title: High resolution crystal structure of dengue-3 envelope protein domain III suggests possible molecular mechanisms for serospecific antibody recognition.
abstract: Dengue viruses are classified into four serotypes. Here, we report a 1.7 Å crystal structure of a recombinant dengue-3 envelope protein domain III (ED3), which contains most of the putative epitopes. Although the fold was well conserved, we found that a local backbone deformation in the first β-strand, which contains the putative epitope-1, occurred upon domain isolation. Furthermore, a comparison with dengue-2 ED3 indicated a large structural change by as much as 4.0 Å at Asp(662), located in epitope-2. These minute structural and surface properties changes observed in the high resolution ED3 structure represent potential determinants for serospecificity and epitope recognition by antibodies.
authors.affiliation: Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, Koganei-shi, Tokyo, Japan.
authors.forename: Montasir
authors.initials: M
authors.lastname: Elahi
authors.forename: Monirul M
authors.initials: MM
authors.lastname: Islam
authors.forename: Keiichi
authors.initials: K
authors.lastname: Noguchi
authors.forename: Masafumi
authors.initials: M
authors.lastname: Yohda
authors.forename: Yutaka
authors.initials: Y
authors.lastname: Kuroda
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D003715:Dengue / Q000821:virology*; D003716:Dengue Virus / Q000737:chemistry*; D000939:Epitopes / Q000737:chemistry; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D016415:Sequence Alignment; D014759:Viral Envelope Proteins / Q000737:chemistry*
chemical_list: D000939:Epitopes; D011994:Recombinant Proteins; D014759:Viral Envelope Proteins