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Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.

Kyle W Roskamp1, David M Montelongo1, Chelsea D Anorma1

  • 1Department of Chemistry, University of California, Irvine, Irvine, California, United States.

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Human gammaS-crystallin (γS-crystallin) aggregation, a cause of cataracts, was studied under various conditions. The G18V variant showed increased aggregation, forming distinct structures via multiple pathways.

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Area of Science:

  • Ophthalmology
  • Biochemistry
  • Materials Science

Background:

  • Cataracts stem from light-scattering precipitates in the eye lens, often due to crystallin damage or mutations.
  • While excised cataracts are amorphous, in vitro crystallin studies reveal diverse morphologies based on preparation.
  • Human gammaS-crystallin (γS-crystallin) is a key structural protein in the lens, and its aggregation is implicated in certain cataracts.

Purpose of the Study:

  • To characterize thermal, pH-dependent, and UV-irradiated aggregates of wild-type human γS-crystallin (γS-WT) and its aggregation-prone variant, γS-G18V.
  • To investigate the influence of preparation methods on crystallin aggregate morphology and properties.

Main Methods:

  • Preparation of γS-WT and γS-G18V aggregates under acidic, neutral, and basic pH, at 25°C or 37°C for 48 hours.
  • UV-induced aggregate formation using a 355-nm laser.
  • Monitoring aggregation via turbidity and thioflavin T (ThT) assays; characterization using fluorescence, X-ray diffraction, and mass spectrometry.

Main Results:

  • The γS-G18V variant exhibited greater aggregation propensity than γS-WT under various conditions (heat, acid, UV).
  • Aggregates formed under basic and acidic conditions showed elevated ThT fluorescence, with low pH aggregates being less turbid.
  • UV-induced aggregates were highly turbid with moderate ThT fluorescence; X-ray diffraction confirmed amyloid character in low-pH and UV-irradiated samples.

Conclusions:

  • γS-G18V demonstrates increased aggregation susceptibility compared to γS-WT when exposed to heat, acid, or UV light.
  • The differing ThT fluorescence and turbidity of aggregates suggest multiple aggregation pathways are accessible for both proteins.
  • Preparation conditions significantly influence the structural characteristics and amyloidogenicity of γS-crystallin aggregates.