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Cataract-causing mutations S78F and S78P of γD-crystallin decrease protein conformational stability and drive

Ningqin Lin1, Ying Zhang2, Xiaohui Song3

  • 1Department of Nephrology, The Children's Hospital, Zhejiang University School of Medicine, National Clinical Research Center for Child Health, Hangzhou, Zhejiang Province, China; Eye Center of the Second Affiliated Hospital, Zhejiang University School of Medicine, 88 Jiefang Road, Hangzhou 310009, China; Institute of Translational Medicine, Zhejiang University School of Medicine, 268 Kaixuan Road, Hangzhou 310020, China.

International Journal of Biological Macromolecules
|September 22, 2023
PubMed
Summary
This summary is machine-generated.

Two congenital cataract mutations in gamma D-crystallin disrupt lens protein structure and cause aggregation. Lanosterol can reverse these aggregates, offering insights into childhood blindness mechanisms.

Keywords:
Congenital cataractLanosterolProtein aggregationProtein stabilityγD-crystallin

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Ophthalmology

Background:

  • Congenital cataract, a primary cause of childhood blindness, is often genetically driven.
  • Gamma D-crystallin (γD-crystallin) is crucial for lens transparency, and mutations can lead to cataracts.
  • The pathogenic mechanisms of many γD-crystallin mutations remain unclear.

Purpose of the Study:

  • To investigate the structural and aggregation mechanisms of two cataract-causing γD-crystallin mutations: Ser78Phe (S78F) and Ser78Pro (S78P).
  • To explore the role of the conserved Ser78 residue in maintaining γD-crystallin stability.
  • To assess the potential of lanosterol in reversing mutation-induced protein aggregation.

Main Methods:

  • Purification and structural characterization of wild-type (WT) and mutant γD-crystallin using fluorescence spectroscopy, circular dichroism (CD), and size-exclusion chromatography (SEC).
  • Expression of mutants in bacterial (E. coli) and mammalian cell lines (HLE-B3, HEK 293T) to study protein solubility and aggresome formation.
  • Investigation of aggregation under environmental stress and assessment of lanosterol's reversal effects.
  • Molecular dynamic simulations to analyze structural changes at the molecular level.

Main Results:

  • Both S78F and S78P mutants exhibited reduced solubility, increased hydrophobic exposure, and decreased thermal stability compared to WT γD-crystallin.
  • Overexpression of mutants induced aggresome formation in cell lines, and aggregation was exacerbated by heat, UV, and oxidative stress.
  • Lanosterol treatment reversed intracellular S78F and S78P aggregates.
  • Molecular dynamics simulations revealed that both mutations disrupt the integrity of Greek-key motif 2.

Conclusions:

  • The conserved Ser78 residue is vital for maintaining γD-crystallin structural stability.
  • S78F and S78P mutations destabilize the protein, leading to aggregation and potentially cataract formation.
  • Lanosterol shows potential for reversing crystallin aggregation, offering therapeutic insights for certain types of cataracts.