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Article: Conserved amino acids W423 and N424 in receptor-binding domain of SARS-CoV are potential targets for therapeutic monoclonal antibody

TitleConserved amino acids W423 and N424 in receptor-binding domain of SARS-CoV are potential targets for therapeutic monoclonal antibody
Authors
Bian, CZhang, XCai, XZhang, LChen, ZZha, YXu, YXu, KLu, WYan, LYuan, JFeng, JHao, PWang, QZhao, GLiu, GZhu, XShen, HZheng, BShen, BSun, B
KeywordsChimeric
Epitope
Monoclonal antibody
Neutralization
Receptor-binding domain
SARS-CoV
Issue Date2009
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yviro
Citation
Virology, 2009, v. 383 n. 1, p. 39-46 How to Cite?
DOI: http://dx.doi.org/10.1016/j.virol.2008.09.029
AbstractThe receptor-binding domain (RBD) on spike protein of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the main region interacting with the viral receptor-ACE2 and is a useful target for induction of neutralizing antibodies against SARS-CoV infection. Here we generated two monoclonal antibodies (mAbs), targeting RBD, with marked virus neutralizing activity. The mAbs recognize a new conformational epitope which consists of several discontinuous peptides (aa. 343-367, 373-390 and 411-428) and is spatially located neighboring the receptor-binding motif (RPM) region of the RBD. Importantly, W423 and N424 residues are essential for mAb recognition and are highly conserved among 107 different strains of SARS, indicating that the residues are the most critical in the epitope which is a novel potential target for therapeutic mAbs. A human-mouse chimeric antibody, based upon the original murine mAb, was also constructed and shown to possess good neutralizing activity and high affinity. © 2008 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/59398
ISSN
0042-6822
2021 Impact Factor: 3.513
2020 SCImago Journal Rankings: 1.389
ISI Accession Number ID
WOS:000262447300006
Funding AgencyGrant Number
National Natural Science Foundation of China30325018
30530700
30623003
30421005
CAS projectKSCX1-YW-R-43
863 key project2006AA02A247
Technology Commission of Shanghai Municipality04DZ14902
04DZ19108
06DZ22032
04DZ19112
E-institutes of Shanghai Universities Immunology Division
Funding Information:

We thank Dr. Vincent Deubel and Dr. Sheri Skinner for reviewing the manuscript and for helpful comments. This work was supported by grants from the National Natural Science Foundation of China (30325018, 30530700, 30623003 and 30421005), the CAS project (KSCX1-YW-R-43), a grant from the 863 key project (2006AA02A247), grants from the Technology Commission of Shanghai Municipality (04DZ14902, 04DZ19108, 06DZ22032 and 04DZ19112), and a grant from the E-institutes of Shanghai Universities Immunology Division.

References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorBian, Cen_HK
dc.contributor.authorZhang, Xen_HK
dc.contributor.authorCai, Xen_HK
dc.contributor.authorZhang, Len_HK
dc.contributor.authorChen, Zen_HK
dc.contributor.authorZha, Yen_HK
dc.contributor.authorXu, Yen_HK
dc.contributor.authorXu, Ken_HK
dc.contributor.authorLu, Wen_HK
dc.contributor.authorYan, Len_HK
dc.contributor.authorYuan, Jen_HK
dc.contributor.authorFeng, Jen_HK
dc.contributor.authorHao, Pen_HK
dc.contributor.authorWang, Qen_HK
dc.contributor.authorZhao, Gen_HK
dc.contributor.authorLiu, Gen_HK
dc.contributor.authorZhu, Xen_HK
dc.contributor.authorShen, Hen_HK
dc.contributor.authorZheng, Ben_HK
dc.contributor.authorShen, Ben_HK
dc.contributor.authorSun, Ben_HK
dc.date.accessioned2010-05-31T03:49:17Z-
dc.date.available2010-05-31T03:49:17Z-
dc.date.issued2009en_HK
dc.identifier.citationVirology, 2009, v. 383 n. 1, p. 39-46en_HK
dc.identifier.issn0042-6822en_HK
dc.identifier.urihttp://hdl.handle.net/10722/59398-
dc.description.abstractThe receptor-binding domain (RBD) on spike protein of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the main region interacting with the viral receptor-ACE2 and is a useful target for induction of neutralizing antibodies against SARS-CoV infection. Here we generated two monoclonal antibodies (mAbs), targeting RBD, with marked virus neutralizing activity. The mAbs recognize a new conformational epitope which consists of several discontinuous peptides (aa. 343-367, 373-390 and 411-428) and is spatially located neighboring the receptor-binding motif (RPM) region of the RBD. Importantly, W423 and N424 residues are essential for mAb recognition and are highly conserved among 107 different strains of SARS, indicating that the residues are the most critical in the epitope which is a novel potential target for therapeutic mAbs. A human-mouse chimeric antibody, based upon the original murine mAb, was also constructed and shown to possess good neutralizing activity and high affinity. © 2008 Elsevier Inc. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yviroen_HK
dc.relation.ispartofVirologyen_HK
dc.subjectChimericen_HK
dc.subjectEpitopeen_HK
dc.subjectMonoclonal antibodyen_HK
dc.subjectNeutralizationen_HK
dc.subjectReceptor-binding domainen_HK
dc.subjectSARS-CoVen_HK
dc.subject.meshAntibodies, Monoclonal - immunology - isolation and purification - therapeutic use-
dc.subject.meshAntibodies, Viral - immunology - isolation and purification - therapeutic use-
dc.subject.meshMembrane Glycoproteins - antagonists and inhibitors - chemistry - immunology-
dc.subject.meshSARS Virus - immunology - physiology-
dc.subject.meshViral Envelope Proteins - antagonists and inhibitors - chemistry - immunology-
dc.titleConserved amino acids W423 and N424 in receptor-binding domain of SARS-CoV are potential targets for therapeutic monoclonal antibodyen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0042-6822&volume=383 &issue=1&spage=39&epage=46&date=2009&atitle=Conserved+amino+acids+W423+and+N424+in+receptor-binding+domain+of+SARS-CoV+are+potential+targets+for+therapeutic+monoclonal+antibodyen_HK
dc.identifier.emailChen, Z:zchenai@hkucc.hku.hken_HK
dc.identifier.emailZheng, B:bzheng@hkucc.hku.hken_HK
dc.identifier.authorityChen, Z=rp00243en_HK
dc.identifier.authorityZheng, B=rp00353en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.virol.2008.09.029en_HK
dc.identifier.pmid18986662-
dc.identifier.scopuseid_2-s2.0-57049087447en_HK
dc.identifier.hkuros165449en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-57049087447&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume383en_HK
dc.identifier.issue1en_HK
dc.identifier.spage39en_HK
dc.identifier.epage46en_HK
dc.identifier.isiWOS:000262447300006-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridBian, C=36522152700en_HK
dc.identifier.scopusauthoridZhang, X=9238679400en_HK
dc.identifier.scopusauthoridCai, X=25627476700en_HK
dc.identifier.scopusauthoridZhang, L=8783285300en_HK
dc.identifier.scopusauthoridChen, Z=35271180800en_HK
dc.identifier.scopusauthoridZha, Y=25629148500en_HK
dc.identifier.scopusauthoridXu, Y=55168932400en_HK
dc.identifier.scopusauthoridXu, K=7403282210en_HK
dc.identifier.scopusauthoridLu, W=36077781100en_HK
dc.identifier.scopusauthoridYan, L=8262196300en_HK
dc.identifier.scopusauthoridYuan, J=37020316900en_HK
dc.identifier.scopusauthoridFeng, J=7403883890en_HK
dc.identifier.scopusauthoridHao, P=7005522275en_HK
dc.identifier.scopusauthoridWang, Q=7408173913en_HK
dc.identifier.scopusauthoridZhao, G=7403296532en_HK
dc.identifier.scopusauthoridLiu, G=8833437700en_HK
dc.identifier.scopusauthoridZhu, X=8373708300en_HK
dc.identifier.scopusauthoridShen, H=7404520882en_HK
dc.identifier.scopusauthoridZheng, B=7201780588en_HK
dc.identifier.scopusauthoridShen, B=7401582245en_HK
dc.identifier.scopusauthoridSun, B=24734369900en_HK
dc.identifier.issnl0042-6822-

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