Biophysical Characterization of the Non-Fusogenic Interaction Between Liposomes and the Shrimp Bifunctional Lipoprotein-β-Glucan Binding Protein HDL/BGBP

Author(s): E. F. Moran-Palacio, M. A. Tricerri, K. Garcia-Orozco, M. G. Romo-Figueroa, G. Yepiz-Plascencia, H. A. Garda, R. R. Sotelo-Mundo.

Journal Name: Protein & Peptide Letters

Volume 13 , Issue 1 , 2006

Become EABM
Become Reviewer


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.

Keywords: High density lipoprotein, beta-glucan binding protein, shrimp, Crustacea, Litopenaeus vannamei, liposome, aggregation

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2006
Page: [71 - 75]
Pages: 5
DOI: 10.2174/092986606774502054

Article Metrics

PDF: 9