Zheng Chunfu/Gao Jie was invited to publish a cover review in Journal of Virology

Recently, Professor Chunfu Zheng/Associate Researcher Dr.
Jie Gao of Inner Mongolia University were invited to publish a cover review in the Journal of Virology (JVI): When poly(A) binding proteins meetviral infections.
This paper comprehensively summarizes the evolution of multiple strategies to manipulate PABPs during virus infection So as to enhance the latest research progress of virus replication
.

The impact factor of JVI broke 5 last year, and finally broke 6 this year! ! ! The PABP family is a protein family with RNA-binding function.
In addition to binding the poly(A) tail to participate in the translation initiation of eukaryotic mRNA, it is also involved in the metabolic regulation of mRNA
.

In the process of viral infection, the virus needs to rely on the host's transcriptional machinery to transcribe viral mRNA, and different types of viruses turn off/attenuate the host's transcriptional activity by manipulating various activities of PABPs, and evade the host's antiviral mechanism
.

Viruses destroy PABPs mainly from the following aspects: (1) destroying the formation of eIF4F, the eukaryotic translation initiation complex of PABPs; (2) cleaving PABPs by viral protease; (3) localizing PABPs from the cytoplasm to the nucleus; (4) ) interfere with the formation of stress granules (SGs) containing PABPs
.

There has been no literature update on this aspect in the past ten years, and there is no systematic generalization of the relationship and regularity between the structure of different viral mRNAs and the manipulation of PABPs
.

This review updates the latest related research and summarizes the regularity between the structure of viral mRNA and the manipulation of PABPs
.

Article link: https://journals.
asm.
org/doi/10.
1128/jvi.
00136-22 Figure 1.
Structure of PABPs and eukaryotic mRNA translation initiation complexes
.

(A) Structures of different PABPs, except that PABPC5 and PABPN1 have only RRM domains, the rest of PABPs mainly include N-terminal RRM domain, C-terminal MLLE domain and intermediate proline-rich junction; (B) eukaryotic translation initiation Complex: The poly(A) tail of eukaryotic mRNA binds to the 5' cap through PABPs and eIF4G to form a head-to-tail ring structure, which mediates the binding of ribosomal subunits to initiate translation
.

Figure 2.
Viral protein cleaves PABPs and eIF4G
.

(A) Viral cleavage of PABPs or eIF4G on the translation initiation complex; (B) Different viral proteases cleave different sites of PABPs and eIF4G
.

Figure 3.
Viral proteins mimic the function of PABPs
.

The viral NSP3 protein mimics the function of PABP.
By binding to the special structure of the 3' tail of the rotavirus mRNA and binding to eIF4G, the viral mRNA is linked end-to-end to promote the translation initiation of the viral mRNA
.

Binding of NSP3 to the viral protein RoXaN and the host eIF4G protein is also required for the migration of PABPs from the cytoplasm to the nucleus, which reduces cytoplasmic PABPs to inhibit host translation
.

Figure 4.
HCMV negatively regulates the function of PABPs
.

4E-BP is a translation inhibitor that binds to eIF4E and regulates cellular translation initiation
.

HCMV excludes 4E-BP from the translation initiation complex to facilitate translation of viral mRNA
.

HCMV UL38 enhances the phosphorylation of 4E-BP through mTORC1 signaling, dissociates 4E-BP from eIF4E, and relieves translation initiation inhibition
.

UL38 also increases the levels of PABPs in the cytoplasm, which assist in the translation of viral mRNAs
.

HCMV UL69 dissociates 4E-BP from the complex at the cap end through indirect interaction with eIF4A
.

Figure 5.
Epstein-Barr virus migrates cytoplasmic PABPs to the nucleus
.

In herpesvirus-infected cells, viral proteins such as ICP27 and UL47 in HSV-1, SOX in KSHV and BGLF5 in EBV are all required to redistribute PABPs into the nucleus
.

This process inhibits cellular translation by reducing cytoplasmic PABPs
.

In addition, the EBV EB2 protein facilitates the export of viral mRNA from the nucleus and binds to PABP-eIF4F to facilitate translation initiation of viral mRNA
.

The first author: Dr.
Gao Jie; associate researcher of the School of Life Sciences, Inner Mongolia University, high-level "academic backbone" talents introduced by Inner Mongolia University, engaged in the research on the interaction between herpes virus and host, and has published 4 JVI papers as the first author
.

Corresponding author: Professor Zheng Chunfu, winner of the "Hundred Talents Program" of the Chinese Academy of Sciences (2007), University of Calgary, Canada, adjunct professor, editor and editorial board member of several SCI journals: 1.
mBio editor (zero breakthrough of local editors in mainland China) , 2.
Editorial board member of Journal of Virology, (2015-2024), (there was no local Chinese editorial board member before 2015) 3.
Associate editor of Frontiers in Microbiology; 4.
Associate editor of Frontiers in Immunology; 5.
Associate editor of Virology Journal; 6.
Deputy Editor-in-Chief of Journal of Medical Virology; 7.
Editorial Board Member of Military Medical Research; 8.
Deputy Editor-in-Chief of Gene, Protein and Disease; In addition, Zheng Chunfu participated in the review of dozens of SCI journals, such as Advanced Material, Cell host & Microbe, Seminar in Immunology, Microbiome, Cell Report, cellular and Molecular Immunology, PLoS Pathogen, Molecular Therapy, Acta Pharmaceutica Sinica B, Theranostics, Reviews in Medical Virology,
etc.

Since he started as editor in 2011, he has edited and reviewed more than 573 (303+270) articles
.

Chunfu Zheng won the 2019 Global Publons Peer Review Award (TOP1% in the field of microbiology), and was listed on the Journal of Virology's annual peer review list for three consecutive years from 2019 to 2021 (TOP25, 15-20 papers reviewed annually)
.

Professor Chunfu Zheng has made breakthroughs in the study of the molecular mechanism of the interaction between herpes simplex virus type I (HSV-1) infection and the host, and the study of HSV-1 escaping the host's antiviral innate immunity.
In Trends in Microbiology (IF 17.
257), Microbiology and Molecular Biology Reviews (cover article, IF 12.
568), FEMS Microbiology Reviews (IF 16.
408), Blood (IF 23.
629), Cell Host & Microbe (IF 29.
160), Journal of Medical Virology (immediate IF 17.
909), Cytokine & Growth Factor Reviews (immediate IF 16.
458), Reviews in Medical Virology (immediate IF 9.
858), Proceedings of the National Academy of Sciences USA (IF 12.
173), mBio (IF 7.
867), Journal of Biomedical Science (immediate IF 11.
792), Cellular and Molecular Life Sciences (IF 9.
206), Journal of Virology (23 papers, 2 of which are highlights; IF 5.
103), Journal of Immunology (2 papers, IF 5.
422), Protein and Cell (IF 14.
870; 2 papers), and other mainstream journals published in SCI He has published more than 110 papers, with a total of more than 2,700 citations and an H-index of 28
.

The website of Prof.
Chunfu Zheng's laboratory: https://bms.
fjmu.
edu.
cn/2017/1130/c2905a72170/page.
htm The topics of Prof.
Chunfu Zheng's recent manuscripts are as follows: 1.
Molecular mechanism of antiviral innate immune recognition and regulation and viral pathogenesis Immune Evasion https:// Virology and Antiviral Innate Immunity Assays https://www .
jove.
com/methods-collections/1731/current-experimental-methods-techniques-for-basic-virology-antiviral3.
Herpes virus vaccine development topic https:// characteristics-and-immune-recognition-of-human-herpes-virus-structure-proteins It is worth mentioning that Professor Zheng Chunfu’s article just published 3 months ago has been cited 45 times: