Title

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

Authors

Parveen Salahuddin¹ and Asad U Khan^{1, 2*}

Affiliation

¹Distributed Information Sub-Centre, ²Interdisciplinary Biotechnology Unit, A.M.U., Aligarh 202002, India

Email

asad.k@rediffmail.com

Article Type

Hypothesis

Date

Received April 13, 2009; Revised June 12, 2009; Accepted June 13, 2009; Published August 17, 2009

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

Citation

Salahuddin & Khan, Bioinformation 4(1): 30-35 (2009)

Edited by

P. Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics 

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.