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

MORAN-PALACIO, E. F.; TRICERRI, M. A.; GARCIA-OROZCO, K; ROMO-FIGUEROA, M. G.; YEPIZ-PLASCENCIA, G.; GARDA, H. A.; SOTELO-MUNDO, R. R.

PROTEIN AND PEPTIDE LETTERS

Bentham Science

Año: 2006 vol. 13 p. 71 - 75

0929-8665

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.