A COVID-19 antibody curbs SARS-CoV-2 nucleocapsid protein-induced complement hyperactivation

A COVID-19 antibody curbs SARS-CoV-2 nucleocapsid protein-induced complement hyperactivation | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Article A COVID-19 antibody curbs SARS-CoV-2 nucleocapsid protein-induced complement hyperactivation Sisi Kang, Mei Yang, Suhua He, Yueming Wang, Xiaoxue Chen, Yao-Qing chen, and 14 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-106760/v1 This work is licensed under a CC BY 4.0 License Status: Published Journal Publication published 11 May, 2021 Read the published version in Nature Communications → Version 1 posted You are reading this latest preprint version Abstract Although human antibodies elicited by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nucleocapsid (N) protein are profoundly boosted upon infection, little is known about the function of N-reactive antibodies. Herein, we isolated and profiled a panel of 32 N protein-specific monoclonal antibodies (mAbs) from a quick recovery coronavirus disease-19 (COVID-19) convalescent patient who had dominant antibody responses to the SARS-CoV-2 N protein rather than to the SARS-CoV-2 spike (S) protein. The complex structure of the N protein RNA binding domain with the mAb with the highest binding affinity (nCoV396) revealed changes in the epitopes and antigen’s allosteric regulation. Functionally, a virus-free complement hyper-activation analysis demonstrated that nCoV396 specifically compromises the N protein-induced complement hyper-activation, which is a risk factor for the morbidity and mortality of COVID-19 patients, thus laying the foundation for the identification of functional anti-N protein mAbs. Immunology Structural Biology human monoclonal antibody COVID-19 SARS-CoV-2 nucleocapsid protein crystal structure complement hyperactivation viral protein targeting therapy MASP-2 Figures Figure 1 Figure 2 Figure 3 Figure 4 Full Text Due to technical limitations, full-text HTML conversion of this manuscript could not be completed. However, the latest manuscript can be downloaded and accessed as a PDF. Additional Declarations There is NO Competing Interest. Supplementary Files 5ExTFigTablesNC.pdf 4PDBNC.pdf PDB ID: 7CR5 Cite Share Download PDF Status: Published Journal Publication published 11 May, 2021 Read the published version in Nature Communications → Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-106760","acceptedTermsAndConditions":true,"allowDirectSubmit":false,"archivedVersions":[],"articleType":"Article","associatedPublications":[],"authors":[{"id":5476574,"identity":"053cfcb1-ca56-4240-8ee2-f68c4146bc05","order_by":0,"name":"Sisi Kang","email":"","orcid":"","institution":"Sun Yat-sen University","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Sisi","middleName":"","lastName":"Kang","suffix":""},{"id":5476575,"identity":"bd14f307-5026-4273-8691-cd3e91b1306b","order_by":1,"name":"Mei Yang","email":"","orcid":"","institution":"The Fifth Affiliated Hospital of Sun Yat-sen University","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Mei","middleName":"","lastName":"Yang","suffix":""},{"id":5476576,"identity":"3118775a-e5e4-4ace-8512-7fd5ef7b5015","order_by":2,"name":"Suhua He","email":"","orcid":"","institution":"The Fifth Affiliated Hospital of Sun Yat-sen University","correspondingAuthor":false,"submittingAuthor":false,"prefix":"","firstName":"Suhua","middleName":"","lastName":"He","suffix":""},{"id":5476577,"identity":"8968e8c7-35f6-4216-a085-9645b2c60306","order_by":3,"name":"Yueming Wang","email":"","orcid":"","institution":"Jinan University; 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Serum antibody titers of six SARS-CoV-2\nconvalescent patients to the SARS-CoV-2 S (a) and N (b) proteins measured by ELISA. Sorting of\nsingle plasma cells (c) with CD38 and CD27 double-positive B cells and single N and S proteinspecific\nmemory B cells (d) by FACS. (e) Percentage of different isotypes, VH and VL gene families of\n32 isolated N-reactive antibodies. (f) Number of mutations in nucleotides and amino acids in VH and\nVL (Vκ and Vλ) of 32 N-reactive antibodies and eight S-reactive antibodies (g). Length of the 32 Nreactive\nantibodies (h) and eight S-reactive antibodies (i) in H-CDR3.","description":"","filename":"1.png","url":"https://assets-eu.researchsquare.com/files/rs-106760/v1/8f489f53aac32dd6e5ada27e.png"},{"id":3966682,"identity":"b9dc3475-94ae-4395-b5f7-bc5424054ac0","added_by":"auto","created_at":"2020-12-02 20:14:41","extension":"png","order_by":2,"title":"Figure 2","display":"","copyAsset":false,"role":"figure","size":118066,"visible":true,"origin":"","legend":"Reactivity and affinity of the isolated antibodies to the N protein antigens. (a) Schematic presentation of the SARS-CoV-2 N protein and two variants. (b) Antibodies expressed in transfected 293 cells were evaluated for binding to N-FL, N-NTD and N-CTD by ELISA. Plasma from patient ZD006 and an irrelevant mAb TRN006 were used as the positive control and negative control, respectively. (c) The ability of nine purified antibodies to the N-FL protein was determined by ELISA. (d) Binding affinity of nine selected antibodies to the N protein was measured by SPR. KD values are shown above the individual plots.","description":"","filename":"2.png","url":"https://assets-eu.researchsquare.com/files/rs-106760/v1/dece694dc4210172a0d438cf.png"},{"id":3966683,"identity":"6bec18ab-69d6-49ae-99db-dce3260aede1","added_by":"auto","created_at":"2020-12-02 20:14:41","extension":"png","order_by":3,"title":"Figure 3","display":"","copyAsset":false,"role":"figure","size":523374,"visible":true,"origin":"","legend":"Complex structure of mAb nCoV396 with SARS-CoV-2 N-NTD(a) Overall structure of the mAb SARS-CoV-2 N-NTD complex. The light chain (pink) and heavy chain (blue) of mAb nCoV396 are illustrated with the ribbon representation. SARS-CoV-2 N-NTD is illustrated with an electrostatic surface, in which blue denotes a positive charge potential, while red indicates a negative charge potential. (b) The N-N􀀂D epitope recognized by mAb nCoV396. The interacting residues of N-NTD and nCoV396 are highlighted with the stict representation. Recognition of Q163 (c),K169 (d) and L167 (e) in N-NTD by mAb nCoV396. The dashed blue line represents hydrogen bonds. Hydrophobic interactions are illustrated with the dot representation. (f) Conformational changes in N-NTD upon mAb nCoV396 binding. The apo structure of N-NTD is colored gray. Antibody-bound N-N􀀂D is colored green. The N-terminus and C-terminus of the N-NTD are labeled with circles. mAb nCoV396 is illustrated with surface representation. All figures were prepared by PyMol.","description":"","filename":"3.png","url":"https://assets-eu.researchsquare.com/files/rs-106760/v1/2b1652c45f74ab85f19d960d.png"},{"id":3966686,"identity":"277b5a18-3aa5-458a-b36c-67a290b46f35","added_by":"auto","created_at":"2020-12-02 20:14:42","extension":"png","order_by":4,"title":"Figure 4","display":"","copyAsset":false,"role":"figure","size":215815,"visible":true,"origin":"","legend":"Antibody nCoV396 compromises SARS-CoV-2 N protein-induced complement hyperactivation. (a) Flow scheme of the SARS-CoV-2 N protein and nCoV396 influencing the protease activity of MASP-2 in the serum of autoimmune disease patients. The Michaelis-Menten curve shows the effect of increasing the N protein concentration (b) and antibody concentration (d) on the substrate C2 cleavage of MAPS-2 in the serum of patient 49 and patient 20. (c) A Hanes plot where C2 concentrationN0 is plotted against C2 concentration with the addition of 5 µM N protein. (e) The mAb nCoV396 inhibits the N protein-induced excessive cleavage of C2 in the serum of six autoimmune disease patients, and the last panel shows a summary of Vmax for all patients. Negative control (Negative Ctrl) and blank control (Blank Ctrl) represent reactions containing bovine serum albumin (BSA) instead of N or N+mAb and without exogenous protein, respectively. The mean and standard deviation (SD) values of three technical replicates are shown. P values: *P \u003c 0.05; **P \u003c 0.01; \"-\" indicates that the experimental kinetics did not conform to Michaelis-Menten kinetics. ","description":"","filename":"4.png","url":"https://assets-eu.researchsquare.com/files/rs-106760/v1/a964eff04f8f517ed949f44f.png"},{"id":15782670,"identity":"e95e0c06-3a04-49c3-a075-cd1a744c1e36","added_by":"auto","created_at":"2021-11-22 15:48:24","extension":"pdf","order_by":3,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":723272,"visible":true,"origin":"","legend":"Article file","description":"","filename":"NCOMMS2045166manuscriptupdate.pdf","url":"https://assets-eu.researchsquare.com/files/rs-106760/v1_covered.pdf"},{"id":13561282,"identity":"fab0d8a0-30fd-49ea-a418-e221c1d9d017","added_by":"auto","created_at":"2021-09-17 03:08:08","extension":"pdf","order_by":3,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":718309,"visible":true,"origin":"","legend":"Article file","description":"","filename":"NCOMMS2045166manuscriptupdate.pdf","url":"https://assets-eu.researchsquare.com/files/rs-106760/v1_covered.pdf"},{"id":3966687,"identity":"a39d7a27-38e8-45c9-be8b-24c02e01e268","added_by":"auto","created_at":"2020-12-02 20:14:45","extension":"pdf","order_by":3,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":351222,"visible":true,"origin":"","legend":"Article file","description":"","filename":"NCOMMS2045166manuscriptupdate.pdf","url":"https://assets-eu.researchsquare.com/files/rs-106760/v1_stamped.pdf"},{"id":3966684,"identity":"0dc948f9-e927-46d3-91c6-5e7ab2a94787","added_by":"auto","created_at":"2020-12-02 20:14:42","extension":"pdf","order_by":1,"title":"","display":"","copyAsset":false,"role":"supplement","size":2877012,"visible":true,"origin":"","legend":"","description":"","filename":"5ExTFigTablesNC.pdf","url":"https://assets-eu.researchsquare.com/files/rs-106760/v1/c1ca15e4936dcd197a609825.pdf"},{"id":3966685,"identity":"3f2e4db7-e184-49c7-b4ea-240a973f9d54","added_by":"auto","created_at":"2020-12-02 20:14:42","extension":"pdf","order_by":2,"title":"","display":"","copyAsset":false,"role":"supplement","size":617411,"visible":true,"origin":"","legend":"PDB ID: 7CR5","description":"","filename":"4PDBNC.pdf","url":"https://assets-eu.researchsquare.com/files/rs-106760/v1/78f58ba9ab76851741479c70.pdf"}],"financialInterests":"There is \u003cb\u003eNO\u003c/b\u003e Competing Interest.","formattedTitle":"A COVID-19 antibody curbs SARS-CoV-2 nucleocapsid protein-induced complement hyperactivation","fulltext":[{"header":"Full Text","content":"Due to technical limitations, full-text HTML conversion of this manuscript could not be completed. However, the latest manuscript can be downloaded and \u003ca href='/article/rs-106760/latest.pdf' target='_blank'\u003e accessed as a PDF.\u003c/a\u003e"}],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":false,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":false,"hideJournal":false,"highlight":"","institution":"","isAcceptedByJournal":true,"isAuthorSuppliedPdf":true,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":false,"isPdfUpToDate":true,"isWithdrawnOrRetracted":false,"journal":{"display":true,"email":"[email protected]","identity":"nature-portfolio","isNatureJournal":true,"hasQc":false,"allowDirectSubmit":false,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"","title":"Nature Portfolio","twitterHandle":"","acdcEnabled":false,"dfaEnabled":false,"editorialSystem":"ejp","reportingPortfolio":"","inReviewEnabled":true,"inReviewRevisionsEnabled":false},"keywords":"human monoclonal antibody, COVID-19, SARS-CoV-2, nucleocapsid protein, crystal structure, complement hyperactivation, viral protein targeting therapy, MASP-2","lastPublishedDoi":"10.21203/rs.3.rs-106760/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-106760/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"Although human antibodies elicited by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nucleocapsid (N) protein are profoundly boosted upon infection, little is known about the function of N-reactive antibodies. Herein, we isolated and profiled a panel of 32 N protein-specific monoclonal antibodies (mAbs) from a quick recovery coronavirus disease-19 (COVID-19) convalescent patient who had dominant antibody responses to the SARS-CoV-2 N protein rather than to the SARS-CoV-2 spike (S) protein. The complex structure of the N protein RNA binding domain with the mAb with the highest binding affinity (nCoV396) revealed changes in the epitopes and antigen’s allosteric regulation. Functionally, a virus-free complement hyper-activation analysis demonstrated that nCoV396 specifically compromises the N protein-induced complement hyper-activation, which is a risk factor for the morbidity and mortality of COVID-19 patients, thus laying the foundation for the identification of functional anti-N protein mAbs.","manuscriptTitle":"A COVID-19 antibody curbs SARS-CoV-2 nucleocapsid protein-induced complement hyperactivation","msid":"","msnumber":"","nonDraftVersions":[{"code":1,"date":"2020-12-02 20:14:39","doi":"10.21203/rs.3.rs-106760/v1","editorialEvents":[],"status":"published","journal":{"display":true,"email":"[email protected]","identity":"nature-communications","isNatureJournal":true,"hasQc":false,"allowDirectSubmit":false,"externalIdentity":"NCOMMS","sideBox":"Learn more about [Nature Communications](http://www.nature.com/ncomms/)","snPcode":"","submissionUrl":"https://mts-ncomms.nature.com/","title":"Nature Communications","twitterHandle":"","acdcEnabled":true,"dfaEnabled":true,"editorialSystem":"ejp","reportingPortfolio":"Nature Communications","inReviewEnabled":true,"inReviewRevisionsEnabled":false}}],"origin":"","ownerIdentity":"81f6b868-8926-447b-aa27-6758bbfd79d2","owner":[],"postedDate":"December 2nd, 2020","published":true,"recentEditorialEvents":[],"rejectedJournal":[],"revision":"","amendment":"","status":"published-in-journal","subjectAreas":[{"id":1290475,"name":"Immunology"},{"id":1290476,"name":"Structural Biology"}],"tags":[],"updatedAt":"2021-11-22T15:43:09+00:00","versionOfRecord":{"articleIdentity":"rs-106760","link":"https://doi.org/10.1038/s41467-021-23036-9","journal":{"identity":"nature-communications","isVorOnly":false,"title":"Nature Communications"},"publishedOn":"2021-05-11 04:00:00","publishedOnDateReadable":"May 11th, 2021"},"versionCreatedAt":"2020-12-02 20:14:39","video":"","vorDoi":"10.1038/s41467-021-23036-9","vorDoiUrl":"https://doi.org/10.1038/s41467-021-23036-9","workflowStages":[]},"version":"v1","identity":"rs-106760","journalConfig":"researchsquare"},"__N_SSP":true},"page":"/article/[identity]/[[...version]]","query":{"redirect":"/article/rs-106760","identity":"rs-106760","version":["v1"]},"buildId":"7rjqhiLT3MXkJMwkYKINL","isFallback":false,"isExperimentalCompile":false,"dynamicIds":[84888],"gssp":true,"scriptLoader":[]}