综述

冠状病毒组装及释放机制的研究进展

  • 杨昆 ,
  • 王兰 ,
  • 赵志虎 ,
  • 张彦 ,
  • 余国营
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  • 1.河南师范大学生命科学学院 (河南 新乡 453007 )
    2.河南省肺纤维化国际联合实验室 (河南 新乡 453007 )
    3.军事科学院军事医学研究院生物工程研究所 (北京 100097 )

收稿日期: 2024-02-11

  网络出版日期: 2024-09-30

基金资助

国家重点研发计划(2018YFA0900801)

Research progress on the assembly and release mechanisms of coronaviruses

  • Kun YANG ,
  • Lan WANG ,
  • Zhihu ZHAO ,
  • Yan ZHANG ,
  • Guoying. YU
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  • College of Life Sciences,He′nan Normal University,Xinxiang 453007,China; *He′nan International Joint Laboratory for Pulmonary Fibrosis,Xinxiang 453007,ChinaCorrsponding author: YU Guoying E?mail: 2018043@htu. edu. cn

Received date: 2024-02-11

  Online published: 2024-09-30

摘要

冠状病毒在近几十年中引起了多次大规模的传染病造成了严重的人员伤亡,严重威胁着人类的生命健康。病毒的组装与释放是冠状病毒生命周期的关键阶段,因此对冠状病毒组装和释放机制进行研究是至关重要的。该文对冠状病毒组装包装机制、冠状病毒多种释放途径以及相应的靶向抗病毒药物进行阐述,为其应对冠状病毒的预防与治疗提供参考。

本文引用格式

杨昆 , 王兰 , 赵志虎 , 张彦 , 余国营 . 冠状病毒组装及释放机制的研究进展[J]. 实用医学杂志, 2024 , 40(18) : 2654 -2659 . DOI: 10.3969/j.issn.1006-5725.2024.18.025

Abstract

In recent decades, the advent of coronaviruses has engendered multiple large-scale infectious outbreaks, leading to profound human casualties and posing a significant menace to global public health. At the crux of the coronavirus lifecycle, the assembly and release phases emerge as pivotal processes, necessitating meticulous investigation into the underlying mechanisms. This paper systematically expounds upon the intricate assembly and packaging mechanisms intrinsic to coronaviruses, scrutinizes the diverse release pathways employed by these viruses, and delves into the discourse surrounding targeted antiviral drugs. The comprehensive insights encapsulated in this exposition serve as valuable reference points for formulating effective strategies in the prevention and treatment of coronavirus infections.

参考文献

1 LUDWIG S, ZARBOCK A. Coronaviruses and SARS-CoV-2: A brief overview[J]. Anesth Analg, 2020, 131(1): 93-96. doi:10.1213/ane.0000000000004845
2 周恩豪,杨春. 新型冠状病毒肺炎的研究进展[J]. 实用医学杂志,2020,36(19):2609-2615.
3 栾涛,杨罡,王帅颖,等. “长新冠”综合征研究最新进展[J]. 实用医学杂志,2023,39(10):1195-1200.
4 ZHANG Y, HUANG Z, ZHU J, et al. An updated review of SARS-CoV-2 detection methods in the context of a novel coronavirus pandemic[J]. Bioeng Transl Med, 2022, 8(1): e10356. doi:10.1002/btm2.10356
5 江晶晶,冯富娟,高春,等. 新型冠状病毒肺炎的药物治疗研究进展[J]. 实用医学杂志,2022,38(7):786-790.
6 ARTIKA I M, DEWANTARI A K, WIYATNO A. Molecular biology of coronaviruses: current knowledge[J]. Heliyon, 2020, 6(8): e04743. doi:10.1016/j.heliyon.2020.e04743
7 MASTERS P S. Coronavirus genomic RNA packaging[J]. Virology, 2019, 537: 198-207. doi:10.1016/j.virol.2019.08.031
8 BAI Z, CAO Y, LIU W, et al. The SARS-CoV-2 nucleocapsid protein and its role in viral structure, biological functions, and a potential target for drug or vaccine mitigation [J]. Viruses, 2021, 13(6): 1115. doi:10.3390/v13061115
9 ADLY A N, BI M, CARLSON C R, et al. Assembly of SARS-CoV-2 ribonucleosomes by truncated N? variant of the nucleocapsid protein[J]. J Biol Chem, 2023, 299(12): 105362. doi:10.1016/j.jbc.2023.105362
10 FUNG T S, LIU D X. Human coronavirus: host-pathogen interaction[J]. Annu Rev Microbiol, 2019, 73(1): 529-557. doi:10.1146/annurev-micro-020518-115759
11 MUKHERJEE S, BHATTACHARYYA D, BHUNIA A. Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain[J]. Biophys Chem, 2020, 266: 106452. doi:10.1016/j.bpc.2020.106452
12 ZHANG Z, NOMURA N, MURAMOTO Y, et al. Structure of SARS-CoV-2 membrane protein essential for virus assembly[J]. Nat Commun, 2022, 13(1): 4399. doi:10.1038/s41467-022-32019-3
13 CASTA?O-RODRIGUEZ C, HONRUBIA JOSE M, GUTIéRREZ-áLVAREZ J, et al. Role of severe acute respiratory syndrome coronavirus viroporins E, 3a, and 8a in replication and pathogenesis[J]. mBio, 2018, 9(3): e02325-17. doi:10.1128/mbio.02325-17
14 KUZMIN A, OREKHOV P, ASTASHKIN R, et al. Structure and dynamics of the SARS-CoV-2 envelope protein monomer[J]. Proteins, 2022, 90(5): 1102-1114. doi:10.1002/prot.26317
15 ALSAADI E A J, NEUMAN B W, JONES I M. Identification of a membrane binding peptide in the envelope protein of MHV coronavirus[J]. Viruses, 2020, 12(9): 1054. doi:10.3390/v12091054
16 ZHANG J, XIAO T, CAI Y, et al. Structure of SARS-CoV-2 spike protein[J]. Curr Opin Virol, 2021, 50: 173-182. doi:10.1016/j.coviro.2021.08.010
17 WRAPP D, WANG N, CORBETT K S, et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation[J]. Science, 2020, 367(6483): 1260-1263. doi:10.1126/science.abb2507
18 KATHIRAVAN M K, RADHAKRISHNAN S, NAMASIVAYAM V, et al. An overview of spike surface glycoprotein in severe acute respiratory syndrome-coronavirus[J]. Front Mol Biosci, 2021, 8: 637550. doi:10.3389/fmolb.2021.637550
19 LI D, LIU Y, LU Y, et al. Palmitoylation of SARS-CoV-2 S protein is critical for S-mediated syncytia formation and virus entry Palmitoylation of SARS‐CoV‐2 S protein is critical for S‐mediated syncytia formation and virus entry[J]. J Med Virol, 2022, 94(1): 342-348. doi:10.1002/jmv.27339
20 PLESCIA C B, DAVID E A, PATRA D, et al. SARS-CoV-2 viral budding and entry can be modeled using BSL-2 level virus-like particles[J]. J Biol Chem, 2021, 296: 100103. doi:10.1074/jbc.ra120.016148
21 SCHOEMAN D, FIELDING B C. Coronavirus envelope protein: current knowledge[J]. Virol J, 2019, 16(1): 69. doi:10.1186/s12985-019-1182-0
22 MAIN A, FULLER W. Protein S‐Palmitoylation: advances and challenges in studying a therapeutically important lipid modification[J]. FEBS J, 2021, 289(4): 861-882. doi:10.1111/febs.15781
23 CADENA-LóPEZ D, VILLALBA-NIETO M, CAMPOS-MELENDEZ F, et al. Assembly of Coronaviruses and CoV-Like-Particles[M] // COMAS-GARCIA M, ROSALES-MENDOZA S. Physical Virology. Cham: Springer, 2023: 141-160. doi:10.1007/978-3-031-36815-8_7
24 CUBUK J, ALSTON J J, INCICCO J J, et al. The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA[J]. Nat Commun, 2021, 12(1): 1936. doi:10.1038/s41467-021-21953-3
25 LU S, YE Q, SINGH D, et al. The SARS-CoV-2 nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein[J]. Nat Commun, 2021, 12(1): 502. doi:10.1038/s41467-020-20768-y
26 ETIBOR T A, YAMAUCHI Y, AMORIM M J. Liquid biomolecular condensates and viral lifecycles: Review and perspectives[J]. Viruses, 2021, 13(3): 366. doi:10.3390/v13030366
27 SARASTE J, PRYDZ K. Assembly and cellular exit of coronaviruses: hijacking an unconventional secretory pathway from the pre-Golgi intermediate compartment via the Golgi ribbon to the extracellular space[J]. Cells, 2021, 10(3): 503. doi:10.3390/cells10030503
28 KUMAR B, HAWKINS G M, KICMAL T, et al. Assembly and entry of severe acute respiratory syndrome coronavirus 2 (SARS-CoV2): evaluation using virus-like particles[J]. Cells, 2021, 10(4): 853. doi:10.3390/cells10040853
29 SCHERER K M, MASCHERONI L, CARNELL G W, et al. SARS-CoV-2 nucleocapsid protein adheres to replication organelles before viral assembly at the Golgi/ERGIC and lysosome-mediated egress[J]. Sci Adv, 2022, 8(1): eabl4895. doi:10.1126/sciadv.abl4895
30 GHOSH S, DELLIBOVI-RAGHEB T A, KERVIEL A, et al. β- Coronaviruses use lysosomes for egress instead of the biosynthetic secretory pathway [J]. Cell, 2020, 183(6): 1520-1535.e1514.
31 EYMIEUX S, UZBEKOV R, ROUILLé Y, et al. Secretory vesicles are the principal means of SARS-CoV-2 egress[J]. Cells, 2021, 10(8): 2047. doi:10.3390/cells10082047
32 BAI Z, CAO Y, LIU W, et al. The SARS-CoV-2 Nucleocapsid Protein and Its Role in Viral Structure, Biological Functions, and a Potential Target for Drug or Vaccine Mitigation[J]. Viruses, 2021, 13(6):1115. doi:10.3390/v13061115
33 DAWOOD A A, ALTOBJE M A. Inhibition of N-linked glycosylation by tunicamycin may contribute to the treatment of SARS-CoV-2[J]. Microb Pathog, 2020, 149: 104586. doi:10.1016/j.micpath.2020.104586
34 COUR M, OVIZE M, ARGAUD L. Cyclosporine A: a valid candidate to treat COVID-19 patients with acute respiratory failure?[J]. Crit Care, 2020, 24(1):276. doi:10.1186/s13054-020-03014-1
35 RAJ K, KAUR K, GUPTA G D, et al. Current understanding on molecular drug targets and emerging treatment strategy for novel coronavirus-19[J]. Naunyn Schmiedebergs Arch Pharmacol, 2021, 394(7): 1383-1402. doi:10.1007/s00210-021-02091-5
36 D′ALESSANDRO S, SCACCABAROZZI D, SIGNORINI L, et al. The Use of Antimalarial Drugs against Viral Infection[J]. Microorganisms, 2020, 8(1):85.
37 RICHARDSON P, GRIFFIN I, TUCKER C, et al. Baricitinib as potential treatment for 2019-nCoV acute respiratory disease[J]. Lancet, 2020, 395(10223): e30-e31. doi:10.1016/s0140-6736(20)30304-4
38 WANG J, FANG S, XIAO H, et al. Interaction of the Coronavirus Infectious Bronchitis Virus Membrane Protein with β-Actin and Its Implication in Virion Assembly and Budding[J]. PLoS One, 2009, 4(3): e4908. doi:10.1371/journal.pone.0004908
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