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

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

Document Type: Research Article

Affiliations: Aquatic Molecular Biology Laboratory, Centro de Investigacion en Alimentacion y Desarrollo, A.C. PO Box 1735, Hermosillo Sonora, 83000 Mexico.

Publication date: 2006-01-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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