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SARS-CoV-2 Assembly: Gaining Infectivity and Beyond

Katiyar et al., Viruses, doi:10.3390/v16111648
Oct 2024  
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Review of SARS-CoV-2 assembly and the roles of viral structural proteins. Authors describe the key steps including the synthesis and trafficking of spike (S), membrane (M), envelope (E), and nucleocapsid (N) proteins to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) where they assemble with the viral RNA genome into new virions. The M protein drives assembly through self-multimerization and interactions with other components. The E protein promotes membrane curvature and scission to complete budding. N packages the viral RNA genome. S enables infectivity by binding cellular receptors. Various experimental systems are discussed for studying assembly. Cellular proteins can either promote or restrict the assembly process. Assembly is also regulated by viral accessory proteins and post-translational modifications of structural proteins.
Katiyar et al., 22 Oct 2024, Canada, peer-reviewed, 4 authors. Contact: chen.liang@mcgill.ca (corresponding author), harshita.katiyar@mail.mcgill.ca, ariana.arduini@mail.mcgill.ca, yichen.li2@mail.mcgill.ca.
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SARS-CoV-2 Assembly: Gaining Infectivity and Beyond
Harshita Katiyar, Ariana Arduini, Yichen Li, Chen Liang
Viruses, doi:10.3390/v16111648
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was responsible for causing the COVID-19 pandemic. Intensive research has illuminated the complex biology of SARS-CoV-2 and its continuous evolution during and after the COVID-19 pandemic. While much attention has been paid to the structure and functions of the viral spike protein and the entry step of viral infection, partly because these are targets for neutralizing antibodies and COVID-19 vaccines, the later stages of SARS-CoV-2 replication, including the assembly and egress of viral progenies, remain poorly characterized. This includes insight into how the activities of the viral structural proteins are orchestrated spatially and temporally, which cellular proteins are assimilated by the virus to assist viral assembly, and how SARS-CoV-2 counters and evades the cellular mechanisms antagonizing virus assembly. In addition to becoming infectious, SARS-CoV-2 progenies also need to survive the hostile innate and adaptive immune mechanisms, such as recognition by neutralizing antibodies. This review offers an updated summary of the roles of SARS-CoV-2 structural proteins in viral assembly, the regulation of assembly by viral and cellular factors, and the cellular mechanisms that restrict this process. Knowledge of these key events often reveals the vulnerabilities of SARS-CoV-2 and aids in the development of effective antiviral therapeutics.
Author Contributions: Writing-original draft preparation, H.K. and Y.L.; writing-review and editing, H.K., A.A. and C.L.; visualization-figure preparation, H.K. All authors have read and agreed to the published version of the manuscript.
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While much ' 'attention has been paid to the structure and functions of the viral spike protein and the ' 'entry step of viral infection, partly because these are targets for neutralizing antibodies ' 'and COVID-19 vaccines, the later stages of SARS-CoV-2 replication, including the assembly and ' 'egress of viral progenies, remain poorly characterized. This includes insight into how the ' 'activities of the viral structural proteins are orchestrated spatially and temporally, which ' 'cellular proteins are assimilated by the virus to assist viral assembly, and how SARS-CoV-2 ' 'counters and evades the cellular mechanisms antagonizing virus assembly. In addition to ' 'becoming infectious, SARS-CoV-2 progenies also need to survive the hostile innate and ' 'adaptive immune mechanisms, such as recognition by neutralizing antibodies. This review ' 'offers an updated summary of the roles of SARS-CoV-2 structural proteins in viral assembly, ' 'the regulation of assembly by viral and cellular factors, and the cellular mechanisms that ' 'restrict this process. Knowledge of these key events often reveals the vulnerabilities of ' 'SARS-CoV-2 and aids in the development of effective antiviral therapeutics.</jats:p>', 'DOI': '10.3390/v16111648', 'type': 'journal-article', 'created': { 'date-parts': [[2024, 10, 22]], 'date-time': '2024-10-22T08:10:14Z', 'timestamp': 1729584614000}, 'page': '1648', 'source': 'Crossref', 'is-referenced-by-count': 0, 'title': 'SARS-CoV-2 Assembly: Gaining Infectivity and Beyond', 'prefix': '10.3390', 'volume': '16', 'author': [ { 'given': 'Harshita', 'family': 'Katiyar', 'sequence': 'first', 'affiliation': [ { 'name': 'Lady Davis Institute, Jewish General Hospital, Montreal, QC H3T ' '1E2, Canada'}, { 'name': 'Department of Microbiology and Immunology, McGill University, ' 'Montreal, QC H3A 2B4, Canada'}]}, { 'given': 'Ariana', 'family': 'Arduini', 'sequence': 'additional', 'affiliation': [ { 'name': 'Lady Davis Institute, Jewish General Hospital, Montreal, QC H3T ' '1E2, Canada'}, { 'name': 'Department of Medicine, McGill University, Montreal, QC H3G 2M1, ' 'Canada'}]}, { 'given': 'Yichen', 'family': 'Li', 'sequence': 'additional', 'affiliation': [ { 'name': 'Lady Davis Institute, Jewish General Hospital, Montreal, QC H3T ' '1E2, Canada'}, { 'name': 'Department of Microbiology and Immunology, McGill University, ' 'Montreal, QC H3A 2B4, Canada'}]}, { 'given': 'Chen', 'family': 'Liang', 'sequence': 'additional', 'affiliation': [ { 'name': 'Lady Davis Institute, Jewish General Hospital, Montreal, QC H3T ' '1E2, Canada'}, { 'name': 'Department of Microbiology and Immunology, McGill University, ' 'Montreal, QC H3A 2B4, Canada'}, { 'name': 'Department of Medicine, McGill University, Montreal, QC H3G 2M1, ' 'Canada'}]}], 'member': '1968', 'published-online': {'date-parts': [[2024, 10, 22]]}, 'reference': [ { 'key': 'ref_1', 'doi-asserted-by': 'crossref', 'first-page': '727', 'DOI': '10.1056/NEJMoa2001017', 'article-title': 'A Novel Coronavirus from Patients with Pneumonia in China, 2019', 'volume': '382', 'author': 'Zhu', 'year': '2020', 'journal-title': 'N. 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