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Hen lysozyme amyloid fibrils induce aggregation of erythrocytes and lipid vesicles

Nitin Chaudhary1, Ramakrishnan Nagaraj

  • 1Centre for Cellular and Molecular Biology, Hyderabad, India.

Molecular and Cellular Biochemistry
|March 27, 2009
PubMed

Insights

Hen egg white lysozyme (HEWL) amyloid fibrils aggregate human red blood cells and lipid vesicles without causing significant cell damage. This membrane activity suggests a potential role in disease pathogenesis.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Biophysics

Background:

  • Amyloid fibrils are protein aggregates implicated in various diseases.
  • Lysozyme can form amyloid structures.
  • Cellular membrane interactions are crucial for understanding disease mechanisms.

Purpose of the Study:

  • To investigate the interaction between hen egg white lysozyme (HEWL) amyloid fibrils and human erythrocytes.
  • To examine the effect of HEWL fibrils on lipid vesicles.
  • To assess the membrane activity and potential cellular consequences of HEWL fibril interactions.

Main Methods:

  • Preparation of hen egg white lysozyme (HEWL) amyloid fibrils.
  • Incubation of HEWL fibrils with human erythrocytes (red blood cells).
  • Incubation of HEWL fibrils with model lipid vesicles.
  • Microscopic observation and aggregation assays.

Main Results:

  • HEWL amyloid fibrils induced significant aggregation of human erythrocytes.
  • HEWL fibrils also caused aggregation of lipid vesicles.
  • No significant lysis (cell membrane rupture) was observed for erythrocytes.
  • The fibrils demonstrated notable membrane activity.

Conclusions:

  • HEWL amyloid fibrils interact with and aggregate cellular membranes, including erythrocytes and lipid vesicles.
  • The observed membrane activity, without significant lysis, highlights a specific type of cellular interaction.
  • These findings suggest that the interaction of lysozyme fibrils with cellular membranes may contribute to disease processes.

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