Manjiri Kulkarni - Academia.edu (original) (raw)
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Papers by Manjiri Kulkarni
Acta Crystallographica Section A Foundations and Advances, 2017
Biochemical and Biophysical Research Communications, 2016
Acta Crystallographica Section A Foundations and Advances, 2017
Biomolecules
Dengue fever is a mosquito-borne endemic disease in tropical and subtropical regions, causing a s... more Dengue fever is a mosquito-borne endemic disease in tropical and subtropical regions, causing a significant public health problem in Southeast Asia. Domain III (ED3) of the viral envelope protein contains the two dominant putative epitopes and part of the heparin sulfate receptor binding region that drives the dengue virus (DENV)’s fusion with the host cell. Here, we used high-hydrostatic-pressure nuclear magnetic resonance (HHP-NMR) to obtain residue-specific information on the folding process of domain III from serotype 4 dengue virus (DEN4-ED3), which adopts the classical three-dimensional (3D) ß-sandwich structure known as the Ig-like fold. Interestingly, the folding pathway of DEN4-ED3 shares similarities with that of the Titin I27 module, which also adopts an Ig-like fold, but is functionally unrelated to ED3. For both proteins, the unfolding process starts by the disruption of the N- and C-terminal strands on one edge of the ß-sandwich, yielding a folding intermediate stable ...
Dengue viruses are classified into four serotypes (DENV1∼4), and the severe forms of dengue disea... more Dengue viruses are classified into four serotypes (DENV1∼4), and the severe forms of dengue disease, the dengue hemorrhagic fever and shock syndrome, are caused by sero-cross-reacting antibodies. However, the residue determinants of the serospecificity and sero-cross-reactivity are yet to be identified. Here, we report an epitope grafting mutational analysis of the serospecificity and cross-serospecificity of the envelope protein domain 3 (ED3; 107 residues, ∼11.6kDa), which contains two major putative epitopes of DENVs. To this end, we constructed ED3 from DENV3 (3ED3) and DENV4 (4ED3), and six epitope-grafted variants, where we transferred epitope 1 (L304I, K305D, V309M, and S310A) and/or epitope 2 (D383N, K384S, K387T, and N389H) of 4ED3 onto 3ED3 and vice versa. Mice immunization using 3ED3 and 4ED3 generated serotype-specific antisera, as expected. Similarly, most epitope-grafted ED3s produced antisera serospecific to the template ED3 with little or no cross-recognition of ED3 ...
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2015
Acta Crystallographica Section A Foundations and Advances, 2017
Biochemical and Biophysical Research Communications, 2016
Acta Crystallographica Section A Foundations and Advances, 2017
Biomolecules
Dengue fever is a mosquito-borne endemic disease in tropical and subtropical regions, causing a s... more Dengue fever is a mosquito-borne endemic disease in tropical and subtropical regions, causing a significant public health problem in Southeast Asia. Domain III (ED3) of the viral envelope protein contains the two dominant putative epitopes and part of the heparin sulfate receptor binding region that drives the dengue virus (DENV)’s fusion with the host cell. Here, we used high-hydrostatic-pressure nuclear magnetic resonance (HHP-NMR) to obtain residue-specific information on the folding process of domain III from serotype 4 dengue virus (DEN4-ED3), which adopts the classical three-dimensional (3D) ß-sandwich structure known as the Ig-like fold. Interestingly, the folding pathway of DEN4-ED3 shares similarities with that of the Titin I27 module, which also adopts an Ig-like fold, but is functionally unrelated to ED3. For both proteins, the unfolding process starts by the disruption of the N- and C-terminal strands on one edge of the ß-sandwich, yielding a folding intermediate stable ...
Dengue viruses are classified into four serotypes (DENV1∼4), and the severe forms of dengue disea... more Dengue viruses are classified into four serotypes (DENV1∼4), and the severe forms of dengue disease, the dengue hemorrhagic fever and shock syndrome, are caused by sero-cross-reacting antibodies. However, the residue determinants of the serospecificity and sero-cross-reactivity are yet to be identified. Here, we report an epitope grafting mutational analysis of the serospecificity and cross-serospecificity of the envelope protein domain 3 (ED3; 107 residues, ∼11.6kDa), which contains two major putative epitopes of DENVs. To this end, we constructed ED3 from DENV3 (3ED3) and DENV4 (4ED3), and six epitope-grafted variants, where we transferred epitope 1 (L304I, K305D, V309M, and S310A) and/or epitope 2 (D383N, K384S, K387T, and N389H) of 4ED3 onto 3ED3 and vice versa. Mice immunization using 3ED3 and 4ED3 generated serotype-specific antisera, as expected. Similarly, most epitope-grafted ED3s produced antisera serospecific to the template ED3 with little or no cross-recognition of ED3 ...
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2015