To acknowledge above data, we screen GJA8 gene of 27 cataract patients with no family history of cataract, a subtle 1104G>C (pE368Q) (GenBank KY556641) transversion that substitutes glutamic acid to glutamine was identified at exon 2 of GJA8 gene in one of the patient, which revealed that glutamic acid at position 368 in normal GJA8 protein was changed to glutamine, which is highlighted in Figure 6.
Substitution of negatively charged amino acid with neutral interrupts its interaction with neighboring molecules but have no inauspicious effect on the overall structure of mutated GJA8 protein.
Energetically mutated GJA8 is immensely stable in comparison to wild type GJA8 with an energy difference of -2.72 kcal/mol.
Mutational screening of GJA8 gene showed substitution of glutamic acid to glutamine at codon position 368 in the coding region of GJA8 exon 2, which is a novel mutation.
A novel Cx50 (GJA8) p.H277Y mutation associated with autosomal dominant congenital cataract identified with targeted next-generation sequencing.
Identification of a novel GJA8 (Cx50) point mutation causes human dominant congenital cataracts.
A novel mutation in GJA8 causing congenital cataract-microcornea syndrome in a Chinese pedigree.
Mutation screening and genotype phenotype correlation of [alpha]-crystallin, g-crystallin, and GJA8 gene in congenital cataract.
To date, about 28 GJA8 mutations have been reported in CC patients [Figure 1]d.
In this study, by combined NGS and targeted genomic enrichment technology, we identified a novel 15 deletion in a highly conserved region of CL domain of the GJA8 gene associated with cataracts in a three-generation Chinese family with ADCC (mutations have never reported in CL domain before).