Research Materials

Abstract

Similar articles

Cited by

Publication types

MeSH terms

Substances

Related information

LinkOut - more resources

Full Text Sources

Other Literature Sources

Research Materials