Solution structure of the envelope protein domain III of dengue-4 virus

Virology

Volumn 364, Issue 1, 2007, Pages 147-154

  Volk, David E ^a   Lee, Yi Chien ^a   Li, Xin ^a   Thiviyanathan, Varatharasa ^a   Gromowski, Gregory D ^a,b   Li, Li ^a,b   Lamb, Ashley R ^c   Beasley, David W C ^a,b   Barrett, Alan D T ^a,b   Gorenstein, David G ^a  

^a University of Texas Medical Branch School of Medicine   (United States)

^b UNIVERSITY OF TEXAS MEDICAL BRANCH   (United States)

^c UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

Dengue; Dengue 4 virus; Envelope protein domain III; Flavivirus; Nuclear magnetic resonance; Structure

Indexed keywords

VIRUS ENVELOPE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; DENGUE VIRUS; HUMAN; HUMAN CELL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; RECEPTOR BINDING; VIRUS CELL INTERACTION; VIRUS STRAIN;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; ANTIBODIES, VIRAL; DENGUE VIRUS; ELECTROSTATICS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; THERMODYNAMICS; VIRAL ENVELOPE PROTEINS;

FLAVIVIRUS;

EID: 34249651385     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2007.02.023     Document Type: Article

References (46)

1. Bax A., Clore G.M., and Gronenborn A.M. H-1-H-1 correlation via isotropic mixing of C-13 magnetization, a new 3-dimensional approach for assigning H-1 and C-13 spectra of C-13 enriched proteins. J. Magn. Reson. 88 (1990) 425-431
2. Calisher C.H., Karabatsos N., Dalrymple J.M., Shope R.E., Porterfield J.S., Westaway E.G., and Brandt W.E. Antigenic relationships between flaviviruses as determined by cross-neutralization tests with polyclonal antisera. J. Gen. Virol. 70 (1989) 37-43
3. Case D.A., Pearlman D.A., Caldwell J.W., Cheatham III T.E., Rose W.S., Simmerling C.L., Darden K.M., Merz R.V., Stanton A.L., Cheng J.J., Vincent M., Crowley D.M., Ferguson R.J., Radmer G.L., Seibel U.C., Singh P.K., Weiner S.J., and Kollman P.A. AMBER6.0 (1999), University of California, San Francisco, CA
4. Chu J.J., Rajamanonmani R., Bhuvanakantham R., Lescar J., and Ng M.L. Inhibition of West Nile virus entry by using a recombinant domain III from the envelope glycoprotein. J. Gen. Virol. 86 (2005) 405-412
5. Clore G.M., and Gronenborn A.M. Multidimensional heteronuclear nuclear magnetic resonance of proteins. Methods Enzymol. 239 (1994) 249-363
6. Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
7. Crill W., and Roehrig J.T. Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J. Virol. 75 (2001) 7769-7773
8. Duggan B.M., Legge G.B., and Wright P.E. SANE (Structure assisted NOE evaluation): an automated model-based approach for NOE assignment. J. Biomol. NMR 19 (2001) 321-329
9. Ferrin T.E., Huang C.C., Jarvis L.C., and Langridge R. The MIDAS Display System. J. Mol. Graph. 6 (1988) 13-27
10. Grzesiek S., and Bax A. Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114 (1992) 6291-6293
11. Heinz F.X., and Allison S.L. Structures and mechanisms in flavivirus fusion. Adv. Virus Res. 55 (2000) 231-269
12. Heinz F.X., and Allison S.L. The machinery for flavivirus fusion with host cell membranes. Curr. Opin. Microbiol. 4 (2001) 450-455
13. Heinz F.X., and Allison S. Flavivirus structure and membrane fusion. Adv. Virus Res. 59 (2003) 63-97
14. Hiramatsu K., Tadano M., Men R., and Lai C.J. Mutational analysis of a neutralization epitope on the dengue type 2 virus (DEN2) envelope protein: monoclonal antibody resistant DEN2/DEN4 chimeras exhibit reduced mouse neurovirulence. Virology 224 (1996) 437-445
15. Hung J.J., Hsieh M.T., Young M.J., Kao C.L., King C.C., and Chang W. An external loop region of domain III of dengue virus type 2 envelope protein is involved in serotype-specific binding to mosquito but not mammalian cells. J. Virol. 78 (2004) 378-388
16. Ikura M., Bax A., Clore G.M., and Gronenborn A.M. Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional NMR spectroscopy. J. Am. Chem. Soc. 112 (1990) 9020-9022
17. John B., Plant D., and Hurd R.E. A simple experimental scheme using pulsed field gradients for coherence pathway rejection and solvent suppression in phase-sensitive heteronuclear correlation spectra. J. Magn. Reson., Ser. A 101 (1993) 113
18. Kanai R., Kar K., Anthony K., Gould L.H., Ledizet M., Fikrig E., Koski R.A., and Modis Y. Crystal structure of West Nile virus envelope glycoprotein reveals viral surface epitopes. J. Virol. 80 (2006) 11000-11008
19. Kay L.E., Kiefer R., and Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114 (1992) 10663-10665
20. Koradi R., Billeter M., and Wuthrich K. MOLMOL: A Program for Display and Analysis of Macromolecular Structure (1996), Institute for Molecular Biology and Biophysics, Swiss Federal Institute of Technology, Zürich, Switzerland
21. Kuhn R.J., Zhang W., Rossman M.G., Pletnev S.V., Corver J., Lenches E., Jones C.T., Mukhopadhyay S., Chipman P.R., Strauss E.G., Baker T.S., and Strauss J.H. Structure of dengue virus: implications for flavivirus organization, maturation and fusion. Cell 108 (2002) 717-725
22. Laskowski R.A., Rullman J.A.C., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-496
23. Lin B., Parrish C.R., Murray J.M., and P.J. Wright P.J. Localization of a neutralizing epitope on the envelope protein of dengue virus type 2. Virology 202 (1994) 885-890
24. Lohr F., and Ruterjans H. A new triple-resonance experiment for the assignment of backbone resonances in proteins. J. Biomol. NMR 6 (1995) 189-197
25. Lok S.M., Ng M.L., and Aaskov J. Amino acid and phenotypic changes in dengue 2 virus associated with escape from neutralisation by IgM antibody. J. Med. Virol. 65 (2001) 315-323
26. Mandl C., Guirakhoo F., Holzmann H., Heinz F.X., and Kunz C. Antigenic structure of the flavivirus envelope protein E at the molecular level, using tick-borne encephalitis virus as a model. J. Virol. 63 (1989) 564-571
27. Marion D., Kay L.E., Sparks S.W., Torchia D.A., and Bax A. Three-dimensional heteronuclear NMR of 15N labeled proteins. J. Am. Chem. Soc. 111 (1989) 1515-1517
28. Modis Y., Ogata S., Clements D., and Harrison S.C. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 6986-6991
29. Modis Y., Ogata S., Clements D., and Harrison S.C. Structure of the dengue virus envelope protein after membrane fusion. Nature 427 (2004) 313-319
30. Modis Y., Ogata S., Clements D., and Harrison S.C. Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J. Virol. 79 (2005) 1223
31. Mukhopadhyay S., Kim B.-S., Chipman P.R., Rossman M.G., and Kuhn R.J. Structure of West Nile virus. Science 302 (2003) 248
32. Mukherjee M., Dutta K., White M.A., Cowburn D., and Fox R.O. NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition. Prot. Sci. 15 (2006) 1342-1355
33. Nybakken G.E., Oliphant T., Johnson S., Burke S., Diamond M.S., and Fremont D.H. Structural basis of West Nile virus neutralization by a therapeutic antibody. Nature 437 (2005) 764-769
34. Nybakken G.E., Nelson C.A., Chen B.R., Diamond M.S., and Fremont D.H. Crystal structure of the West Nile virus envelope glycoprotein. J. Virol. 80 (2006) 11467-11474
35. Rey F.A., Heinz F.X., Mandl C.W., Kunz C., and Harrison S.C. The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature 375 (1995) 198-291
36. Roehrig J.T. Antigenic structure of flavivirus proteins. Adv. Virus Res. 59 (2003) 141-175
37. Sattler M., Schleucher J., and Griesinger C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. NMR Spectrosc. 34 (1999) 93-158
38. Twiddy S.S., Woelk C.H., and Holmes E.C. Phylogenetic evidence for adaptive evolution of dengue viruses in nature. J. Gen. Virol. 83 (2002) 1679-1689
39. Twiddy S.S., Holmes E.C., and Rambaut A. Inferring the rate and time-scale of dengue virus evolution. Mol. Biol. Evol. 20 (2003) 122-129
40. Volk D.E., Beasley D.W.C., Kallick D.A., Holbrook M.R., Barrett A.D.T., and Gorenstein D.G. Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus. J. Biol. Chem. 279 (2004) 38755-38761
41. Volk D.E., Chavez L., Beasley D.W.C., Barrett A.D.T., Holbrook M.R., and Gorenstein D.G. Structure of the envelope protein domain III of Omsk hemorrhagic fever virus. Virology 351 (2006) 188-195
42. Volk D.E., Lee Y.-C., Li X., Barrett A.D.T., and Gorenstein D.G. 1H, 13C and 15N assignments of the dengue-4 envelope protein domain III. J. Biomol. NMR 36 (2006) 62
43. Vuister G.W., and Bax A. Resolution enhancement and spectral editing of uniformly 13C enriched proteins by homonuclear broadband 13C decoupling. J. Magn. Reson. 98 (1992) 428-435
44. Wang E., Ni H., Xu R., Barrett A.D., Watowich S.J., Gubler D.J., and Weaver S.C. Evolutionary relationships of endemic/epidemic and sylvatic dengue viruses. J. Virol. 74 (2000) 3227-3234
45. Wu K.-P., Wu C.-W., Tsao Y.-P., Kuo T.-W., Lou Y.-C., Lin C.-W., Wu S.-C., and Cheng J.-W. Structural basis of a flavivirus recognized by its neutralizing antibody. J. Biol. Chem. 278 (2003) 46007-46013
46. Yamazaki T., Forman-Kay J.D., and Kay L.E. 2-Dimensional NMR experiments for correlating C-13 beta and H-1-delta/epsilon chemical-shifts of aromatic residues in C-13-labeled proteins via scalar couplings. J. Am. Chem. Soc. 115 (1993) 11054-11055