Aixia Jin1, Yu Zhang2, Dongchang Xiao1, Mengqing Xiang1,3, Kangxin Jin1, Mingbing Zeng1,4. 1. State Key Laboratory of Ophthalmology, Zhongshan Ophthalmic Center, Sun Yat-sen University, Guangzhou, China. 2. Department of Gastroenterology, Renmin Hospital of Wuhan University, Wuhan, China. 3. Guangdong Provincial Key Laboratory of Brain Function and Disease, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, China. 4. Hainan Eye Hospital, Hainan Key Laboratory of Ophthalmology, Zhongshan Ophthalmic Center, Sun Yat-sen University, Haikou, China.
Abstract
Purpose: To identify the pathogenetic mutations in a four-generation Chinese family with dominant congenital cataracts and microphthalmia. Methods: A four-generation Chinese family with dominant congenital cataracts were recruited. Genomic DNAs were collected from their peripheral blood leukocytes and subjected to whole exome sequencing. The genetic mutations were identified by bioinformatic analyses and verified by Sanger sequencing. Results: Whole exome sequencing revealed a c.279C>G point mutation in the CRYBB1 gene which was further verified by Sanger sequencing. The nucleotide replacement results in a novel mutation p.S93R in a conserved residue of βB1 crystallin which is predicted to disrupt normal βB1 structure and function.Conclusions: We identified a novel missense mutation p.S93R in CRYBB1 in a Chinese family with autosomal dominant congenital cataracts and microphthalmia. This serine residue is extremely conserved evolutionarily in more than 50 βγ-crystallins of many species. These data will be very helpful to further understand the structural and functional features of crystallins.
Purpose: To identify the pathogenetic mutations in a four-generation Chinese family with dominant congenital cataracts and microphthalmia. Methods: A four-generation Chinese family with dominant congenital cataracts were recruited. Genomic DNAs were collected from their peripheral blood leukocytes and subjected to whole exome sequencing. The genetic mutations were identified by bioinformatic analyses and verified by Sanger sequencing. Results: Whole exome sequencing revealed a c.279C>G point mutation in the CRYBB1 gene which was further verified by Sanger sequencing. The nucleotide replacement results in a novel mutation p.S93R in a conserved residue of βB1 crystallin which is predicted to disrupt normal βB1 structure and function.Conclusions: We identified a novel missense mutation p.S93R in CRYBB1 in a Chinese family with autosomal dominant congenital cataracts and microphthalmia. This serine residue is extremely conserved evolutionarily in more than 50 βγ-crystallins of many species. These data will be very helpful to further understand the structural and functional features of crystallins.
Authors: Philippa Harding; Maria Toms; Elena Schiff; Nicholas Owen; Suzannah Bell; Ian Christopher Lloyd; Mariya Moosajee Journal: Int J Mol Sci Date: 2021-02-22 Impact factor: 5.923
Authors: Johanna L Jones; Bennet J McComish; Sandra E Staffieri; Emmanuelle Souzeau; Lisa S Kearns; James E Elder; Jac C Charlesworth; David A Mackey; Jonathan B Ruddle; Deepa Taranath; John Pater; Theresa Casey; Jamie E Craig; Kathryn P Burdon Journal: BMJ Open Ophthalmol Date: 2022-08