By a News Reporter-Staff News Editor at Information Technology Newsweekly -- Current study results on Bioinformatics have been published. According to news reporting originating in Bethesda, Maryland, by VerticalNews journalists, research stated, "Influenza A viruses possess RNA genomes that mutate frequently in response to immune pressures. The mutations in the hemagglutinin genes are particularly significant, as the hemagglutinin proteins mediate attachment and fusion to host cells, thereby influencing viral pathogenicity and species specificity."
The news reporters obtained a quote from the research from the National Institute of Allergy and Infectious Diseases (NIAID), "Large-scale influenza A genome sequencing efforts have been ongoing to understand past epidemics and pandemics and anticipate future outbreaks. Sequencing efforts thus far have generated nearly 9,000 distinct hemagglutinin amino acid sequences. Comparative models for all publicly available influenza A hemagglutinin protein sequences (8,769 to date) were generated using the Rosetta modeling suite. The C-alpha root mean square deviations between a randomly chosen test set of models and their crystallographic templates were less than 2 A, suggesting that the modeling protocols yielded high-quality results. The models were compiled into an online resource, the Hemagglutinin Structure Prediction (HASP) server. The HASP server was designed as a scientific tool for researchers to visualize hemagglutinin protein sequences of interest in a three-dimensional context. With a built-in molecular viewer, hemagglutinin models can be compared side-by-side and navigated by a corresponding sequence alignment. The models and alignments can be downloaded for offline use and further analysis. The modeling protocols used in the HASP server scale well for large amounts of sequences and will keep pace with expanded sequencing efforts. The conservative approach to modeling and the intuitive search and visualization interfaces allow researchers to quickly analyze hemagglutinin sequences of interest in the context of the most highly related experimental structures, and allow them to directly compare hemagglutinin sequences to each other simultaneously in their two-and three-dimensional contexts."
According to the news reporters, the research concluded: "The models and methodology have shown utility in current research efforts and the ongoing aim of the HASP server is to continue to accelerate influenza A research and have a positive impact on global public health."
For more information on this research see: HASP server: a database and structural visualization platform for comparative models of influenza A hemagglutinin proteins. Bmc Bioinformatics, 2013;14():197. (BioMed Central - www.biomedcentral.com/; Bmc Bioinformatics - www.biomedcentral.com/bmcbioinformatics/)
Our news correspondents report that additional information may be obtained by contacting X.I. Ambroggio, Bioinformatics and Computational Biosciences Branch, Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, United States. Additional authors for this research include J. Dommer, V. Gopalan, E.J. Dunham, J.K. Taubenberger and D.E Hurt.
Keywords for this news article include: Bethesda, Maryland, Peptides, Proteins, Amino Acids, United States, Bioinformatics, North and Central America.
Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2013, NewsRx LLC