Structure of SARS-CoV-2 Spike Glycoprotein for Therapeutic and Preventive Target
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The global crisis caused by the coronavirus disease 2019 (COVID-19) led to the most significant economic loss and human deaths after World War II. The pathogen causing this disease is a novel virus called the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). As of December 2020, there have been 80.2 million confirmed patients, and the mortality rate is known as 2.16% globally. A strategy to protect a host from SARS-CoV-2 is by suppressing intracellular viral replication or preventing viral entry. We focused on the spike glycoprotein that is responsible for the entry of SARS-CoV-2 into the host cell. Recently, the US Food and Drug Administration/EU Medicines Agency authorized a vaccine and antibody to treat COVID-19 patients by emergency use approval in the absence of long-term clinical trials. Both commercial and academic efforts to develop preventive and therapeutic agents continue all over the world. In this review, we present a perspective on current reports about the spike glycoprotein of SARS-CoV-2 as a therapeutic target.
Abstract
The global crisis caused by the coronavirus disease 2019 (COVID-19) led to the most significant economic loss and human deaths after World War II. The pathogen causing this disease is a novel virus called the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). As of December 2020, there have been 80.2 million confirmed patients, and the mortality rate is known as 2.16% globally. A strategy to protect a host from SARS-CoV-2 is by suppressing intracellular viral replication or preventing viral entry. We focused on the spike glycoprotein that is responsible for the entry of SARS-CoV-2 into the host cell. Recently, the US Food and Drug Administration/EU Medicines Agency authorized a vaccine and antibody to treat COVID-19 patients by emergency use approval in the absence of long-term clinical trials. Both commercial and academic efforts to develop preventive and therapeutic agents continue all over the world. In this review, we present a perspective on current reports about the spike glycoprotein of SARS-CoV-2 as a therapeutic target.
참고문헌 (114)
- Huang C, "Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China", Lancet, 395, pp.497~506 (2020)
- "WHO coronavirus disease (COVID-19) dashboard"[URL]
- Chan SW, "Current and future direct-acting antivirals against COVID-19", Front Microbiol, 11, pp.587944~ (2020)
- "Report of the WHO-China joint mission on coronavirus disease 2019(COVID-19)"[URL]
- Dai L, "Viral targets for vaccines against COVID-19", Nat Rev Immunol, 21, pp.73~82 (2021)
- Gorbalenya AE, "Nidovirales : evolving the largest RNA virus genome", Virus Res, 117, pp.17~37 (2006)
- Philip V’kovski, "Coronavirus biology and replication: implications for SARS-CoV-2", Nature Reviews Microbiology, 19(3), pp.155~170 (2021), Springer Science and Business Media LLC[DOI]
- Tizard IR, "Vaccination against coronaviruses in domestic animals", Vaccine, 38, pp.5123~5130 (2020)
- "World Health Organization"[URL]
- Zhou P, "A pneumonia outbreak associated with a new coronavirus of probable bat origin", Nature, 579, pp.270~273 (2020)
- Gao Q, "Development of an inactivated vaccine candidate for SARS-CoV-2", Science, 369, pp.77~81 (2020)
- Mercado NB, "Single-shot Ad26 vaccine protects against SARS-CoV-2 in rhesus macaques", Nature, 586, pp.583~588 (2020)
- Wang H, "Development of an inactivated vaccine candidate, BBIBP-CorV, with potent protection against SARS-CoV-2", Cell, 182, pp.713.e9~721.e9 (2020)
- Yu J, "DNA vaccine protection against SARS-CoV-2 in rhesus macaques", Science, 369, pp.806~811 (2020)
- Bloch EM, "Deployment of convalescent plasma for the prevention and treatment of COVID-19", J Clin Invest, 130, pp.2757~2765 (2020)
- Burrage DR, "Immunomodulatory drugs in the management of SARS-CoV-2", Front Immunol, 11, pp.1844~ (2020)
- Monica Fung, "Treatment of immunocompromised COVID‐19 patients with convalescent plasma", Transplant Infectious Disease, 23(2) (2021), Wiley[DOI]
- Hueso T, "Convalescent plasma therapy for B-cell-depleted patients with protracted COVID-19", Blood, 136, pp.2290~2295 (2020)
- Liu X, "High-dose intravenous immunoglobulins in the treatment of severe acute viral pneumonia : the known mechanisms and clinical effects", Front Immunol, 11, pp.1660~ (2020)
- Shen C, "Treatment of 5 critically ill patients with COVID-19 with convalescent plasma", JAMA, 323, pp.1582~1589 (2020)
- Frangoul H, "CRISPR-Cas9 gene editing for sickle cell disease and β-thalassemia", N Engl J Med, 384, pp.252~260 (2021)
- Mahase E, "Covid-19: FDA authorises neutralising antibody bamlanivimab for non-admitted patients", BMJ, 371, pp.m4362~ (2020)
- Addetia A, "Neutralizing antibodies correlate with protection from SARS-CoV-2 in humans during a fishery vessel outbreak with a high attack rate", J Clin Microbiol, 58, pp.e02107~e02120 (2020)
- Chen J, "Cellular immune responses to severe acute respiratory syndrome coronavirus(SARS-CoV)infection in senescent BALB", c mice : CD4+T cells are important in control of SARS-CoV infection, 2010, pp.84, 1289~1301
- Sun J, "Generation of a broadly useful model for COVID-19 pathogenesis, vaccination, and treatment", Cell, 182, pp.734.e5~743.e5 (2020)
- Zhao J, "Rapid generation of a mouse model for Middle East respiratory syndrome", Proc Natl Acad Sci U S A, 111, pp.4970~4975 (2014)
- Zhao J, "T cell responses are required for protection from clinical disease and for virus clearance in severe acute respiratory syndrome coronavirus-infected mice", J Virol, 84, pp.9318~9325 (2010)
- Mathew D, "Deep immune profiling of COVID-19 patients reveals distinct immunotypes with therapeutic implications", Science, 369, pp.eabc8511~ (2020)
- Sekine T, "Robust T cell immunity in convalescent individuals with asymptomatic or mild COVID-19", Cell, 183, pp.158.e14~168.e14 (2020)
- Zhu L, "Single-cell sequencing of peripheral mononuclear cells reveals distinct immune response landscapes of COVID-19and influenza patients", Immunity, 53, pp.685.e3~696.e3 (2020)
- Lee WS, "Antibody-dependent enhancement and SARS-CoV-2 vaccines and therapies", Nat Microbiol, 5, pp.1185~1191 (2020)
- Rey FA, "The bright and the dark side of human antibody responses to flaviviruses : lessons for vaccine design", EMBO Rep, 19, pp.206~224 (2018)
- Halstead SB, "Dengue viruses and mononuclear phagocytes. I. Infection enhancement by non-neutralizing antibody", J Exp Med, 146, pp.201~217 (1977)
- Halstead SB, "Dengue viruses and mononuclear phagocytes. II. Identity of blood and tissue leukocytes supporting in vitro infection", J Exp Med, 146, pp.218~229 (1977)
- Katzelnick LC, "Zika virus infection enhances future risk of severe dengue disease", Science, 369, pp.1123~1128 (2020)
- Hohdatsu T, "A study on the mechanism of antibodydependent enhancement of feline infectious peritonitis virus infection in feline macrophages by monoclonal antibodies", Arch Virol, 120, pp.207~217 (1991)
- Takano T, "Antibody-dependent enhancement occurs upon re-infection with the identical serotype virus in feline infectious peritonitis virus infection", J Vet Med Sci, 70, pp.1315~1321 (2008)
- Takano T, "Pathogenesis of oral type I feline infectious peritonitis virus(FIPV)infection : antibody-dependent enhancement infection of cats with type I FIPV via the oral route", J Vet Med Sci, 81, pp.911~915 (2019)
- Vennema H, "Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization", J Virol, 64, pp.1407~1409 (1990)
- Jaume M, "Anti-severe acute respiratory syndrome coronavirus spike antibodies trigger infection of human immune cells via a pH-and cysteine protease-independent FcγR pathway", J Virol, 85, pp.10582~10597 (2011)
- Kam YW, "Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcγRII-dependent entry into B cells in vitro", Vaccine, 25, pp.729~740 (2007)
- Liu L, "Anti-spike IgG causes severe acute lung injury by skewing macrophage responses during acute SARS-CoV infection", JCI Insight, 4, pp.e123158~ (2019)
- Wan Y, "Molecular mechanism for antibody-dependent enhancement of coronavirus entry", J Virol, 94, pp.e02015~e02019 (2020)
- Wang Q, "Immunodominant SARS coronavirus epitopes in humans elicited both enhancing and neutralizing effects on infection in nonhuman primates", ACS Infect Dis, 2, pp.361~376 (2016)
- Wang SF, "Antibody-dependent SARS coronavirus infection is mediated by antibodies against spike proteins", Biochem Biophys Res Commun, 451, pp.208~214 (2014)
- Bolles M, "A double-inactivated severe acute respiratory syndrome coronavirus vaccine provides incomplete protection in mice and induces increased eosinophilic proinflammatory pulmonary response upon challenge", J Virol, 85, pp.12201~12215 (2011)
- Deming D, "Vaccine efficacy in senescent mice challenged with recombinant SARS-CoV bearing epidemic and zoonotic spike variants", PLoS Med, 3, pp.e525~ (2006)
- Tseng CT, "Immunization with SARS coronavirus vaccines leads to pulmonary immunopathology on challenge with the SARS virus", PLoS One, 7, pp.e35421~ (2012)
- Yasui F, "Prior immunization with severe acute respiratory syndrome(SARS)-associated coronavirus(SARS-CoV)nucleocapsid protein causes severe pneumonia in mice infected with SARS-CoV", J Immunol, 181, pp.6337~6348 (2008)
- Luo F, "Evaluation of antibody-dependent enhancement of SARS-CoV infection in rhesus macaques immunized with an inactivated SARS-CoV vaccine", Virol Sin, 33, pp.201~204 (2018)
- Qin E, "Immunogenicity and protective efficacy in monkeys of purified inactivated Vero-cell SARS vaccine", Vaccine, 24, pp.1028~1034 (2006)
- 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)
- 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)
- 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)
- Blobel G, "Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma", J Cell Biol, 67, pp.835~851 (1975)
- Walter P, "Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein(SRP)binds to in-vitro-assembled polysomes synthesizing secretory protein", J Cell Biol, 91, pp.545~550 (1981)
- Sharpe HJ, "A comprehensive comparison of transmembrane domains reveals organelle-specific properties", Cell, 142, pp.158~169 (2010)
- 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)
- Millet JK, "Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein", Proc Natl Acad Sci U S A, 111, pp.15214~15219 (2014)
- Keidar S, "ACE2 of the heart : from angiotensin I to angiotensin(1-7)", Cardiovasc Res, 73, pp.463~469 (2007)
- Shang J, "Structural basis of receptor recognition by SARS-CoV-2", Nature, 581, pp.221~224 (2020)
- Wang Q, "Structural and functional basis of SARS-CoV-2 entry by using human ACE2", Cell, 181, pp.894.e9~904.e9 (2020)
- Yan R, "Structural basis for the recognition of SARS-CoV-2 by fulllength human ACE2", Science, 367, pp.1444~1448 (2020)
- Hoffmann M, "SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor", Cell, 181, pp.271.e8~280.e8 (2020)
- Wang Q, "Structural basis for RNA replication by the SARS-CoV-2 polymerase", Cell, 182, pp.417.e13~428.e13 (2020)
- Wong SK, "A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2", J Biol Chem, 279, pp.3197~3201 (2004)
- Zhang H, "Angiotensin-converting enzyme 2(ACE2)as a SARSCoV-2 receptor : molecular mechanisms and potential therapeutic target", Intensive Care Med, 46, pp.586~590 (2020)
- Walls AC, "Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein", Cell, 181, pp.281.e6~292.e6 (2020)
- Li F, "Structure of SARS coronavirus spike receptor-binding domain complexed with receptor", Science, 309, pp.1864~1868 (2005)
- Li W, "Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2", EMBO J, 24, pp.1634~1643 (2005)
- Shah M, "Mutations in the SARS-CoV-2 spike RBD are responsible for stronger ACE2 binding and poor anti-SARS-CoV mAbs cross-neutralization", Comput Struct Biotechnol J, 18, pp.3402~3414 (2020)
- Guan Q, "A genetic barcode of SARS-CoV-2 for monitoring global distribution of different clades during the COVID-19 pandemic", Int J Infect Dis, 100, pp.216~223 (2020)
- 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]
- Jessica A. Plante, "Spike mutation D614G alters SARS-CoV-2 fitness", Nature, 592(7852), pp.116~121 (2021), Springer Science and Business Media LLC[DOI]
- Korber B, "Tracking changes in SARS-CoV-2 spike : evidence that D614G increases infectivity of the COVID-19 virus", Cell, 182, pp.812.e19~827.e19 (2020)
- Adebalİ O, "Phylogenetic analysis of SARS-CoV-2genomes in Turkey", Turk J Biol, 44, pp.146~156 (2020)
- Mahase E, "Covid-19 : Novavax vaccine efficacy is 86% against UK variant and 60% against South African variant", BMJ, 372, pp.n296~ (2021)
- Julian W. Tang, "Introduction of the South African SARS-CoV-2 variant 501Y.V2 into the UK", Journal of Infection, 82(4), pp.e8~e10 (2021), Elsevier BV[DOI]
- Xie X, "Neutralization of SARS-CoV-2 spike 69", 70 deletion, E484K, and N501Y variants by BNT162b2 vaccineelicited sera, 2021.01.27.427998, pp.2021, ~
- Lu R, "Genomic characterisation and epidemiology of 2019 novel coronavirus : implications for virus origins and receptor binding", Lancet, 395, pp.565~574 (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, "Cell entry mechanisms of SARS-CoV-2", Proc Natl Acad Sci U S A, 117, pp.11727~11734 (2020)
- Wrapp D, "Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation", Science, 367, pp.1260~1263 (2020)
- Kalathiya U, "Highly conserved homotrimer cavity formed by the SARS-CoV-2 spike glycoprotein : a novel binding site", J Clin Med, 9, pp.1473~ (2020)
- Osmair Vital de Oliveira, "Repurposing approved drugs as inhibitors of SARS-CoV-2 S-protein from molecular modeling and virtual screening", Journal of Biomolecular Structure and Dynamics, 39(11), pp.3924~3933 (2021), Informa UK Limited[DOI]
- Wahedi HM, "Stilbene-based natural compounds as promising drug candidates against COVID-19", J Biomol Struct Dyn (2020)[DOI]
- Bongini P, "A possible strategy to fight COVID-19 : interfering with spike glycoprotein trimerization", Biochem Biophys Res Commun, 528, pp.35~38 (2020)
- Drew ED, "Identification of a druggable binding pocket in the spike protein reveals a key site for existing drugs potentially capable of combating Covid-19 infectivity", BMC Mol Cell Biol, 21, pp.49~ (2020)
- Barnes CO, "Structures of human antibodies bound to SARS-CoV-2 spike reveal common epitopes and recurrent features of antibodies", Cell, 182, pp.828.e16~842.e16 (2020)
- Brouwer PJ, "Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability", Science, 369, pp.643~650 (2020)
- Cao Y, "Potent neutralizing antibodies against SARS-CoV-2 identified by high-throughput single-cell sequencing of convalescent patients' B cells", Cell, 182, pp.73.e16~84.e16 (2020)
- Ju B, "Human neutralizing antibodies elicited by SARS-CoV-2 infection", Nature, 584, pp.115~119 (2020)
- Wu Y, "A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2", Science, 368, pp.1274~1278 (2020)
- Wu Y, "Identification of human single-domain antibodies against SARS-CoV-2", Cell Host Microbe, 27, pp.891.e5~898.e5 (2020)
- Hansen J, "Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail", Science, 369, pp.1010~1014 (2020)
- Monteil V, "Inhibition of SARS-CoV-2 infections in engineered human tissues using clinicalgrade soluble human ACE2", Cell, 181, pp.905.e7~913.e7 (2020)
- Lei C, "Neutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig", Nat Commun, 11, pp.2070~ (2020)
- Ou X, "Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV", Nat Commun, 11, pp.1620~ (2020)
- Wang L, "Spike glycoprotein-mediated entry of SARS coronaviruses", Viruses, 12, pp.1289~ (2020)
- Xia S, "Fusion mechanism of 2019-nCoV and fusion inhibitors targeting HR1 domain in spike protein", Cell Mol Immunol, 17, pp.765~767 (2020)
- Zhu Y, "Design of potent membrane fusion inhibitors against SARS-CoV-2, an emerging coronavirus with high fusogenic activity", J Virol, 94, pp.e00635~e00620 (2020)
- Ling R, "In silico design of antiviral peptides targeting the spike protein of SARS-CoV-2", Peptides, 130, pp.170328~ (2020)
- Romeo A, "Targeting the SARS-CoV-2 spike glycoprotein prefusion conformation : virtual screening and molecular dynamics simulations applied to the identification of potential fusion inhibitors", Virus Res, 286, pp.198068~ (2020)
- Su S, "A peptide-based HIV-1 fusion inhibitor with two tail-anchors and palmitic acid exhibits substantially improved in vitro and ex vivo anti-HIV-1 activity and prolonged in vivo half-life", Molecules, 24, pp.1134~ (2019)
- Xia S, "A pan-coronavirus fusion inhibitor targeting the HR1 domain of human coronavirus spike", Sci Adv, 5, pp.eaav4580~ (2019)
- Bi W, "IgG Fc-binding motifconjugated HIV-1 fusion inhibitor exhibits improved potency and in vivo half-life : potential application in combination with broad neutralizing antibodies", PLoS Pathog, 15, pp.e1008082~ (2019)
- Cheng S, "Glycosylated enfuvirtide : a long-lasting glycopeptide with potent anti-HIV activity", J Med Chem, 58, pp.1372~1379 (2015)
- Wang C, "Long-acting HIV-1 fusion inhibitory peptides and their mechanisms of action", Viruses, 11, pp.811~ (2019)
- Zorzi A, "Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides", Nat Commun, 8, pp.16092~ (2017)
- Werle M, "Strategies to improve plasma half life time of peptide and protein drugs", Amino Acids, 30, pp.351~367 (2006)
- Mathieu C, "Prevention of measles virus infection by intranasal delivery of fusion inhibitor peptides", J Virol, 89, pp.1143~1155 (2015)
- Mathieu C, "Fusion inhibitory lipopeptides engineered for prophylaxis of Nipah virus in primates", J Infect Dis, 218, pp.218~227 (2018)
