Advanced search
1 file | 786.23 KB Add to list

Insight into highly conserved H1 subtype-specific epitopes in influenza virus hemagglutinin

(2014) PLOS ONE. 9(2).
Author
Organization
Abstract
Influenza viruses continuously undergo antigenic changes with gradual accumulation of mutations in hemagglutinin (HA) that is a major determinant in subtype specificity. The identification of conserved epitopes within specific HA subtypes gives an important clue for developing new vaccines and diagnostics. We produced and characterized nine monoclonal antibodies that showed significant neutralizing activities against H1 subtype influenza viruses, and determined the complex structure of HA derived from a 2009 pandemic virus A/Korea/01/2009 (KR01) and the Fab fragment from H1-specific monoclonal antibody GC0587. The overall structure of the complex was essentially identical to the previously determined KR01 HA-Fab0757 complex structure. Both Fab0587 and Fab0757 recognize readily accessible head regions of HA, revealing broadly shared and conserved antigenic determinants among H1 subtypes. The beta-strands constituted by Ser110-Glu115 and Lys169-Lys170 form H1 epitopes with distinct conformations from those of H1 and H3 HA sites. In particular, Glu112, Glu115, Lys169, and Lys171 that are highly conserved among H1 subtype HAs have close contacts with HCDR3 and LCDR3. The differences between Fab0587 and Fab0757 complexes reside mainly in HCDR3 and LCDR3, providing distinct antigenic determinants specific for 1918 pdm influenza strain. Our results demonstrate a potential key neutralizing epitope important for H1 subtype specificity in influenza virus.
Keywords
PATHOGENICITY, MORTALITY, ANTIBODY, NEUTRALIZING EPITOPE, A VIRUSES, MEMBRANE-FUSION, RECEPTOR-BINDING

Downloads

  • 2293 14Cho.pdf
    • full text
    • |
    • open access
    • |
    • PDF
    • |
    • 786.23 KB

Citation

Please use this url to cite or link to this publication:

MLA
Cho, Ki Joon et al. “Insight into Highly Conserved H1 Subtype-specific Epitopes in Influenza Virus Hemagglutinin.” PLOS ONE 9.2 (2014): n. pag. Print.
APA
Cho, K. J., Hong, K. W., Kim, S.-H., Seok, J. H., Kim, S., Lee, J.-H., Saelens, X., et al. (2014). Insight into highly conserved H1 subtype-specific epitopes in influenza virus hemagglutinin. PLOS ONE, 9(2).
Chicago author-date
Cho, Ki Joon, Kwang W Hong, Se-Ho Kim, Jong Hyeon Seok, Sella Kim, Ji-Hye Lee, Xavier Saelens, and Kyung Hyun Kim. 2014. “Insight into Highly Conserved H1 Subtype-specific Epitopes in Influenza Virus Hemagglutinin.” Plos One 9 (2).
Chicago author-date (all authors)
Cho, Ki Joon, Kwang W Hong, Se-Ho Kim, Jong Hyeon Seok, Sella Kim, Ji-Hye Lee, Xavier Saelens, and Kyung Hyun Kim. 2014. “Insight into Highly Conserved H1 Subtype-specific Epitopes in Influenza Virus Hemagglutinin.” Plos One 9 (2).
Vancouver
1.
Cho KJ, Hong KW, Kim S-H, Seok JH, Kim S, Lee J-H, et al. Insight into highly conserved H1 subtype-specific epitopes in influenza virus hemagglutinin. PLOS ONE. 2014;9(2).
IEEE
[1]
K. J. Cho et al., “Insight into highly conserved H1 subtype-specific epitopes in influenza virus hemagglutinin,” PLOS ONE, vol. 9, no. 2, 2014.
@article{4362185,
  abstract     = {Influenza viruses continuously undergo antigenic changes with gradual accumulation of mutations in hemagglutinin (HA) that is a major determinant in subtype specificity. The identification of conserved epitopes within specific HA subtypes gives an important clue for developing new vaccines and diagnostics. We produced and characterized nine monoclonal antibodies that showed significant neutralizing activities against H1 subtype influenza viruses, and determined the complex structure of HA derived from a 2009 pandemic virus A/Korea/01/2009 (KR01) and the Fab fragment from H1-specific monoclonal antibody GC0587. The overall structure of the complex was essentially identical to the previously determined KR01 HA-Fab0757 complex structure. Both Fab0587 and Fab0757 recognize readily accessible head regions of HA, revealing broadly shared and conserved antigenic determinants among H1 subtypes. The beta-strands constituted by Ser110-Glu115 and Lys169-Lys170 form H1 epitopes with distinct conformations from those of H1 and H3 HA sites. In particular, Glu112, Glu115, Lys169, and Lys171 that are highly conserved among H1 subtype HAs have close contacts with HCDR3 and LCDR3. The differences between Fab0587 and Fab0757 complexes reside mainly in HCDR3 and LCDR3, providing distinct antigenic determinants specific for 1918 pdm influenza strain. Our results demonstrate a potential key neutralizing epitope important for H1 subtype specificity in influenza virus.},
  articleno    = {e89803},
  author       = {Cho, Ki Joon and Hong, Kwang W and Kim, Se-Ho and Seok, Jong Hyeon and Kim, Sella and Lee, Ji-Hye and Saelens, Xavier and Kim, Kyung Hyun},
  issn         = {1932-6203},
  journal      = {PLOS ONE},
  keywords     = {PATHOGENICITY,MORTALITY,ANTIBODY,NEUTRALIZING EPITOPE,A VIRUSES,MEMBRANE-FUSION,RECEPTOR-BINDING},
  language     = {eng},
  number       = {2},
  pages        = {9},
  title        = {Insight into highly conserved H1 subtype-specific epitopes in influenza virus hemagglutinin},
  url          = {http://dx.doi.org/10.1371/journal.pone.0089803},
  volume       = {9},
  year         = {2014},
}

Altmetric
View in Altmetric
Web of Science
Times cited: