Fig 1.
Graphical representation of the methodology undertaken during the study.
Table 1.
Comparison of blood parameters between dengue patients with dengue fever (DF) and dengue hemorrhagic fever (DHF).
Fig 2.
Agarose gel electrophoresis of the amplicons generated from PCR using different primer sets.
Primer set 1, 2, 3 and 4 covered the entire coding region of GATA1. For proper estimation of the size of the DNA bands, 100bp ladder DNA was used. S1 = Sample 1; S2 = Sample 2; NC = Negative Control.
Table 2.
Variations in the exonic regions of GATA1 along with their respective frequency distribution in total patients, patients with DF and DHF as well as annotation in database.
Table 3.
Variations of GATA1 gene and their subsequent amino acid changes in protein sequence.
Fig 3.
Comparative analyses of the platelet counts.
(A) Between different groups of dengue patients with respect to variants recognized within the exonic regions of GATA1 gene with respect to nonsynonymous mutations and wild genotype (those harboring exactly the same sequence as the reference nucleotides). (B) Platelet counts of patients with nonsynonymous and wild type variants in GATA1 gene were stratified according to DF and DHF. Data has been presented as mean±SEM and p<0.05 was considered as the level of significance. Statistical analyses revealed that neither of the groups had significant differences.
Table 4.
Association of DNA variants with platelets count before and after adjusting the confounding factors in female dengue patients.
Table 5.
Prediction of association between GATA1 nonsynonymous mutations and disease.
Fig 4.
Structure analyses of ab initio GATA1 modelled protein.
(A) Predicted 3D structure of the protein (B) Ramachandran plot of the structure (C) Z-score plot from PROSA (D) Residual error value plot from ERRAT2.
Fig 5.
Surface structure of the modelled GATA1 protein with structural domains.
N-terminal activation domain, AD (red color), N-terminal Zinc finger domain, N-ZF (orange color) and C terminal Zinc finger domain, C-ZF (purple color).
Table 6.
Structure analyses of mutated amino acids in GATA1 protein using Pymol and Missense3D.
Fig 6.
Evaluation of the effect of nonsynonymous mutations on the structure and interactions between side chain and neighboring residues.
Among non-synonymous mutations, P21H (A) and S26T (B) mutations were found in the AD domain of the protein while Q262H (F) was within the C-ZF domain. Other mutations including S91L (C), G99S (D), S129N (E) and H289D (G) were found in regions outside the functional domains of GATA1 protein.