Case Report: A de novo Variant of CRYGC Gene Associated With Congenital Cataract and Microphthalmia

Abstract

Background: Congenital cataract is one of the most common causes of blindness in children. A rapid and accurate genetic diagnosis benefit the patients in the pediatric department. The current study aims to identify the genetic defects in a congenital cataract patient without a family history.Case presentation: A congenital cataract patient with microphthalmia and nystagmus was recruited for this study. Trio-based whole-exome sequencing revealed a de novo variant (c.394delG, p.V132Sfs*15) in CRYGC gene. According to the American College of Medical Genetics and Genomics (ACMG) criteria, the variant could be annontated as pathogenic.Conclusion: Our findings provide new knowledge of the variant spectrum of CRYGC gene and are essential for understanding the heterogeneity of cataracts in the Chinese population.

Novel CRYGC Mutation in Conserved Ultraviolet-Protective Tryptophan (p.Trp131Arg) Is Linked to Autosomal Dominant Congenital Cataract

“…To date, the Online Mendelian Inheritance in Man (OMIM) documented the identification of 49 loci and 37 genes associated with isolated CC (https://www.ncbi.nlm.nih.gov/omim/ (accessed on 9 July 2023)). These associated genes can broadly be grouped into cytoplasmic proteins (i.e., crystallins), membrane proteins (i.e., connexins, aquaporins), cytoskeletal proteins, and DNA/RNA-binding proteins (i.e., transcription factors) [13,14].…”

“…α-crystallins are small heat shock proteins. They exert their chaperone function by binding to unfolded or damaged βand γ-crystallins to prevent their aggregation, preserving lens transparency [13]. βand γ-crystallins function as structural proteins and contain Greek key domains as secondary protein structures [13].…”

“…They exert their chaperone function by binding to unfolded or damaged βand γ-crystallins to prevent their aggregation, preserving lens transparency [13]. βand γ-crystallins function as structural proteins and contain Greek key domains as secondary protein structures [13]. A primary distinction between βand γ-crystallins lies in their ability to assemble into oligomers.…”