Biophysical characterization of the non-fusogenic interaction between liposomes and the shrimp bifunctional lipoprotein-beta-glucan binding protein HDL/BGBP.
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.
Morán-Palacio
Edgar F
EF
Aquatic Molecular Biology Laboratory, Centro de Investigación en Alimentación y Desarrollo, A.C. PO Box 1735, Hermosillo Sonora, 83000 México.
Tricerri
M Alejandra
MA
García-Orozco
Karina
K
Romo-Figueroa
Maria Gabriela
MG
Yepiz-Plascencia
Gloria
G
Garda
Horacio A
HA
Sotelo-Mundo
Rogerio R
RR
D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D002352:Carrier Proteins / Q000737:chemistry* / Q000648:ultrastructure; D008076:Cholesterol, HDL / Q000737:chemistry*; D003445:Crustacea; D037102:Lectins / Q000737:chemistry* / Q000648:ultrastructure; D008081:Liposomes; D008563:Membrane Lipids / Q000737:chemistry; D008854:Microscopy, Electron; D013050:Spectrometry, Fluorescence
D002352:Carrier Proteins; D008076:Cholesterol, HDL; D037102:Lectins; D008081:Liposomes; D008563:Membrane Lipids; C037937:glucan-binding proteins