{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T06:04:39Z","timestamp":1790661879843,"version":"4.1.0"},"reference-count":98,"publisher":"Portland Press Ltd.","issue":"10","license":[{"start":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T00:00:00Z","timestamp":1789344000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"No funding"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2026,10,21]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The Spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates host cell attachment and entry through the binding of its cognate receptor, angiotensin-converting enzyme 2 (ACE2). This interaction occurs within the receptor-binding domain (RBD) of the Spike protein and is critical to the lifecycle and fitness of SARS-CoV-2. A rigorous analysis of this interaction is crucial to understanding this viral entry mechanism. In the present communication, a biophysical examination of the RBD, ACE2, and their interaction is presented. These studies led to the discovery that disulfide bonds stabilize and protect the RBD from thermal and chemical denaturation. It is further hypothesized that disulfide bond stabilization preserves the ability of the RBD to bind ACE2 following its denaturation. The present hypothesis is supported by the finding that the RBD retains ACE2-binding activity after treatment to high temperatures (95\u00b0C) under non-reducing, but not reducing, conditions. These results suggest a mechanism by which SARS-CoV-2 overcomes environmental stress to preserve its RBD\u2013ACE2 interaction.<\/jats:p>","DOI":"10.1042\/bsr20260440","type":"journal-article","created":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T14:20:43Z","timestamp":1789395643000},"update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Disulfide bonds stabilize the SARS-CoV-2 RBD and preserve binding to ACE2 following thermal denaturation"],"prefix":"10.1042","volume":"46","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5730-2649","authenticated-orcid":false,"given":"Nathan\u00a0R.","family":"McCann","sequence":"first","affiliation":[{"name":"The W.M. Keck Center for Transgene Research and the Department of Chemistry and Biochemistry, The University of Notre Dame, Notre Dame, IN 46556, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0317-9539","authenticated-orcid":false,"given":"Francis\u00a0J.","family":"Castellino","sequence":"additional","affiliation":[{"name":"The W.M. Keck Center for Transgene Research and the Department of Chemistry and Biochemistry, The University of Notre Dame, Notre Dame, IN 46556, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2026,9,29]]},"reference":[{"key":"2026092901415082500_B1","doi-asserted-by":"publisher","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. Engl. J. Med."},{"key":"2026092901415082500_B2","doi-asserted-by":"publisher","first-page":"61","DOI":"10.46234\/ccdcw2020.017","article-title":"A novel coronavirus genome identified in a cluster of pneumonia cases\u2014Wuhan, China 2019\u20132020","volume":"2","author":"Tan","year":"2020","journal-title":"China CDC Wkly"},{"key":"2026092901415082500_B3","doi-asserted-by":"publisher","first-page":"536","DOI":"10.1038\/s41564-020-0695-z","article-title":"The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2","volume":"5","author":"Coronaviridae Study Group of the International Committee on Taxonomy of Viruses","year":"2020","journal-title":"Nat. Microbiol."},{"key":"2026092901415082500_B4","article-title":"Naming the coronavirus disease (COVID-19) and the virus that causes it","author":"WHO"},{"key":"2026092901415082500_B5","doi-asserted-by":"publisher","first-page":"1260","DOI":"10.1126\/science.abb2507","article-title":"Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation","volume":"367","author":"Wrapp","year":"2020","journal-title":"Science"},{"key":"2026092901415082500_B6","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1016\/j.cell.2020.02.058","article-title":"Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein","volume":"181","author":"Walls","year":"2020","journal-title":"Cell"},{"key":"2026092901415082500_B7","doi-asserted-by":"publisher","first-page":"eabe5575","DOI":"10.1126\/sciadv.abe5575","article-title":"Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM","volume":"7","author":"Xu","year":"2021","journal-title":"Sci. Adv."},{"key":"2026092901415082500_B8","doi-asserted-by":"publisher","first-page":"327","DOI":"10.1038\/s41586-020-2772-0","article-title":"Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion","volume":"588","author":"Benton","year":"2020","journal-title":"Nature"},{"key":"2026092901415082500_B9","doi-asserted-by":"publisher","first-page":"8801","DOI":"10.1128\/JVI.77.16.8801-8811.2003","article-title":"The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex","volume":"77","author":"Bosch","year":"2003","journal-title":"J. Virol."},{"key":"2026092901415082500_B10","doi-asserted-by":"publisher","first-page":"270","DOI":"10.1038\/s41586-020-2012-7","article-title":"A pneumonia outbreak associated with a new coronavirus of probable bat origin","volume":"579","author":"Zhou","year":"2020","journal-title":"Nature"},{"key":"2026092901415082500_B11","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1016\/j.cell.2020.02.052","article-title":"SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor","volume":"181","author":"Hoffmann","year":"2020","journal-title":"Cell"},{"key":"2026092901415082500_B12","doi-asserted-by":"publisher","first-page":"562","DOI":"10.1038\/s41564-020-0688-y","article-title":"Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses","volume":"5","author":"Letko","year":"2020","journal-title":"Nat. Microbiol."},{"key":"2026092901415082500_B13","doi-asserted-by":"publisher","first-page":"11157","DOI":"10.1073\/pnas.1708727114","article-title":"Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion","volume":"114","author":"Walls","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026092901415082500_B14","doi-asserted-by":"publisher","first-page":"7001","DOI":"10.1073\/pnas.2002589117","article-title":"Enhanced isolation of SARS-CoV-2 by TMPRSS2-expressing cells","volume":"117","author":"Matsuyama","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026092901415082500_B15","doi-asserted-by":"publisher","first-page":"e107821","DOI":"10.15252\/embj.2021107821","article-title":"TMPRSS2 expression dictates the entry route used by SARS-CoV-2 to infect host cells","volume":"40","author":"Koch","year":"2021","journal-title":"EMBO J."},{"key":"2026092901415082500_B16","doi-asserted-by":"publisher","first-page":"e202000786","DOI":"10.26508\/lsa.202000786","article-title":"TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells","volume":"3","author":"Bestle","year":"2020","journal-title":"Life Sci. Alliance"},{"key":"2026092901415082500_B17","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1038\/s41392-021-00558-8","article-title":"Cathepsin L plays a key role in SARS-CoV-2 infection in humans and humanized mice and is a promising target for new drug development","volume":"6","author":"Zhao","year":"2021","journal-title":"Signal Transduct. Target. Ther."},{"key":"2026092901415082500_B18","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1038\/s41580-021-00418-x","article-title":"Mechanisms of SARS-CoV-2 entry into cells","volume":"23","author":"Jackson","year":"2022","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2026092901415082500_B19","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1126\/science.abb9983","article-title":"Site-specific glycan analysis of the SARS-CoV-2 spike","volume":"369","author":"Watanabe","year":"2020","journal-title":"Science"},{"key":"2026092901415082500_B20","doi-asserted-by":"publisher","first-page":"10053","DOI":"10.1038\/s41598-023-33088-0","article-title":"Site specific N- and O-glycosylation mapping of the spike proteins of SARS-CoV-2 variants of concern","volume":"13","author":"Shajahan","year":"2023","journal-title":"Sci. Rep."},{"key":"2026092901415082500_B21","doi-asserted-by":"publisher","first-page":"188","DOI":"10.1093\/glycob\/cwad007","article-title":"Quantitative profiling of N-glycosylation of SARS-CoV-2 spike protein variants","volume":"33","author":"Xie","year":"2023","journal-title":"Glycobiology"},{"key":"2026092901415082500_B22","doi-asserted-by":"publisher","first-page":"eabq8678","DOI":"10.1126\/sciadv.abq8678","article-title":"Role for N-glycans and calnexin-calreticulin chaperones in SARS-CoV-2 Spike maturation and viral infectivity","volume":"8","author":"Yang","year":"2022","journal-title":"Sci. Adv."},{"key":"2026092901415082500_B23","doi-asserted-by":"crossref","DOI":"10.1101\/2020.06.26.173765","volume-title":"Glycans on the SARS-CoV-2 Spike Control the Receptor Binding Domain Conformation","author":"Henderson","year":"2020"},{"key":"2026092901415082500_B24","doi-asserted-by":"publisher","first-page":"963","DOI":"10.1038\/s41557-021-00758-3","article-title":"A glycan gate controls opening of the SARS-CoV-2 spike protein","volume":"13","author":"Sztain","year":"2021","journal-title":"Nat. Chem."},{"key":"2026092901415082500_B25","doi-asserted-by":"publisher","first-page":"1170","DOI":"10.1038\/s42003-022-04138-6","article-title":"SARS-CoV-2 spike opening dynamics and energetics reveal the individual roles of glycans and their collective impact","volume":"5","author":"Pang","year":"2022","journal-title":"Commun. Biol."},{"key":"2026092901415082500_B26","doi-asserted-by":"publisher","first-page":"1722","DOI":"10.1021\/acscentsci.0c01056","article-title":"Beyond shielding: the roles of glycans in the SARS-CoV-2 spike protein","volume":"6","author":"Casalino","year":"2020","journal-title":"ACS Cent. Sci."},{"key":"2026092901415082500_B27","doi-asserted-by":"publisher","first-page":"14991","DOI":"10.1038\/s41598-020-71748-7","article-title":"Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition","volume":"10","author":"Grant","year":"2020","journal-title":"Sci. Rep."},{"key":"2026092901415082500_B28","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1371\/journal.pcbi.1008790","article-title":"Computational epitope map of SARS-CoV-2 spike protein","volume":"17","author":"Sikora","year":"2021","journal-title":"PLoS Comput. Biol."},{"key":"2026092901415082500_B29","doi-asserted-by":"publisher","first-page":"651","DOI":"10.1038\/s41557-021-00707-0","article-title":"SARS-CoV-2 simulations go exascale to predict dramatic spike opening and cryptic pockets across the proteome","volume":"13","author":"Zimmerman","year":"2021","journal-title":"Nat. Chem."},{"key":"2026092901415082500_B30","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1038\/s41586-020-2180-5","article-title":"Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor","volume":"581","author":"Lan","year":"2020","journal-title":"Nature"},{"key":"2026092901415082500_B31","doi-asserted-by":"publisher","first-page":"1024.e21","DOI":"10.1016\/j.cell.2020.09.037","article-title":"Mapping neutralizing and immunodominant sites on the SARS-CoV-2 spike receptor-binding domain by structure-guided high-resolution serology","volume":"183","author":"Piccoli","year":"2020","journal-title":"Cell"},{"key":"2026092901415082500_B32","doi-asserted-by":"publisher","first-page":"eabi9915","DOI":"10.1126\/scitranslmed.abi9915","article-title":"Antibodies elicited by mRNA-1273 vaccination bind more broadly to the receptor binding domain than do those from SARS-CoV-2 infection","volume":"13","author":"Greaney","year":"2021","journal-title":"Sci. Transl. Med."},{"key":"2026092901415082500_B33","doi-asserted-by":"publisher","first-page":"2183","DOI":"10.1016\/j.cell.2021.02.032","article-title":"The antigenic anatomy of SARS-CoV-2 receptor binding domain","volume":"184","author":"Dejnirattisai","year":"2021","journal-title":"Cell"},{"key":"2026092901415082500_B34","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1016\/j.chom.2021.02.003","article-title":"Comprehensive mapping of mutations in the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human plasma antibodies","volume":"29","author":"Greaney","year":"2021","journal-title":"Cell Host Microbe"},{"key":"2026092901415082500_B35","doi-asserted-by":"publisher","first-page":"2020.08.21.261727","DOI":"10.1101\/2020.08.21.261727","article-title":"The receptor binding domain of SARS-CoV-2 spike is the key target of neutralizing antibody in human polyclonal sera","author":"Steffen","year":"2020","journal-title":"bioRxiv"},{"key":"2026092901415082500_B36","doi-asserted-by":"publisher","first-page":"100040","DOI":"10.1016\/j.xcrm.2020.100040","article-title":"Rapid generation of neutralizing antibody responses in COVID-19 patients","volume":"1","author":"Suthar","year":"2020","journal-title":"Cell Rep. Med."},{"key":"2026092901415082500_B37","doi-asserted-by":"publisher","first-page":"11727","DOI":"10.1073\/pnas.2003138117","article-title":"Cell entry mechanisms of SARS-CoV-2","volume":"117","author":"Shang","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026092901415082500_B38","doi-asserted-by":"publisher","first-page":"925","DOI":"10.1038\/s41594-020-0479-4","article-title":"Controlling the SARS-CoV-2 spike glycoprotein conformation","volume":"27","author":"Henderson","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026092901415082500_B39","doi-asserted-by":"publisher","first-page":"926","DOI":"10.1038\/s41565-025-01908-1","article-title":"Modulation of SARS-CoV-2 spike binding to ACE2 through conformational selection","volume":"20","author":"Saha","year":"2025","journal-title":"Nat. Nanotechnol."},{"key":"2026092901415082500_B40","doi-asserted-by":"publisher","first-page":"942","DOI":"10.1038\/s41594-020-0483-8","article-title":"Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation","volume":"27","author":"McCallum","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026092901415082500_B41","doi-asserted-by":"publisher","first-page":"934","DOI":"10.1038\/s41594-020-0478-5","article-title":"A thermostable, closed SARS-CoV-2 spike protein trimer","volume":"27","author":"Xiong","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026092901415082500_B42","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1038\/nature12711","article-title":"Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor","volume":"503","author":"Ge","year":"2013","journal-title":"Nature"},{"key":"2026092901415082500_B43","doi-asserted-by":"publisher","first-page":"3253","DOI":"10.1128\/JVI.02582-15","article-title":"Isolation and characterization of a novel bat coronavirus closely related to the direct progenitor of severe acute respiratory syndrome coronavirus","volume":"90","author":"Yang","year":"2016","journal-title":"J. Virol."},{"key":"2026092901415082500_B44","doi-asserted-by":"publisher","first-page":"e1006698","DOI":"10.1371\/journal.ppat.1006698","article-title":"Discovery of a rich gene pool of bat SARS-related coronaviruses provides new insights into the origin of SARS coronavirus","volume":"13","author":"Hu","year":"2017","journal-title":"PLoS Pathog."},{"key":"2026092901415082500_B45","doi-asserted-by":"publisher","first-page":"4380.e14","DOI":"10.1016\/j.cell.2021.06.008","article-title":"Identification of novel bat coronaviruses sheds light on the evolutionary origins of SARS-CoV-2 and related viruses","volume":"184","author":"Zhou","year":"2021","journal-title":"Cell"},{"key":"2026092901415082500_B46","doi-asserted-by":"publisher","first-page":"450","DOI":"10.1038\/nature02145","article-title":"Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus","volume":"426","author":"Li","year":"2003","journal-title":"Nature"},{"key":"2026092901415082500_B47","doi-asserted-by":"publisher","first-page":"e1010828","DOI":"10.1371\/journal.ppat.1010828","article-title":"An ACE2-dependent Sarbecovirus in Russian bats is resistant to SARS-CoV-2 vaccines","volume":"18","author":"Seifert","year":"2022","journal-title":"PLoS Pathog."},{"key":"2026092901415082500_B48","doi-asserted-by":"publisher","first-page":"8869","DOI":"10.1038\/s41467-024-53029-3","article-title":"Sarbecovirus RBD indels and specific residues dictating multi-species ACE2 adaptiveness","volume":"15","author":"Si","year":"2024","journal-title":"Nat. Commun."},{"key":"2026092901415082500_B49","doi-asserted-by":"publisher","first-page":"eadr8772","DOI":"10.1126\/sciadv.adr8772","article-title":"SARS-related coronavirus S-protein structures reveal synergistic RBM interactions underpinning high-affinity human ACE2 binding","volume":"11","author":"Wang","year":"2025","journal-title":"Sci. Adv."},{"key":"2026092901415082500_B50","doi-asserted-by":"publisher","first-page":"457","DOI":"10.1128\/MMBR.00004-08","article-title":"Cross-Species Virus Transmission and the Emergence of New Epidemic Diseases","volume":"72","author":"Parrish","year":"2008","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"2026092901415082500_B51","doi-asserted-by":"publisher","first-page":"6103","DOI":"10.1038\/s41467-021-26401-w","article-title":"Molecular insights into receptor binding of recent emerging SARS-CoV-2 variants","volume":"12","author":"Han","year":"2021","journal-title":"Nat. Commun."},{"key":"2026092901415082500_B52","doi-asserted-by":"publisher","first-page":"e70002","DOI":"10.7554\/eLife.70002","article-title":"The alpha\/B.1.1.7 SARS-CoV-2 variant exhibits significantly higher affinity for ACE-2 and requires lower inoculation doses to cause disease in K18-hACE2 mice","volume":"10","author":"Bayarri-Olmos","year":"2021","journal-title":"eLife"},{"key":"2026092901415082500_B53","doi-asserted-by":"publisher","first-page":"167058","DOI":"10.1016\/j.jmb.2021.167058","article-title":"Experimental evidence for enhanced receptor binding by rapidly spreading SARS-CoV-2 variants","volume":"433","author":"Laffeber","year":"2021","journal-title":"J. Mol. Biol."},{"key":"2026092901415082500_B54","doi-asserted-by":"publisher","first-page":"1621","DOI":"10.1126\/science.abl8506","article-title":"Molecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants","volume":"374","author":"McCallum","year":"2021","journal-title":"Science"},{"key":"2026092901415082500_B55","doi-asserted-by":"publisher","first-page":"630.e10","DOI":"10.1016\/j.cell.2022.01.001","article-title":"Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2","volume":"185","author":"Han","year":"2022","journal-title":"Cell"},{"key":"2026092901415082500_B56","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1038\/s41421-022-00431-0","article-title":"Broader-species receptor binding and structural bases of Omicron SARS-CoV-2 to both mouse and palm-civet ACE2s","volume":"8","author":"Li","year":"2022","journal-title":"Cell Discov."},{"key":"2026092901415082500_B57","doi-asserted-by":"publisher","first-page":"2952.e10","DOI":"10.1016\/j.cell.2022.06.023","article-title":"Structural basis of human ACE2 higher binding affinity to currently circulating Omicron SARS-CoV-2 sub-variants BA.2 and BA.1.1","volume":"185","author":"Li","year":"2022","journal-title":"Cell"},{"key":"2026092901415082500_B58","doi-asserted-by":"publisher","first-page":"5135","DOI":"10.1038\/s41467-021-25479-6","article-title":"Neutralization of SARS-CoV-2 variants by convalescent and BNT162b2 vaccinated serum","volume":"12","author":"Bates","year":"2021","journal-title":"Nat. Commun."},{"key":"2026092901415082500_B59","doi-asserted-by":"publisher","first-page":"2384.e12","DOI":"10.1016\/j.cell.2021.03.036","article-title":"SARS-CoV-2 variants B.1.351 and P.1 escape from neutralizing antibodies","volume":"184","author":"Hoffmann","year":"2021","journal-title":"Cell"},{"key":"2026092901415082500_B60","doi-asserted-by":"publisher","first-page":"917","DOI":"10.1038\/s41591-021-01318-5","article-title":"Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies","volume":"27","author":"Planas","year":"2021","journal-title":"Nat. Med."},{"key":"2026092901415082500_B61","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1038\/s41586-021-03398-2","article-title":"Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7","volume":"593","author":"Wang","year":"2021","journal-title":"Nature"},{"key":"2026092901415082500_B62","doi-asserted-by":"publisher","first-page":"2820","DOI":"10.1021\/acs.jmedchem.1c00311","article-title":"Insights into SARS-CoV-2\u2019s mutations for evading human antibodies: sacrifice and survival","volume":"65","author":"Luan","year":"2022","journal-title":"J. Med. Chem."},{"key":"2026092901415082500_B63","doi-asserted-by":"publisher","first-page":"467","DOI":"10.1016\/j.jinf.2021.07.019","article-title":"Cross-neutralization of SARS-CoV-2 B.1.1.7 and P.1 variants in vaccinated, convalescent and P.1 infected","volume":"83","author":"Gidari","year":"2021","journal-title":"J. Infect."},{"key":"2026092901415082500_B64","doi-asserted-by":"publisher","first-page":"e283","DOI":"10.1016\/S2666-5247(21)00068-9","article-title":"SARS-CoV-2 spike E484K mutation reduces antibody neutralisation","volume":"2","author":"Jangra","year":"2021","journal-title":"Lancet Microbe"},{"key":"2026092901415082500_B65","doi-asserted-by":"publisher","first-page":"276","DOI":"10.1038\/s41586-021-03777-9","article-title":"Reduced sensitivity of SARS-CoV-2 variant Delta to antibody neutralization","volume":"596","author":"Planas","year":"2021","journal-title":"Nature"},{"key":"2026092901415082500_B66","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1038\/s41586-021-03944-y","article-title":"SARS-CoV-2 B.1.617.2 Delta variant replication and immune evasion","volume":"599","author":"Mlcochova","year":"2021","journal-title":"Nature"},{"key":"2026092901415082500_B67","doi-asserted-by":"publisher","first-page":"167622","DOI":"10.1016\/j.jmb.2022.167622","article-title":"Biophysical fitness landscape of the SARS-CoV-2 Delta variant receptor binding domain","volume":"434","author":"Patrick","year":"2022","journal-title":"J. Mol. Biol."},{"key":"2026092901415082500_B68","doi-asserted-by":"publisher","first-page":"1693","DOI":"10.3390\/v13091693","article-title":"Antibody-mediated neutralization of authentic SARS-CoV-2 B.1.617 variants harboring L452R and T478K\/E484Q","volume":"13","author":"Wilhelm","year":"2021","journal-title":"Viruses"},{"key":"2026092901415082500_B69","doi-asserted-by":"publisher","first-page":"2557","DOI":"10.1038\/s41423-021-00772-y","article-title":"Delta variant (B.1.617.2) sublineages do not show increased neutralization resistance","volume":"18","author":"Arora","year":"2021","journal-title":"Cell. Mol. Immunol."},{"key":"2026092901415082500_B70","doi-asserted-by":"publisher","first-page":"671","DOI":"10.1038\/s41586-021-04389-z","article-title":"Considerable escape of SARS-CoV-2 Omicron to antibody neutralization","volume":"602","author":"Planas","year":"2022","journal-title":"Nature"},{"key":"2026092901415082500_B71","doi-asserted-by":"publisher","first-page":"676","DOI":"10.1038\/s41586-021-04388-0","article-title":"Striking antibody evasion manifested by the Omicron variant of SARS-CoV-2","volume":"602","author":"Liu","year":"2022","journal-title":"Nature"},{"key":"2026092901415082500_B72","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1038\/s41586-021-04385-3","article-title":"Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies","volume":"602","author":"Cao","year":"2022","journal-title":"Nature"},{"key":"2026092901415082500_B73","doi-asserted-by":"publisher","first-page":"1093.e3","DOI":"10.1016\/j.chom.2022.04.014","article-title":"Neutralization of SARS-CoV-2 Omicron sub-lineages BA.1, BA.1.1, and BA.2","volume":"30","author":"Evans","year":"2022","journal-title":"Cell Host Microbe"},{"key":"2026092901415082500_B74","doi-asserted-by":"publisher","first-page":"eabn8543","DOI":"10.1126\/scitranslmed.abn8543","article-title":"SARS-CoV-2 BA.1 variant is neutralized by vaccine booster-elicited serum but evades most convalescent serum and therapeutic antibodies","volume":"14","author":"Lusvarghi","year":"2022","journal-title":"Sci. Transl. Med."},{"key":"2026092901415082500_B75","doi-asserted-by":"publisher","first-page":"e2200592119","DOI":"10.1073\/pnas.2200592119","article-title":"Omicron mutations enhance infectivity and reduce antibody neutralization of SARS-CoV-2 virus-like particles","volume":"119","author":"Syed","year":"2022","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026092901415082500_B76","doi-asserted-by":"publisher","first-page":"1161","DOI":"10.1038\/s41564-022-01143-7","article-title":"SARS-CoV-2 Omicron is an immune escape variant with an altered cell entry pathway","volume":"7","author":"Willett","year":"2022","journal-title":"Nat. Microbiol."},{"key":"2026092901415082500_B77","doi-asserted-by":"publisher","first-page":"279.e8","DOI":"10.1016\/j.cell.2022.12.018","article-title":"Alarming antibody evasion properties of rising SARS-CoV-2 BQ and XBB subvariants","volume":"186","author":"Wang","year":"2023","journal-title":"Cell"},{"key":"2026092901415082500_B78","doi-asserted-by":"publisher","first-page":"112443","DOI":"10.1016\/j.celrep.2023.112443","article-title":"Enhanced evasion of neutralizing antibody response by Omicron XBB.1.5, CH.1.1, and CA.3.1 variants","volume":"42","author":"Qu","year":"2023","journal-title":"Cell Rep."},{"key":"2026092901415082500_B79","doi-asserted-by":"publisher","first-page":"781","DOI":"10.1016\/S1473-3099(23)00289-X","article-title":"Neutralising immunity to omicron sublineages BQ.1.1, XBB, and XBB.1.5 in healthy adults is boosted by bivalent BA.1-containing mRNA vaccination and previous Omicron infection","volume":"23","author":"Carr","year":"2023","journal-title":"Lancet Infect. Dis."},{"key":"2026092901415082500_B80","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1016\/S1473-3099(22)00816-7","article-title":"Humoral immune evasion of the omicron subvariants BQ.1.1 and XBB","volume":"23","author":"Uraki","year":"2023","journal-title":"Lancet Infect. Dis."},{"key":"2026092901415082500_B81","doi-asserted-by":"publisher","first-page":"2103.e19","DOI":"10.1016\/j.cell.2022.04.035","article-title":"Virological characteristics of the SARS-CoV-2 Omicron BA.2 spike","volume":"185","author":"Yamasoba","year":"2022","journal-title":"Cell"},{"key":"2026092901415082500_B82","doi-asserted-by":"publisher","first-page":"W216","DOI":"10.1093\/nar\/gkab225","article-title":"Expasy, the Swiss Bioinformatics Resource Portal, as designed by its users","volume":"49","author":"Duvaud","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"2026092901415082500_B83","doi-asserted-by":"publisher","first-page":"167357","DOI":"10.1016\/j.jmb.2021.167357","article-title":"Disulfide bonds play a critical role in the structure and function of the receptor-binding domain of the SARS-CoV-2 spike antigen","volume":"434","author":"Grishin","year":"2022","journal-title":"J. Mol. Biol."},{"key":"2026092901415082500_B84","doi-asserted-by":"publisher","first-page":"16292","DOI":"10.1021\/acsomega.0c02125","article-title":"Impact of thiol-disulfide balance on the binding of Covid-19 spike protein with angiotensin-converting enzyme 2 receptor","volume":"5","author":"Hati","year":"2020","journal-title":"ACS Omega"},{"key":"2026092901415082500_B85","doi-asserted-by":"publisher","first-page":"e21651","DOI":"10.1096\/fj.202100560R","article-title":"Disruption of disulfides within RBD of SARS-CoV-2 spike protein prevents fusion and represents a target for viral entry inhibition by registered drugs","volume":"35","author":"Man\u010dek-Keber","year":"2021","journal-title":"FASEB J."},{"key":"2026092901415082500_B86","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1016\/j.bbrc.2022.01.106","article-title":"The function of SARS-CoV-2 spike protein is impaired by disulfide-bond disruption with mutation at cysteine-488 and by thiol-reactive N-acetyl-cysteine and glutathione","volume":"597","author":"Murae","year":"2022","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2026092901415082500_B87","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1016\/S0168-1656(96)01636-7","article-title":"Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies","volume":"52","author":"Arora","year":"1996","journal-title":"J. Biotechnol."},{"key":"2026092901415082500_B88","doi-asserted-by":"publisher","first-page":"148","DOI":"10.1016\/S0006-291X(03)00578-3","article-title":"The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation","volume":"304","author":"Arakawa","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2026092901415082500_B89","doi-asserted-by":"publisher","first-page":"4919","DOI":"10.1021\/bi047528r","article-title":"Role of arginine in the stabilization of proteins against aggregation","volume":"44","author":"Baynes","year":"2005","journal-title":"Biochemistry"},{"key":"2026092901415082500_B90","doi-asserted-by":"publisher","first-page":"986","DOI":"10.1038\/cr.2013.92","article-title":"Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4","volume":"23","author":"Wang","year":"2013","journal-title":"Cell Res."},{"key":"2026092901415082500_B91","doi-asserted-by":"publisher","first-page":"1501","DOI":"10.1126\/science.abd0826","article-title":"Structure-based design of prefusion-stabilized SARS-CoV-2 spikes","volume":"369","author":"Hsieh","year":"2020","journal-title":"Science"},{"key":"2026092901415082500_B92","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1038\/s41586-020-2179-y","article-title":"Structural basis of receptor recognition by SARS-CoV-2","volume":"581","author":"Shang","year":"2020","journal-title":"Nature"},{"key":"2026092901415082500_B93","doi-asserted-by":"publisher","first-page":"1606","DOI":"10.1016\/S0006-3495(00)76713-0","article-title":"Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling","volume":"78","author":"Schuck","year":"2000","journal-title":"Biophys. J."},{"key":"2026092901415082500_B94","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1007\/s00249-023-01629-0","article-title":"SEDNTERP: a calculation and database utility to aid interpretation of analytical ultracentrifugation and light scattering data","volume":"52","author":"Philo","year":"2023","journal-title":"Eur. Biophys. J."},{"key":"2026092901415082500_B95","doi-asserted-by":"publisher","first-page":"E3095","DOI":"10.1073\/pnas.1500851112","article-title":"Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy","volume":"112","author":"Micsonai","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026092901415082500_B96","doi-asserted-by":"publisher","first-page":"W315","DOI":"10.1093\/nar\/gky497","article-title":"BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra","volume":"46","author":"Micsonai","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"2026092901415082500_B97","doi-asserted-by":"publisher","first-page":"2947","DOI":"10.1093\/bioinformatics\/btm404","article-title":"Clustal W and Clustal X version 2.0","volume":"23","author":"Larkin","year":"2007","journal-title":"Bioinformatics"},{"key":"2026092901415082500_B98","doi-asserted-by":"publisher","first-page":"1189","DOI":"10.1093\/bioinformatics\/btp033","article-title":"Jalview Version 2\u2014a multiple sequence alignment editor and analysis workbench","volume":"25","author":"Waterhouse","year":"2009","journal-title":"Bioinformatics"}],"container-title":["Bioscience Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/bioscirep\/article-pdf\/doi\/10.1042\/BSR20260440\/992014\/bsr-2026-0440-t.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/bioscirep\/article-pdf\/doi\/10.1042\/BSR20260440\/992014\/bsr-2026-0440-t.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T05:42:00Z","timestamp":1790660520000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/bioscirep\/article\/46\/10\/BSR20260440\/238062\/Disulfide-bonds-stabilize-the-SARS-CoV-2-RBD-and"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,29]]},"references-count":98,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2026,10,21]]}},"URL":"https:\/\/doi.org\/10.1042\/bsr20260440","relation":{},"ISSN":["0144-8463","1573-4935"],"issn-type":[{"value":"0144-8463","type":"print"},{"value":"1573-4935","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2026,10]]},"published":{"date-parts":[[2026,9,29]]},"article-number":"BSR20260440"}}