Pandey, Kalpana and Rathore, Yogendra S and Nath, Samir K and Ganguly, Ashish (2014) Towards strain-independent anti-influenza peptides: a SAXS- and modeling-based study. Journal of biomolecular structure & dynamics, 32 (11). pp. 1720-33. ISSN 1538-0254
Full text not available from this repository. (Request a copy)Abstract
Using small angle X-ray scattering (SAXS) data, we reconstructed the scattering shape of the Hemagglutinin (HA) trimer protein from five different influenza strains. Comparison with the known crystal structures-based information aided in identifying volumes pertaining to the glycosylation in the HA trimers. By merging sequence information on HA proteins from pathogenic strains of influenza, we identified a novel druggable pocket composed of residues which remained conserved during evolution, lack propensity to be glycosylated, and play important role in maintaining interchain contacts in the pH-sensitive head group. To test our hypothesis that molecules reactive to this site may retard pH-induced opening of HA trimer in strain-independent manner, we performed in vitro screening of peptides representing interacting epitopes for their ability to retard pH-induced opening of HA trimers. Results brought forth that some of the 20 peptides tested can retard low pH-induced opening/association of HA proteins across different subtypes, thus propagating notion that the drug site and peptides identified here may pave way towards strain-independent anti-influenza molecules.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to Taylor & Francis. |
| Uncontrolled Keywords: | influenza, hemagglutinin trimer, sequence alignment, glycosylation, normal mode analysis, small angle X-ray scattering, drug site, peptide design |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 19 Jul 2015 11:58 |
| Last Modified: | 19 Jul 2015 11:58 |
| URI: | http://crdd.osdd.net/open/id/eprint/1717 |
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