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

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

Volume: 13 Issue: 1

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

Affiliation:

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

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.

Cite this article as:

Moran-Palacio F. E., Tricerri A. M., Garcia-Orozco K., Romo-Figueroa G. M., Yepiz-Plascencia G., Garda A. H. and Sotelo-Mundo R. R., Biophysical Characterization of the Non-Fusogenic Interaction Between Liposomes and the Shrimp Bifunctional Lipoprotein-β-Glucan Binding Protein HDL/BGBP, Protein & Peptide Letters 2006; 13 (1) . https://dx.doi.org/10.2174/092986606774502054