Authors: Wu, Guang; Yan, Shaomin

Source: Protein and Peptide Letters, Volume 13, Number 2, February 2006 , pp. 143-148(6)

Publisher: Bentham Science Publishers

Abstract:

In this study, we calculated the amino-acid distribution rank of 1201 hemagglutinins from influenza A viruses dated from 1918 to 2004 in order to compare them with respect to subtypes, species and years. After noticing fluctuations in distribution rank along the time course, we used the fast Fourier transform to determine the mutation periodicity of the hemagglutinins. Then we estimated our position at the current cycle of hemagglutinin evolutionary process to determine how many years remain before the next possible outbreak of influenza and bird flu. Finally, we used the trend channel to outlook the future of hemagglutinins for the next half A century. As our study covers almost all the full-length amino-acid sequences of hemagglutinins from various influenza A viruses, the conclusions will be valid for years until the number of hemagglutinins in Protein Databank is significantly increased.

Keywords: Distribution; Fast Fourier transform; Hemagglutinin; Influenza A virus; Mutation; Periodicity

Document Type: Research article

DOI: http://dx.doi.org/10.2174/092986606775101616

Affiliations: 1: Computational Mutation Project, DreamSciTech Consulting, 301, Building 12, Nanyou A-zone, Jiannan Road, Shenzhen, Guangdong Province, CN-518054, China.

Publication date: 2006-02-01

More about this publication?

• Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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