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Updated: Aug 18, 2026
Preparation and Immunofluorescence Staining of Bundles and Single Fiber Cells from the Cortex and Nucleus of the Eye Lens
Published on: June 9, 2023
Interaction and biophysical properties of human lens Q155* betaB2-crystallin mutant
1Center for Ophthalmic Research/Surgery, Brigham and Women's Hospital, Boston, MA 02115, USA.
Purpose:
Missense mutations in crystallin genes have been identified in autosomal dominant congenital cataracts. A truncation in the CRYBB2 gene (Q155*) has been associated with cerulean cataract, however its effects on biophysical properties have not been reported. We sought to determine the changes in conformation and protein-protein interactions brought about by this mutation.
Methods:
Site specific mutations were performed to obtain the Q155* betaB2-crystallin mutant. Protein-protein interactions were screened by a mammalian two-hybrid system assay. Conformational changes were studied with spectroscopy (circular dichroism and fluorescence) and FPLC chromatography.
Results:
We detected a decrease in protein-protein interactions for the Q155* betaB2-crystallin mutant. The Q155* mutant shows decreased ordered structure and stability but the partially unfolded protein retains some dimer structure.
Conclusions:
The Q155* mutation in betaB2-crystallin causes changes in biophysical properties that might contribute to cataract formation.
