SARS-CoV-2 Delta (B.1.617.2) Variant: A Unique T478K Mutation in Receptor Binding Motif (RBM) of Spike Gene
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초록
Over two hundred twenty-eight million cases of coronavirus disease 2019 (COVID-19) in the world have been reported until the 21st of September 2021 after the first rise in December 2019. The virus caused the disease called severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Over 4 million deaths blame COVID-19 during the last one year and 8 months in the world. Currently, four SARS-CoV-2 variants of concern are mainly focused by pandemic studies with limited experiments to translate the infectivity and pathogenicity of each variant. The SARS-CoV-2 α, β, γ, and δ variant of concern was originated from United Kingdom, South Africa, Brazil/Japan, and India, respectively. The classification of SARS-CoV-2 variant is based on the mutation in spike (S) gene on the envelop of SARS-CoV-2. This review describes four SARS-CoV-2 α, β, γ, and δ variants of concern including SARS-CoV-2 ε, ζ, η, ι, κ, and B.1.617.3 variants of interest and alert. Recently, SARS-CoV-2 δ variant prevails over different countries that have 3 unique mutation sites: E156del/R158G in the N-terminal domain and T478K in a crucial receptor binding domain. A particular mutation in the functional domain of the S gene is probably associated with the infectivity and pathogenesis of the SARS-CoV-2 variant.
Abstract
Over two hundred twenty-eight million cases of coronavirus disease 2019 (COVID-19) in the world have been reported until the 21st of September 2021 after the first rise in December 2019. The virus caused the disease called severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Over 4 million deaths blame COVID-19 during the last one year and 8 months in the world. Currently, four SARS-CoV-2 variants of concern are mainly focused by pandemic studies with limited experiments to translate the infectivity and pathogenicity of each variant. The SARS-CoV-2 α, β, γ, and δ variant of concern was originated from United Kingdom, South Africa, Brazil/Japan, and India, respectively. The classification of SARS-CoV-2 variant is based on the mutation in spike (S) gene on the envelop of SARS-CoV-2. This review describes four SARS-CoV-2 α, β, γ, and δ variants of concern including SARS-CoV-2 ε, ζ, η, ι, κ, and B.1.617.3 variants of interest and alert. Recently, SARS-CoV-2 δ variant prevails over different countries that have 3 unique mutation sites: E156del/R158G in the N-terminal domain and T478K in a crucial receptor binding domain. A particular mutation in the functional domain of the S gene is probably associated with the infectivity and pathogenesis of the SARS-CoV-2 variant.
참고문헌 (63)
- Brown CM, "Outbreak of SARS-CoV-2 infections, including COVID-19 vaccine breakthrough infections, associated with large public gatherings-Barnstable County, Massachusetts, July 2021", MMWR Morb Mortal Wkly Rep, 70, pp.1059~1062 (2021)
- Dagpunar J, "Interim estimates of increased transmissibility, growth rate, and reproduction number of the COVID-19 B.1.617.2 variant of concern in the United Kingdom", medRxiv, doi:10.1101, 2021 (2021)
- Liu Y, "The reproductive number of the delta variant of SARS-CoV-2 is far higher compared to the ancestral SARS-CoV-2 virus", J Travel Med, pp.taab124~ (2021)
- Li B, "Viral infection and transmission in a large, well-traced outbreak caused by the SARS-CoV-2 delta variant", medRxiv. doi:10.1101, 2021 (2021)
- Ong SWX, "Clinical and virological features of SARS-CoV-2 variants of concern: a retrospective cohort study comparing B.1.1.7(alpha), B.1.315 (beta), and B.1.617.2 (delta)", Clin Infect Dis, pp.ciab721~ (2021)
- Riemersma KK, "Shedding of infectious SARS-CoV-2 despite vaccination", medRxiv. doi: 10.1101, 2021 (2021)
- Shi Q, "Rapid global spread of the SARS-CoV-2 delta(B. 1. 617. 2)variant : spatiotemporal variation and public health impact", Zoonoses, 1, pp.1~6 (2021)
- Lopez Bernal J, "Effectiveness of COVID-19 vaccines against the B. 1. 617. 2(delta)variant", N Engl J Med, 385, pp.585~594 (2021)
- Sheikh A, "SARS-CoV-2 delta VOC in Scotland: demographics, risk of hospital admission, and vaccine effectiveness", Lancet, 397, pp.2461~2462 (2021)
- Li W, "Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus", Nature, 426, pp.450~454 (2003)
- Chen Y, "Structure analysis of the receptor binding of 2019-nCoV", Biochem Biophys Res Commun, 525, pp.135~140 (2020)
- Lan J, "Structure of the SARSCoV-2 spike receptor-binding domain bound to the ACE2 receptor", Nature, 581, pp.215~220 (2020)
- Shang J, "Structural basis of receptor recognition by SARS-CoV-2", Nature, 581, pp.221~224 (2020)
- Song W, "Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2", PLoS Pathog, 14, pp.e1007236~ (2018)
- Wrapp D, "Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation", Science, 367, pp.1260~1263 (2020)
- Yan R, "Structural basis for the recognition of SARS-CoV-2 by fulllength human ACE2", Science, 367, pp.1444~1448 (2020)
- Yuan M, "A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV", Science, 368, pp.630~633 (2020)
- Yuan Y, "Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains", Nat Commun, 8, pp.15092~ (2017)
- Creech CB, "SARS-CoV-2 vaccines", JAMA, 325, pp.1318~1320 (2021)
- 홍재우, "Structure of SARS-CoV-2 Spike Glycoprotein for Therapeutic and Preventive Target", Immune Network, 21(1), pp.1~17 (2021), 대한면역학회[DOI]
- Sinae Kim, "The Progression of SARS Coronavirus 2 (SARS-CoV2): Mutation in the Receptor Binding Domain of Spike Gene", Immune Network, 20(5), pp.1~11 (2020), 대한면역학회[DOI]
- Martínez-Flores D, "SARS-CoV-2 vaccines based on the spike glycoprotein and implications of new viral variants", Front Immunol, 12, pp.701501~ (2021)
- Kim B, "The interleukin-1α precursor is biologically active and is likely a key alarmin in the IL-1 family of cytokines", Front Immunol, 4, pp.391~ (2013)
- Areum Kwak, "Intracellular interleukin (IL)-1 family cytokine processing enzyme", Archives of Pharmacal Research, 39(11), pp.1556~1564 (2016), 대한약학회
- Lee S, "Proinsulin shares a motif with interleukin-1α(IL-1α)and induces inflammatory cytokine via interleukin-1 receptor 1", J Biol Chem, 291, pp.14620~14627 (2016)
- Li F, "Structure of SARS coronavirus spike receptor-binding domain complexed with receptor", Science, 309, pp.1864~1868 (2005)
- Wang Q, "Structural and functional basis of SARS-CoV-2 entry by using human ACE2", Cell, 181, pp.894~904.e9 (2020)
- Chen RE, "In vivo monoclonal antibody efficacy against SARS-CoV-2 variant strains", Nature, 596, pp.103~108 (2021)
- Taylor PC, "Neutralizing monoclonal antibodies for treatment of COVID-19", Nat Rev Immunol, 21, pp.382~393 (2021)
- Gao Q, "Development of an inactivated vaccine candidate for SARS-CoV-2", Science, 369, pp.77~81 (2020)
- Corbett KS, "SARS-CoV-2 mRNA vaccine design enabled by prototype pathogen preparedness", Nature, 586, pp.567~571 (2020)
- Folegatti PM, "Safety and immunogenicity of the ChAdOx1 nCoV-19 vaccine against SARS-CoV-2 : a preliminary report of a phase 1", 2, single-blind, randomised controlled trial, 2020, pp.396, 467~478
- Frater J, "Safety and immunogenicity of the ChAdOx1 nCoV-19(AZD1222)vaccine against SARS-CoV-2 in HIV infection : a single-arm substudy of a phase 2", 3 clinical trial, 2021, pp.8, e474~e485
- Hassan AO, "A single-dose intranasal ChAd vaccine protects upper and lower respiratory tracts against SARSCoV-2", Cell, 183, pp.169~184.e13 (2020)
- Keech C, "Phase 1-2 trial of a SARS-CoV-2 recombinant spike protein nanoparticle vaccine", N Engl J Med, 383, pp.2320~2332 (2020)
- Wang J, "New strategy for COVID-19 vaccination : targeting the receptor-binding domain of the SARSCoV-2 spike protein", Cell Mol Immunol, 18, pp.243~244 (2021)
- Yang J, "A vaccine targeting the RBD of the S protein of SARS-CoV-2 induces protective immunity", Nature, 586, pp.572~577 (2020)
- Arif TB, "The 501.V2 and B.1.1.7 variants of coronavirus disease 2019 (COVID-19): a new time-bomb in the making?", Infect Control Hosp Epidemiol, 2021, pp.1~2 (2021)
- Davies NG, "Estimated transmissibility and impact of SARS-CoV-2 lineage B.1.1.7 in England", Science, 372, pp.eabg3055~ (2021)
- Wu K, "mRNA-1273 vaccine induces neutralizing antibodies against spike mutants from global SARS-CoV-2 variants", bioRxiv. doi: 10.1101, 2021 (2021)
- Barrett CT, "Effect of clinical isolate or cleavage site mutations in the SARS-CoV-2 spike protein on protein stability, cleavage, and cell-cell fusion", J Biol Chem, 297, pp.100902~ (2021)
- Belouzard S, "Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites", Proc Natl Acad Sci U S A, 106, pp.5871~5876 (2009)
- Simmons G, "Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry", Proc Natl Acad Sci U S A, 102, pp.11876~11881 (2005)
- Simmons G, "Proteolytic activation of the SARS-coronavirus spike protein : cutting enzymes at the cutting edge of antiviral research", Antiviral Res, 100, pp.605~614 (2013)
- Claro IM, "Local transmission of SARS-CoV-2 lineage B. 1. 1. 7, Brazil, December 2020", Emerg Infect Dis, 27, pp.970~972 (2021)
- Gidari A, "Cross-neutralization of SARS-CoV-2 B. 1. 1. 7 and P. 1 variants in vaccinated, convalescent and P. 1 infected", J Infect, 83, pp.467~472 (2021)
- Wang P, "Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization", bioRxiv. doi:10.1101, 2021 (2021)
- Yadav PD, "Isolation and characterization of the new SARS-CoV-2 variant in travellers from the United Kingdom to India: VUI202012", 01 of the B.1.1.7 lineage, 2021, pp.28, taab009~
- Leung K, "Early transmissibility assessment of the N501Y mutant strains of SARS-CoV-2 in the United Kingdom, October to November 2020", Euro Surveill, 26 (2021)[DOI]
- Planas D, "Reduced sensitivity of SARS-CoV-2 variant delta to antibody neutralization", Nature, 596, pp.276~280 (2021)
- Chen LL, "Impact of SARS-CoV-2 variant-associated RBD mutations on the susceptibility to serum antibodies elicited by COVID-19 infection or vaccination", Clin Infect Dis, pp.ciab656~ (2021)
- Deng X, "Transmission, infectivity, and antibody neutralization of an emerging SARS-CoV-2 variant in California carrying a L452R spike protein mutation", medRxiv. doi:10.1101, 2021 (2021)
- Martin Webb L, "Identification of and surveillance for the SARS-CoV-2 variants B. 1. 427 and B. 1. 429-Colorado, January-March 2021", MMWR Morb Mortal Wkly Rep, 70, pp.717~718 (2021)
- Ozer EA, "Coincident rapid expansion of two SARS-CoV-2 lineages with enhanced infectivity in Nigeria", medRxiv. doi: 10.1101, 2021 (2021)
- Annavajhala MK, "Emergence and expansion of the SARS-CoV-2 variant B.1.526 identified in New York", medRxiv . doi: 10.1101, 2021 (2021)
- Collier DA, "Sensitivity of SARS-CoV-2 B. 1. 1. 7 to mRNA vaccine-elicited antibodies", Nature, 593, pp.136~141 (2021)
- Emary KR, "Efficacy of ChAdOx1 nCoV-19(AZD1222)vaccine against SARS-CoV-2 variant of concern 202012", 01(B. 1. 1. 7) : an exploratory analysis of a randomised controlled trial, 2021, pp.397, 1351~1362
- Wang P, "Antibody resistance of SARS-CoV-2 variants B. 1. 351 and B. 1. 1. 7", Nature, 593, pp.130~135 (2021)
- Jangra S, "SARS-CoV-2 spike E484K mutation reduces antibody neutralisation", Lancet Microbe, 2, pp.e283~e284 (2021)
- Greaney AJ, "Comprehensive mapping of mutations in the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human plasma antibodies", Cell Host Microbe, 29, pp.463~476.e6 (2021)
- McCallum M, "SARS-CoV-2 immune evasion by the B. 1. 427", B. 1. 429 variant of concern, 2021, pp.373, 648~654
- Elbe S, "Data, disease and diplomacy : GISAID's innovative contribution to global health", Glob Chall, 1, pp.33~46 (2017)
- Liu C, "Reduced neutralization of SARS-CoV-2 B. 1. 617 by vaccine and convalescent serum", Cell, 184, pp.4220~4236.e13 (2021)
