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Article: Peptide mimics of a conserved H5N1 avian influenza virus neutralization site

TitlePeptide mimics of a conserved H5N1 avian influenza virus neutralization site
Authors
KeywordsAnti-H5 monoclonal antibody
H5N1 avian influenza virus
Haemagglutination
Hepatitis virus
Influenza
Peptide mimic
Issue Date2009
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 2009, v. 419 n. 1, p. 133-139 How to Cite?
AbstractA panel of 52 murine monoclonal antibodies was found to recognize antigenic determinants that had been conserved among all major genetic subgroups of the H5N1 avian influenza virus prevalent since 1997. We screened a phage display library for peptides recognized by one such antibody (8H5). We analysed the specificity of 8H5 for reactive peptides presented as fusion proteins of HBc (hepatitis B core protein) and HEV (hepatitis E virus) structural protein, p239. This was then related to the specificity of the native HA (haemagglutinin) molecule by virtue of the capacity of fusion proteins to compete for 8H5 binding with different strains of H5N1 virus and the reactivity of antisera generated against fusion proteins to bind native HA molecules, and to inhibit haemagglutination and arrest infection by the virus. Nine reactive peptides of different amino acid sequences were identified, six of which were also reactive with the antibody in association with HBc and four were in association with p239. Binding occurred with the dimeric form of the four p239-fusion proteins and one of the HBc-fusion proteins, but not with the monomeric form. The HBc-fusion proteins blocked 8H5 binding with four strains of H5N1 influenza virus. Mouse antisera generated against fusion proteins bound to HA molecules, but did not inhibit haemagglutination or arrest H5N1 infection. Our findings indicate that 8H5 recognizes discontinuous sites presented by secondary and possibly higher structural orders of the peptides in spatially favourable positions for binding with the antibody, and that the peptides partially mimic the native 8H5 epitopes on the H5N1 virus. © The Authors Journal compilation.
Persistent Identifierhttp://hdl.handle.net/10722/59405
ISSN
2014 Impact Factor: 4.396
2014 SCImago Journal Rankings: 2.424
ISI Accession Number ID
Funding AgencyGrant Number
Science and Technology Foundation of Fujian Province2008Y0059
F2006BA101B06
Key Project of Chinese Ministry of Education1081157
Foundation front Ministry of Science and Technology2005DC105006
Funding Information:

this work was supported by the Science and Technology Foundation of Fujian Province [grant numbers 2008Y0059 and F2006BA101B06], the Key Project of Chinese Ministry of Education [grant number 1081157] and the Foundation front Ministry of Science and Technology [grant number 2005DC105006].

References

 

DC FieldValueLanguage
dc.contributor.authorLuo, Wen_HK
dc.contributor.authorChen, Yen_HK
dc.contributor.authorWang, Men_HK
dc.contributor.authorChen, Yen_HK
dc.contributor.authorZheng, Zen_HK
dc.contributor.authorSong, Hen_HK
dc.contributor.authorChen, Hen_HK
dc.contributor.authorGuan, Yen_HK
dc.contributor.authorNg, MHen_HK
dc.contributor.authorZhang, Jen_HK
dc.contributor.authorXia, Nen_HK
dc.date.accessioned2010-05-31T03:49:26Z-
dc.date.available2010-05-31T03:49:26Z-
dc.date.issued2009en_HK
dc.identifier.citationBiochemical Journal, 2009, v. 419 n. 1, p. 133-139en_HK
dc.identifier.issn0264-6021en_HK
dc.identifier.urihttp://hdl.handle.net/10722/59405-
dc.description.abstractA panel of 52 murine monoclonal antibodies was found to recognize antigenic determinants that had been conserved among all major genetic subgroups of the H5N1 avian influenza virus prevalent since 1997. We screened a phage display library for peptides recognized by one such antibody (8H5). We analysed the specificity of 8H5 for reactive peptides presented as fusion proteins of HBc (hepatitis B core protein) and HEV (hepatitis E virus) structural protein, p239. This was then related to the specificity of the native HA (haemagglutinin) molecule by virtue of the capacity of fusion proteins to compete for 8H5 binding with different strains of H5N1 virus and the reactivity of antisera generated against fusion proteins to bind native HA molecules, and to inhibit haemagglutination and arrest infection by the virus. Nine reactive peptides of different amino acid sequences were identified, six of which were also reactive with the antibody in association with HBc and four were in association with p239. Binding occurred with the dimeric form of the four p239-fusion proteins and one of the HBc-fusion proteins, but not with the monomeric form. The HBc-fusion proteins blocked 8H5 binding with four strains of H5N1 influenza virus. Mouse antisera generated against fusion proteins bound to HA molecules, but did not inhibit haemagglutination or arrest H5N1 infection. Our findings indicate that 8H5 recognizes discontinuous sites presented by secondary and possibly higher structural orders of the peptides in spatially favourable positions for binding with the antibody, and that the peptides partially mimic the native 8H5 epitopes on the H5N1 virus. © The Authors Journal compilation.en_HK
dc.languageengen_HK
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.orgen_HK
dc.relation.ispartofBiochemical Journalen_HK
dc.subjectAnti-H5 monoclonal antibodyen_HK
dc.subjectH5N1 avian influenza virusen_HK
dc.subjectHaemagglutinationen_HK
dc.subjectHepatitis virusen_HK
dc.subjectInfluenzaen_HK
dc.subjectPeptide mimicen_HK
dc.titlePeptide mimics of a conserved H5N1 avian influenza virus neutralization siteen_HK
dc.typeArticleen_HK
dc.identifier.emailChen, H: hlchen@hku.hken_HK
dc.identifier.emailGuan, Y: yguan@hkucc.hku.hken_HK
dc.identifier.authorityChen, H=rp00383en_HK
dc.identifier.authorityGuan, Y=rp00397en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1042/BJ20080083en_HK
dc.identifier.pmid18973474-
dc.identifier.scopuseid_2-s2.0-62749159748en_HK
dc.identifier.hkuros163958en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-62749159748&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume419en_HK
dc.identifier.issue1en_HK
dc.identifier.spage133en_HK
dc.identifier.epage139en_HK
dc.identifier.isiWOS:000264642800014-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLuo, W=7202199022en_HK
dc.identifier.scopusauthoridChen, Y=8705548300en_HK
dc.identifier.scopusauthoridWang, M=16314645900en_HK
dc.identifier.scopusauthoridChen, Y=35572810100en_HK
dc.identifier.scopusauthoridZheng, Z=23972049100en_HK
dc.identifier.scopusauthoridSong, H=36148613900en_HK
dc.identifier.scopusauthoridChen, H=26643315400en_HK
dc.identifier.scopusauthoridGuan, Y=7202924055en_HK
dc.identifier.scopusauthoridNg, MH=7202076421en_HK
dc.identifier.scopusauthoridZhang, J=35202802400en_HK
dc.identifier.scopusauthoridXia, N=35187953700en_HK

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