Biophysical characterization of the non-fusogenic interaction between liposomes and the shrimp bifunctional lipoprotein-beta-glucan binding protein HDL/BGBP

Protein Pept Lett. 2006;13(1):71-5. doi: 10.2174/092986606774502054.

Abstract

Shrimp High Density Lipoprotein-beta-Glucan Binding Protein (HDL/BGBP) has been studied by its role in nutrition and innate defense. Although the mechanisms of lipid loading are still unknown, HDL-BGBP binds and aggregates phospholipids vesicles in vitro. To gain insights into the HDL-BGBP mechanism of interaction with membranes, we have used fluorescence spectroscopy and electron microscopy. Data show that HDL-BGBP does not induce membrane fusion, leakage nor lipid exchange, although microstructural changes are clearly observed. This work supports a model where protein aggregation leads to liposome clustering. Such interaction may be a critical factor for the activation of the shrimp blood cell in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biophysical Phenomena
  • Biophysics
  • Carrier Proteins / chemistry*
  • Carrier Proteins / ultrastructure
  • Cholesterol, HDL / chemistry*
  • Crustacea
  • Lectins / chemistry*
  • Lectins / ultrastructure
  • Liposomes
  • Membrane Lipids / chemistry
  • Microscopy, Electron
  • Spectrometry, Fluorescence

Substances

  • Carrier Proteins
  • Cholesterol, HDL
  • Lectins
  • Liposomes
  • Membrane Lipids
  • glucan-binding proteins