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High resolution crystal structure of dengue‐3 envelope protein domain III suggests possible molecular mechanisms for serospecific antibody recognition
Author(s) -
Elahi Montasir,
Islam Monirul M.,
Noguchi Keiichi,
Yohda Masafumi,
Kuroda Yutaka
Publication year - 2013
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24237
Subject(s) - epitope , dengue fever , envelope (radar) , virology , dengue virus , antibody , recombinant dna , protein structure , chemistry , biology , genetics , biochemistry , gene , computer science , telecommunications , radar
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. © 2012 Wiley Periodicals, Inc.