NMR assignments of the sylvatic dengue 1 virus envelope protein domain III

David E. Volk, Kurtis M. Anderson, Sai H. A. Gandham, Fiona J. May, Li Li, David W. C. Beasley, Alan D. T. Barrett, David G. Gorenstein
2008 Biomolecular NMR Assignments  
Nearly complete backbone and side chain resonance assignments have been obtained for the third domain, residues M289-K400, of the envelope protein from the sylvatic strain (P72-1244) of the dengue 1 virus, containing mutations N366S and E370K, using double-and triple-resonance spectroscopy. Biological context Dengue 1 virus (DEN1V) is a member of the family Flaviviridae, genus Flavivirus, which contains the dengue viruses (DEN 1-4) , West Nile virus, Langat virus, Omsk hemorrhagic fever virus
more » ... d many others. Receptor binding and membrane fusion of flaviviruses occurs with the envelope (E) protein (Heinz and Allison, 2003). The E protein ectodomain contains three domains, ED1, ED2 and ED3. The highly immunogenic ED3 is a putative receptorbinding domain and many neutralizing antibodies bind to ED3. Thus, ED3 is an attractive target for development of vaccines, anti-viral agents and diagnostic antigens. Chemical shift assignments and/or NMR-based structures for the ED3 proteins of Japanese encephalitis (Wu et al.
doi:10.1007/s12104-008-9109-5 pmid:19636893 pmcid:PMC2593834 fatcat:tuqiujruqjd6fhzob4rx5csjbu