Health
Broadly neutralizing antibodies to SARS-CoV-2 and other human coronaviruses
Mackay, I. M. & Arden, K. E. MERS coronavirus: diagnostics, epidemiology and transmission. Virol. J. 12, 222 (2015).
Stadler, K. et al. SARS–beginning to understand a new virus. Nat. Rev. Microbiol. 1, 209–218 (2003).
Umakanthan, S. et al. Origin, transmission, diagnosis and management of coronavirus disease 2019 (COVID-19). Postgrad. Med. J. 96, 753–758 (2020).
Hu, B., Guo, H., Zhou, P. & Shi, Z. L. Characteristics of SARS-CoV-2 and COVID-19. Nat. Rev. Microbiol. 19, 141–154 (2021).
Coronaviridae Study Group of the International Committee on Taxonomy of Viruses. The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2. Nat. Microbiol. 5, 536–544 (2020).
Zhou, P. et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 579, 270–273 (2020).
Kirtipal, N., Bharadwaj, S. & Kang, S. G. From SARS to SARS-CoV-2, insights on structure, pathogenicity and immunity aspects of pandemic human coronaviruses. Infect. Genet. Evol. 85, 104502 (2020).
Wang, M. Y. et al. SARS-CoV-2: structure, biology, and structure-based therapeutics development. Front. Cell Infect. Microbiol. 10, 587269 (2020).
Jaworski, J. P. Neutralizing monoclonal antibodies for COVID-19 treatment and prevention. Biomed. J. 44, 7–17 (2021).
Oran, D. P. & Topol, E. J. The proportion of SARS-CoV-2 infections that are asymptomatic: a systematic review. Ann. Intern. Med. 174, 655–662 (2021).
Sharma, A., Ahmad Farouk, I. & Lal, S. K. COVID-19: a review on the novel coronavirus disease evolution, transmission, detection, control and prevention. Viruses 13, 202 (2021).
Woo, P. C. et al. Discovery of seven novel mammalian and avian coronaviruses in the genus deltacoronavirus supports bat coronaviruses as the gene source of alphacoronavirus and betacoronavirus and avian coronaviruses as the gene source of gammacoronavirus and deltacoronavirus. J. Virol. 86, 3995–4008 (2012).
Fouchier, R. A. et al. A previously undescribed coronavirus associated with respiratory disease in humans. Proc. Natl Acad. Sci. USA 101, 6212–6216 (2004).
Llanes, A. et al. Betacoronavirus genomes: how genomic information has been used to deal with past outbreaks and the COVID-19 pandemic. Int. J. Mol. Sci. 21, 4546 (2020).
Huang, Y., Yang, C., Xu, X. F., Xu, W. & Liu, S. W. Structural and functional properties of SARS-CoV-2 spike protein: potential antivirus drug development for COVID-19. Acta Pharmacol. Sin. 41, 1141–1149 (2020).
Li, M. Y., Li, L., Zhang, Y. & Wang, X. S. Expression of the SARS-CoV-2 cell receptor gene ACE2 in a wide variety of human tissues. Infect. Dis. Poverty 9, 45 (2020).
de Wit, E., van Doremalen, N., Falzarano, D. & Munster, V. J. SARS and MERS: recent insights into emerging coronaviruses. Nat. Rev. Microbiol. 14, 523–534 (2016).
Raj, V. S. et al. Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC. Nature 495, 251–254 (2013).
Li, W. Delving deep into the structural aspects of a furin cleavage site inserted into the spike protein of SARS-CoV-2: a structural biophysical perspective. Biophys. Chem. 264, 106420 (2020).
Bestle, D. et al. TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells. Life Sci. Alliance 3, e202000786 (2020).
Bayati, A., Kumar, R., Francis, V. & McPherson, P. S. SARS-CoV-2 infects cells after viral entry via clathrin-mediated endocytosis. J. Biol. Chem. 296, 100306 (2021).
Moog, C. et al. Protective effect of vaginal application of neutralizing and nonneutralizing inhibitory antibodies against vaginal SHIV challenge in macaques. Mucosal Immunol. 7, 46–56 (2014).
Cheeseman, H. M. et al. Broadly neutralizing antibodies display potential for prevention of HIV-1 infection of mucosal tissue superior to that of nonneutralizing antibodies. J. Virol. 91, e01762-16 (2017).
Tan, G. S. et al. Broadly-reactive neutralizing and non-neutralizing antibodies directed against the H7 influenza virus hemagglutinin reveal divergent mechanisms of protection. PLoS Pathog. 12, e1005578 (2016).
Yang, F. et al. Generation of neutralizing and non-neutralizing monoclonal antibodies against H7N9 influenza virus. Emerg. Microbes Infect. 9, 664–675 (2020).
Alter, G. & Moody, M. A. The humoral response to HIV-1: new insights, renewed focus. J. Infect. Dis. 202, S315–S322 (2010).
Chi, X. et al. A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2. Science 369, 650–655 (2020).
Suryadevara, N. et al. Neutralizing and protective human monoclonal antibodies recognizing the N-terminal domain of the SARS-CoV-2 spike protein. Cell 184, 2316–2331 (2021).
Liu, L. et al. Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike. Nature 584, 450–456 (2020). This article describes the isolation of a panel of SARS-Co-2 NTD-targeting and RBD-targeting nAbs summarized in this Review.
Cerutti, G. et al. Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite. Cell Host Microbe 29, 819–833 (2021).
Lok, S. M. An NTD supersite of attack. Cell Host Microbe 29, 744–746 (2021).
Wang, P. et al. Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7. Nature 593, 130–135 (2021).
McCallum, M. et al. N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2. Cell 184, 2332–2347 (2021).
Cerutti, G. et al. Neutralizing antibody 5-7 defines a distinct site of vulnerability in SARS-CoV-2 spike N-terminal domain. Cell Rep. 37, 109928 (2021).
Wang, X. et al. Homologous or heterologous booster of inactivated vaccine reduces SARS-CoV-2 Omicron variant escape from neutralizing antibodies. Emerg. Microbes Infect. 11, 477–481 (2022).
Ai, J. et al. Antibody evasion of SARS-CoV-2 Omicron BA.1, BA.1.1, BA.2, and BA.3 sub-lineages. Cell Host Microbe 30, 1077–1083 (2022).
Makdasi, E. et al. The neutralization potency of anti-SARS-CoV-2 therapeutic human monoclonal antibodies is retained against viral variants. Cell Rep. 36, 109679 (2021).
Noy-Porat, T. et al. Therapeutic antibodies, targeting the SARS-CoV-2 spike N-terminal domain, protect lethally infected K18-hACE2 mice. iScience 24, 102479 (2021).
Haslwanter, D. et al. A combination of receptor-binding domain and N-terminal domain neutralizing antibodies limits the generation of SARS-CoV-2 spike neutralization-escape mutants. mBio 12, e0247321 (2021).
Wang, Z. et al. Analysis of memory B cells identifies conserved neutralizing epitopes on the N-terminal domain of variant SARS-Cov-2 spike proteins. Immunity 55, 998–1012 (2022).
Barnes, C. O. et al. SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies. Nature 588, 682–687 (2020). This key article describes the classification of RBD-directed antibodies we adopted in this Review.
Shi, R. et al. A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2. Nature 584, 120–124 (2020).
Kim, C. et al. A therapeutic neutralizing antibody targeting receptor binding domain of SARS-CoV-2 spike protein. Nat. Commun. 12, 288 (2021).
Banach, B. B. et al. Paired heavy- and light-chain signatures contribute to potent SARS-CoV-2 neutralization in public antibody responses. Cell Rep. 37, 109771 (2021).
Annavajhala, M. K. et al. Emergence and expansion of SARS-CoV-2 B.1.526 after identification in New York. Nature 597, 703–708 (2021).
Wang, P. et al. Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization. Cell Host Microbe 29, 747–751 (2021).
Starr, T. N. et al. SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape. Nature 597, 97–102 (2021).
Zhou, T. et al. Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529. Science 376, eabn8897 (2022).
Park, Y. J. et al. Antibody-mediated broad sarbecovirus neutralization through ACE2 molecular mimicry. Science 375, 449–454 (2022).
Cameroni, E. et al. Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift. Nature 602, 664–670 (2022).
Chen, P. et al. SARS-CoV-2 Neutralizing antibody LY-CoV555 in outpatients with Covid-19. N. Engl. J. Med. 384, 229–237 (2021).
Chen, W. H., Hotez, P. J. & Bottazzi, M. E. Potential for developing a SARS-CoV receptor-binding domain (RBD) recombinant protein as a heterologous human vaccine against coronavirus infectious disease (COVID)-19. Hum. Vaccin. Immunother. 16, 1239–1242 (2020).
Hansen, J. et al. Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail. Science 369, 1010–1014 (2020).
Zost, S. J. et al. Potently neutralizing and protective human antibodies against SARS-CoV-2. Nature 584, 443–449 (2020).
Cerutti, G. et al. Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies. Structure 29, 655–663 (2021).
Pinto, D. et al. Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody. Nature 583, 290–295 (2020).
Westendorf, K. et al. LY-CoV1404 (bebtelovimab) potently neutralizes SARS-CoV-2 variants. Cell Rep. https://doi.org/10.1016/j.celrep.2022.110812 (2022).
Wang, L. et al. Ultrapotent antibodies against diverse and highly transmissible SARS-CoV-2 variants. Science 373, eabh1766 (2021).
Fenwick, C. et al. Patient-derived monoclonal antibody neutralizes SARS-CoV-2 Omicron variants and confers full protection in monkeys. Nat. Microbiol. https://doi.org/10.1016/10.1038/s41564-022-01198-6 (2022).
Turelli, P. et al. P2G3 human monoclonal antibody neutralizes SARS-CoV-2 Omicron subvariants including BA.4 and BA.5 and Bebtelovimab escape mutants. Preprint at bioRxiv https://doi.org/10.1101/2022.07.28.501852 (2022).
Wang, Q. et al. Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4 and BA.5. Nature 608, 603–608 (2022).
Cao, Y. et al. Characterizations of enhanced infectivity and antibody evasion of Omicron BA.2.75. Preprint at bioRxiv https://doi.org/10.1101/2022.07.18.500332 (2022).
Luo, S. et al. An Antibody from Single Human VH-rearranging Mouse Neutralizes All SARS-CoV-2 Variants Through BA.5 by Inhibiting Membrane Fusion. Sci. Immuno. https://doi.org/10.1126/sciimmunol.add5446 (2022). This work demonstrates a class 3 mAb, SP1-77, potently neutralizing SARS-CoV-2 by blocking membrane fusion.
Yuan, M. et al. A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV. Science 368, 630–633 (2020).
Wang, P. et al. A monoclonal antibody that neutralizes SARS-CoV-2 variants, SARS-CoV, and other sarbecoviruses. Emerg. Microbes Infect. 11, 147–157 (2022).
Tortorici, M. A. et al. Broad sarbecovirus neutralization by a human monoclonal antibody. Nature 597, 103–108 (2021).
Yuan, M. et al. A broad and potent neutralization epitope in SARS-related coronaviruses. Proc. Natl Acad. Sci. USA 119, e2205784119 (2022).
Rappazzo, C. G. et al. Broad and potent activity against SARS-like viruses by an engineered human monoclonal antibody. Science 371, 823–829 (2021).
Martinez, D. R. et al. A broadly cross-reactive antibody neutralizes and protects against sarbecovirus challenge in mice. Sci. Transl. Med. 14, eabj7125 (2022).
Liu, H. et al. Cross-neutralization of a SARS-CoV-2 antibody to a functionally conserved site is mediated by avidity. Immunity 53, 1272–1280 (2020).
Lv, Z. et al. Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody. Science 369, 1505–1509 (2020).
Yuan, M. et al. Structural basis of a shared antibody response to SARS-CoV-2. Science 369, 1119–1123 (2020).
Wu, Y. et al. A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2. Science 368, 1274–1278 (2020).
Robbiani, D. F. et al. Convergent antibody responses to SARS-CoV-2 in convalescent individuals. Nature 584, 437–442 (2020).
Zhou, D. et al. Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient. Nat. Struct. Mol. Biol. 27, 950–958 (2020).
Kumar, S. et al. Structural insights for neutralization of BA.1 and BA.2 Omicron variants by a broadly neutralizing SARS-CoV-2 antibody. Preprint at bioRxiv https://doi.org/10.1101/2022.05.13.491770 (2022).
Ju, B. et al. Human neutralizing antibodies elicited by SARS-CoV-2 infection. Nature 584, 115–119 (2020).
Li, C. et al. Broad neutralization of SARS-CoV-2 variants by an inhalable bispecific single-domain antibody. Cell 185, 1389–1401 (2022).
Yang, Z. et al. A non-ACE2 competing human single-domain antibody confers broad neutralization against SARS-CoV-2 and circulating variants. Signal. Transduct. Target. Ther. 6, 378 (2021).
Cao, Y. et al. BA.2.12.1, BA.4 and BA.5 escape antibodies elicited by Omicron infection. Nature 608, 593–602 (2022).
Sheward, D. J. et al. Evasion of neutralizing antibodies by Omicron sublineage BA.2.75. Lancet Infect. Dis. https://doi.org/10.1016/S1473-3099(22)00524-2 (2022).
Shrestha, L. B., Tedla, N. & Bull, R. A. Broadly-neutralizing antibodies against emerging SARS-CoV-2 variants. Front. Immunol. 12, 752003 (2021).
Pinto, D. et al. Broad betacoronavirus neutralization by a stem helix-specific human antibody. Science 373, 1109–1116 (2021). This study is the first to identify SH-targeting nAbs that can inhibit all beta-CoV subgenera and reduce viral burden in hamsters infected with SARS-CoV-2.
Zhou, P. et al. A human antibody reveals a conserved site on beta-coronavirus spike proteins and confers protection against SARS-CoV-2 infection. Sci. Transl. Med. 14, eabi9215 (2022).
Shi, W. et al. Vaccine-elicited murine antibody WS6 neutralizes diverse beta-coronaviruses by recognizing a helical stem supersite of vulnerability. Structure https://doi.org/10.1016/j.str.2022.06.004 (2022).
Dacon, C. et al. Broadly neutralizing antibodies target the coronavirus fusion peptide. Science 377, 728–735 (2022). This study is the first to identify FP-targeting nAbs that show broad neutralizing activity against a range of coronaviruses, including Omicron sublineages of SARS-CoV-2.
Low, J. S. et al. ACE2 engagement exposes the fusion peptide to pan-coronavirus neutralizing antibodies. Science 377, 735–742 (2022).
Sun, X. et al. Neutralization mechanism of a human antibody with pan-coronavirus reactivity including SARS-CoV-2. Nat. Microb. 7, 1063–1074 (2022).
Zhao, F. et al. Engineering SARS-CoV-2 neutralizing antibodies for increased potency and reduced viral escape. iScience https://doi.org/10.1016/j.isci.2022.104914 (2022).
Chen, Z. et al. Extremely potent monoclonal antibodies neutralize Omicron and other SARS-CoV-2 variants. Preprint at medRxiv https://doi.org/10.1101/2022.01.12.22269023 (2022).
Wellner, A. et al. Rapid generation of potent antibodies by autonomous hypermutation in yeast. Nat. Chem. Biol. 17, 1057–1064 (2021).
Rouet, R. et al. Potent SARS-CoV-2 binding and neutralization through maturation of iconic SARS-CoV-1 antibodies. MAbs 13, 1922134 (2021).
Liu, M., Li, L., Jin, D. & Liu, Y. Nanobody-A versatile tool for cancer diagnosis and therapeutics. Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. 13, e1697 (2021).
Mitchell, L. S. & Colwell, L. J. Comparative analysis of nanobody sequence and structure data. Proteins 86, 697–706 (2018).
Stanfield, R. L. & Wilson, I. A. Antibody structure. Microbiol. Spectr. https://doi.org/10.1128/microbiolspec.AID-0012-2013 (2014).
Schoof, M. et al. An ultrapotent synthetic nanobody neutralizes SARS-CoV-2 by stabilizing inactive Spike. Science 370, 1473–1479 (2020).
De Gasparo, R. et al. Bispecific IgG neutralizes SARS-CoV-2 variants and prevents escape in mice. Nature 593, 424–428 (2021).
Cho, H. et al. Bispecific antibodies targeting distinct regions of the spike protein potently neutralize SARS-CoV-2 variants of concern. Sci. Transl. Med. 13, eabj5413 (2021).
Ku, Z. et al. Engineering SARS-CoV-2 cocktail antibodies into a bispecific format improves neutralizing potency and breadth. Preprint at bioRxiv https://doi.org/10.1101/2022.02.01.478504 (2022).
Li, Z. et al. An engineered bispecific human monoclonal antibody against SARS-CoV-2. Nat. Immunol. 23, 423–430 (2022).
Du, Y. et al. A broadly neutralizing humanized ACE2-targeting antibody against SARS-CoV-2 variants. Nat. Commun. 12, 5000 (2021).
Chen, Y. et al. ACE2-targeting monoclonal antibody as potent and broad-spectrum coronavirus blocker. Signal. Transduct. Target. Ther. 6, 315 (2022).
Qi, H., Liu, B., Wang, X. & Zhang, L. The humoral response and antibodies against SARS-CoV-2 infection. Nat. Immunol. 23, 1008–1020 (2022).
Zhou, H. et al. Sensitivity to vaccines, therapeutic antibodies, and viral entry inhibitors and advances to counter the SARS-CoV-2 Omicron variant. Clin. Microbiol. Rev. https://doi.org/10.1128/cmr.00014-22 (2022).
Dai, L. & Gao, G. F. Viral targets for vaccines against COVID-19. Nat. Rev. Immunol. 21, 73–82 (2021).
Liu, Z. et al. A novel STING agonist-adjuvanted pan-sarbecovirus vaccine elicits potent and durable neutralizing antibody and T cell responses in mice, rabbits and NHPs. Cell Res. 32, 269–287 (2022). This is the first report about the development of a pan-sarbecovirus vaccine based on a novel adjuvant.
|
Sources 2/ https://www.nature.com/articles/s41577-022-00784-3 The mention sources can contact us to remove/changing this article |
What Are The Main Benefits Of Comparing Car Insurance Quotes Online
LOS ANGELES, CA / ACCESSWIRE / June 24, 2020, / Compare-autoinsurance.Org has launched a new blog post that presents the main benefits of comparing multiple car insurance quotes. For more info and free online quotes, please visit https://compare-autoinsurance.Org/the-advantages-of-comparing-prices-with-car-insurance-quotes-online/ The modern society has numerous technological advantages. One important advantage is the speed at which information is sent and received. With the help of the internet, the shopping habits of many persons have drastically changed. The car insurance industry hasn't remained untouched by these changes. On the internet, drivers can compare insurance prices and find out which sellers have the best offers. View photos The advantages of comparing online car insurance quotes are the following: Online quotes can be obtained from anywhere and at any time. Unlike physical insurance agencies, websites don't have a specific schedule and they are available at any time. Drivers that have busy working schedules, can compare quotes from anywhere and at any time, even at midnight. Multiple choices. Almost all insurance providers, no matter if they are well-known brands or just local insurers, have an online presence. Online quotes will allow policyholders the chance to discover multiple insurance companies and check their prices. Drivers are no longer required to get quotes from just a few known insurance companies. Also, local and regional insurers can provide lower insurance rates for the same services. Accurate insurance estimates. Online quotes can only be accurate if the customers provide accurate and real info about their car models and driving history. Lying about past driving incidents can make the price estimates to be lower, but when dealing with an insurance company lying to them is useless. Usually, insurance companies will do research about a potential customer before granting him coverage. Online quotes can be sorted easily. Although drivers are recommended to not choose a policy just based on its price, drivers can easily sort quotes by insurance price. Using brokerage websites will allow drivers to get quotes from multiple insurers, thus making the comparison faster and easier. For additional info, money-saving tips, and free car insurance quotes, visit https://compare-autoinsurance.Org/ Compare-autoinsurance.Org is an online provider of life, home, health, and auto insurance quotes. This website is unique because it does not simply stick to one kind of insurance provider, but brings the clients the best deals from many different online insurance carriers. In this way, clients have access to offers from multiple carriers all in one place: this website. On this site, customers have access to quotes for insurance plans from various agencies, such as local or nationwide agencies, brand names insurance companies, etc. "Online quotes can easily help drivers obtain better car insurance deals. All they have to do is to complete an online form with accurate and real info, then compare prices", said Russell Rabichev, Marketing Director of Internet Marketing Company. CONTACT: Company Name: Internet Marketing CompanyPerson for contact Name: Gurgu CPhone Number: (818) 359-3898Email: [email protected]: https://compare-autoinsurance.Org/ SOURCE: Compare-autoinsurance.Org View source version on accesswire.Com:https://www.Accesswire.Com/595055/What-Are-The-Main-Benefits-Of-Comparing-Car-Insurance-Quotes-Online View photos
to request, modification Contact us at Here or [email protected]
 |
 |
 |
