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Article: Peptide mimics of a conserved H5N1 avian influenza virus neutralization site
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TitlePeptide mimics of a conserved H5N1 avian influenza virus neutralization site
 
AuthorsLuo, W1
Chen, Y1
Wang, M1
Chen, Y1
Zheng, Z1
Song, H1
Chen, H2
Guan, Y2
Ng, MH1
Zhang, J1
Xia, N1
 
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
 
CitationBiochemical Journal, 2009, v. 419 n. 1, p. 133-139 [How to Cite?]
DOI: http://dx.doi.org/10.1042/BJ20080083
 
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.
 
ISSN0264-6021
2013 Impact Factor: 4.779
 
DOIhttp://dx.doi.org/10.1042/BJ20080083
 
ISI Accession Number IDWOS:000264642800014
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].

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorLuo, W
 
dc.contributor.authorChen, Y
 
dc.contributor.authorWang, M
 
dc.contributor.authorChen, Y
 
dc.contributor.authorZheng, Z
 
dc.contributor.authorSong, H
 
dc.contributor.authorChen, H
 
dc.contributor.authorGuan, Y
 
dc.contributor.authorNg, MH
 
dc.contributor.authorZhang, J
 
dc.contributor.authorXia, N
 
dc.date.accessioned2010-05-31T03:49:26Z
 
dc.date.available2010-05-31T03:49:26Z
 
dc.date.issued2009
 
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.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationBiochemical Journal, 2009, v. 419 n. 1, p. 133-139 [How to Cite?]
DOI: http://dx.doi.org/10.1042/BJ20080083
 
dc.identifier.doihttp://dx.doi.org/10.1042/BJ20080083
 
dc.identifier.epage139
 
dc.identifier.hkuros163958
 
dc.identifier.isiWOS:000264642800014
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].

 
dc.identifier.issn0264-6021
2013 Impact Factor: 4.779
 
dc.identifier.issue1
 
dc.identifier.pmid18973474
 
dc.identifier.scopuseid_2-s2.0-62749159748
 
dc.identifier.spage133
 
dc.identifier.urihttp://hdl.handle.net/10722/59405
 
dc.identifier.volume419
 
dc.languageeng
 
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofBiochemical Journal
 
dc.relation.referencesReferences in Scopus
 
dc.subjectAnti-H5 monoclonal antibody
 
dc.subjectH5N1 avian influenza virus
 
dc.subjectHaemagglutination
 
dc.subjectHepatitis virus
 
dc.subjectInfluenza
 
dc.subjectPeptide mimic
 
dc.titlePeptide mimics of a conserved H5N1 avian influenza virus neutralization site
 
dc.typeArticle
 
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<contributor.author>Guan, Y</contributor.author>
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<contributor.author>Xia, N</contributor.author>
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Author Affiliations
  1. Xiamen University
  2. The University of Hong Kong