3DFlu: database of sequence and structural variability of the influenza hemagglutinin at population scale

The influenza virus type A (IVA) is an important pathogen which is able to cause annual epidemics and even pandemics. This fact is the consequence of the antigenic shifts and drifts capabilities of IVA, caused by the high mutation rate and the reassortment capabilities of the virus. The hemagglutinin (HA) protein constitutes the main IVA antigen and has a crucial role in the infection mechanism, being responsible for the recognition of host-specific sialic acid derivatives. Despite the relative abundance of HA sequence and serological studies, comparative structure-based analysis of HA are less investigated. The 3DFlu database contains well annotated HA representatives: 1192 models and 263 crystallographic structures. The relations between these proteins are defined using different metrics and are visualized as a network in the provided web interface. Moreover structural and sequence comparison of the proteins can be explored. Metadata information (e.g. protein identifier, IVA strain, year and location of infection) can enhance the exploration of the presented data. With our database researchers gain a useful tool for the exploration of high quality HA models, viewing and comparing changes in the HA viral subtypes at several information levels (sequence, structure, ESP). The complete and integrated view of those relations might be useful to determine the efficiency of transmission, pathogenicity and for the investigation of evolutionary tendencies of the influenza virus. Database URL: http://nucleus3d.cent.uw.edu.pl/influenza

[1]  Cédric Notredame,et al.  3DCoffee: combining protein sequences and structures within multiple sequence alignments. , 2004, Journal of molecular biology.

[2]  Ujjwal Maulik,et al.  Fuzzy clustering of physicochemical and biochemical properties of amino Acids , 2011, Amino Acids.

[3]  Ivet Bahar,et al.  ProDy: Protein Dynamics Inferred from Theory and Experiments , 2011, Bioinform..

[4]  Jian Wang,et al.  Influenza Virus Database (IVDB): an integrated information resource and analysis platform for influenza virus research , 2006, Nucleic Acids Res..

[5]  Nathan A. Baker,et al.  iAPBS: a programming interface to Adaptive Poisson-Boltzmann Solver (APBS). , 2012, Computational science & discovery.

[6]  Ryan McBride,et al.  A human-infecting H10N8 influenza virus retains a strong preference for avian-type receptors. , 2015, Cell host & microbe.

[7]  P. Horby,et al.  Estimated global mortality associated with the first 12 months of 2009 pandemic influenza A H1N1 virus circulation: a modelling study. , 2012, The Lancet. Infectious diseases.

[8]  Xiaoli Xiong,et al.  Receptor binding by H10 influenza viruses , 2014, Nature.

[9]  N. Sriwilaijaroen,et al.  Molecular basis of the structure and function of H1 hemagglutinin of influenza virus , 2012, Proceedings of the Japan Academy. Series B, Physical and biological sciences.

[10]  Jimin Pei,et al.  PCMA: fast and accurate multiple sequence alignment based on profile consistency , 2003, Bioinform..

[11]  A. Sali,et al.  Modeller: generation and refinement of homology-based protein structure models. , 2003, Methods in enzymology.

[12]  David J. Lipman,et al.  A global initiative on sharing avian flu data , 2006, Nature.

[13]  R. Webster,et al.  Lethal H5N1 influenza viruses escape host anti-viral cytokine responses , 2002, Nature Medicine.

[14]  T. N. Bhat,et al.  The Protein Data Bank , 2000, Nucleic Acids Res..

[15]  Razif R. Gabdoulline,et al.  Protein interaction property similarity analysis , 2001 .

[16]  Hiroyuki Ogata,et al.  AAindex: Amino Acid Index Database , 1999, Nucleic Acids Res..

[17]  Gert Vriend,et al.  A series of PDB related databases for everyday needs , 2010, Nucleic Acids Res..

[18]  T. Tatusova,et al.  The Influenza Virus Resource at the National Center for Biotechnology Information , 2007, Journal of Virology.

[19]  Nicolai Bovin,et al.  Receptor specificity of influenza viruses from birds and mammals: new data on involvement of the inner fragments of the carbohydrate chain. , 2005, Virology.

[20]  Shibo Jiang,et al.  Roles of the hemagglutinin of influenza A virus in viral entry and development of antiviral therapeutics and vaccines , 2010, Protein & Cell.

[21]  E. Myers,et al.  Basic local alignment search tool. , 1990, Journal of molecular biology.

[22]  Jacyr Pasternak Experimental adaptation of an influenza H5HA strain confers respiratory droplet transmission to reassortant H5H/H1N1 virus strain in ferrets. , 2012, Einstein.

[23]  Gert Vriend,et al.  Everyday , 2020, Oxford Research Encyclopedia of Literature.

[24]  Richard H Scheuermann,et al.  Influenza Research Database: an integrated bioinformatics resource for influenza research and surveillance , 2012, Influenza and other respiratory viruses.

[25]  J. Skolnick,et al.  TM-align: a protein structure alignment algorithm based on the TM-score , 2005, Nucleic acids research.

[26]  Nathan A. Baker,et al.  iAPBS: a programming interface to the adaptive Poisson–Boltzmann solver , 2012 .

[27]  Amos Bairoch,et al.  OpenFluDB, a database for human and animal influenza virus , 2010, Database J. Biol. Databases Curation.

[28]  Ian A. Wilson,et al.  Structure and Receptor Specificity of the Hemagglutinin from an H5N1 Influenza Virus , 2006, Science.

[29]  Jeffrey S. Hall,et al.  Evolution of a reassortant North American gull influenza virus lineage: drift, shift and stability , 2013, Virology Journal.

[30]  Ya Ha,et al.  H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes , 2002, The EMBO journal.

[31]  Pascal Benkert,et al.  QMEAN server for protein model quality estimation , 2009, Nucleic Acids Res..

[32]  Vincent B. Chen,et al.  Correspondence e-mail: , 2000 .