S156 mutation lies at the antigenic subsite of site 2 that corresponds to site B in the H3 subtype. In some strains of non-human origins, there are mutations at the antigenic sites. Interestingly, in AAY56367 strain mutation L138-->H138 lies at the receptor binding site, which also overlaps the antigenic site. Therefore, this amino acid substitution may influence both the specificity of receptor recognition and antibody binding. Seven potential glycosylation sites in human HA and in some strains of non-human sources have been predicted by computer program, Scan Prosite. In some strains of HA from non-human sources because of mutation, an additional glycosylation site appeared at the antigenic site. Therefore in these strains the oligosaccharides will mask the surface of HA as well as antigenic site. Hence these strains will not be recognized by host immune system." />
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Salahuddin P, Khan AU. Identification of mutations at the antigenic and glycosylation sites in hemagglutinin protein of H5N1 strain. Bioinformation. 2009;4(1):30-5doi: 10.6026/97320630004030.
Salahuddin, P., & Khan, A. U. (2009). Identification of mutations at the antigenic and glycosylation sites in hemagglutinin protein of H5N1 strain. Bioinformation, 4(1), 30-5. https://doi.org/10.6026/97320630004030
Salahuddin, Parveen, and Khan, Asad U. "Identification of mutations at the antigenic and glycosylation sites in hemagglutinin protein of H5N1 strain." Bioinformation vol. 4,1 (2009): 30-5. doi: https://doi.org/10.6026/97320630004030
Salahuddin P, Khan AU. Identification of mutations at the antigenic and glycosylation sites in hemagglutinin protein of H5N1 strain. Bioinformation. 2009 Aug 17;4(1):30-5. doi: 10.6026/97320630004030. PMID: 20011150; PMCID: PMC2770368.
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Bioinformation. 2009 Aug 17;4(1):30-5. doi: 10.6026/97320630004030.

Identification of mutations at the antigenic and glycosylation sites in hemagglutinin protein of H5N1 strain.

Bioinformation

Parveen Salahuddin, Asad U Khan

PMID: 20011150 PMCID: PMC2770368 DOI: 10.6026/97320630004030

Abstract

Hemagglutinin (HA) is the principal antigen, present on the viral surface. It is the primary target for neutralizing antibodies. In this paper, we have carried out studies on human hemagglutinin protein from H5N1 strain with homologous hemagglutinin from non-human sources of H5N1 strains. In all strains, part of the antigenic site (128-141) predicted by computer program "Antigenic", corresponds to immunodominant site Sa of H1 subtype. In AAF02304 strain, A156-->S156 mutation lies at the antigenic subsite of site 2 that corresponds to site B in the H3 subtype. In some strains of non-human origins, there are mutations at the antigenic sites. Interestingly, in AAY56367 strain mutation L138-->H138 lies at the receptor binding site, which also overlaps the antigenic site. Therefore, this amino acid substitution may influence both the specificity of receptor recognition and antibody binding. Seven potential glycosylation sites in human HA and in some strains of non-human sources have been predicted by computer program, Scan Prosite. In some strains of HA from non-human sources because of mutation, an additional glycosylation site appeared at the antigenic site. Therefore in these strains the oligosaccharides will mask the surface of HA as well as antigenic site. Hence these strains will not be recognized by host immune system.

Keywords: antigenic site; avian influenza; hemagglutinin

References

  1. J Virol. 1998 Sep;72(9):7367-73 - PubMed
  2. Annu Rev Biochem. 1987;56:365-94 - PubMed
  3. Nature. 1981 Jan 29;289(5796):373-8 - PubMed
  4. J Gen Virol. 2002 Oct;83(Pt 10):2497-2505 - PubMed
  5. Avian Dis. 1974 Jan-Mar;18(1):119-24 - PubMed
  6. In Silico Biol. 2006;6(3):161-8 - PubMed
  7. Nature. 2003 Jul 10;424(6945):121-6 - PubMed
  8. Bioinformation. 2006 Apr 13;1(4):132 - PubMed
  9. Can J Microbiol. 1980 May;26(5):622-9 - PubMed
  10. Proc Natl Acad Sci U S A. 1984 Mar;81(6):1779-83 - PubMed
  11. Virus Res. 1993 Aug;29(2):155-65 - PubMed
  12. Mol Biol Evol. 2002 Apr;19(4):501-9 - PubMed
  13. Virology. 1990 Dec;179(2):759-67 - PubMed
  14. Cell. 1982 Dec;31(2 Pt 1):417-27 - PubMed
  15. Arch Virol. 2007;152(9):1637-44 - PubMed
  16. Virology. 1978 Feb;84(2):268-78 - PubMed
  17. Indian J Med Microbiol. 2004 Jul-Sep;22(3):143-6 - PubMed
  18. Virology. 1991 Jun;182(2):475-85 - PubMed

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