Structural basis of the lipid transfer mechanism of phospholipid transfer protein (PLTP)

Biochim Biophys Acta Mol Cell Biol Lipids. 2018 Sep;1863(9):1082-1094. doi: 10.1016/j.bbalip.2018.06.001.

Meng Zhang ¹, Xiaobo Zhai ¹, Jinping Li ², John J Albers ³, Simona Vuletic ⁴, Gang Ren ⁵

Affiliations

1 The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, United States.
2 Department of Biomedical Science, Mercer University School of Medicine, Savannah, GA 31404, United States.
3 Northwest Lipid Metabolism and Diabetes Research Laboratories, Seattle, WA 98109, United States.
4 Northwest Lipid Metabolism and Diabetes Research Laboratories, Seattle, WA 98109, United States. Electronic address: simona@uw.edu.
5 The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, United States. Electronic address: gren@lbl.gov.

PMID: 29883800 DOI: 10.1016/j.bbalip.2018.06.001

Abstract

Human phospholipid transfer protein (PLTP) mediates the transfer of Phospholipids among atheroprotective high-density lipoproteins (HDL) and atherogenic low-density lipoproteins (LDL) by an unknown mechanism. Delineating this mechanism would represent the first step towards understanding PLTP-mediated lipid transfers, which may be important for treating lipoprotein abnormalities and Cardiovascular Disease. Here, using various electron microscopy techniques, PLTP is revealed to have a banana-shaped structure similar to cholesteryl ester transfer protein (CETP). We provide evidence that PLTP penetrates into the HDL and LDL surfaces, respectively, and then forms a ternary complex with HDL and LDL. Insights into the interaction of PLTP with lipoproteins at the molecular level provide a basis to understand the PLTP-dependent lipid transfer mechanisms for dyslipidemia treatment.

Keywords

Electron microscopy; HDL; Liposome; PLTP; PLTP bound to HDL; PLTP bound to liposome; Phospholipid transfer protein.

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