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2000
Volume 13, Issue 1
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

Shrimp High Density Lipoprotein-β-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.

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/content/journals/ppl/10.2174/092986606774502054
2006-01-01
2025-06-04
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