CD81 extracted in SMALP nanodiscs comprises two distinct protein populations within a lipid environment enriched with negatively charged headgroups.

Szczegóły
Abstrakt

Tytuł:: CD81 extracted in SMALP nanodiscs comprises two distinct protein populations within a lipid environment enriched with negatively charged headgroups.
Autorzy:: Ayub H; College of Health & Life Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK.
Clare M; College of Health & Life Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK.
Milic I; College of Health & Life Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK.
Chmel NP; Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, UK.
Böning H; German Center for Infection Research (DZIF) Hannover-Braunschweig Site and Institute of Virology, Hannover Medical School, 30625 Hannover, Germany.
Devitt A; College of Health & Life Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK.
Krey T; German Center for Infection Research (DZIF) Hannover-Braunschweig Site and Institute of Virology, Hannover Medical School, 30625 Hannover, Germany; Center of Structural and Cell Biology in Medicine, Institute of Biochemistry, University of Luebeck, Luebeck, Germany; Centre for Structural Systems Biology (CSSB), Hamburg, Germany.
Bill RM; College of Health & Life Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK. Electronic address: .
Rothnie AJ; College of Health & Life Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK. Electronic address: .
Źródło:: Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2020 Nov 01; Vol. 1862 (11), pp. 183419. Date of Electronic Publication: 2020 Jul 28.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Original Publication: Amsterdam : Elsevier
MeSH Terms:: Models, Molecular*
Protein Folding*
Tetraspanin 28/*chemistry
Crystallography, X-Ray ; Humans ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Saccharomycetales ; Tetraspanin 28/genetics ; Tetraspanin 28/metabolism
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Grant Information:: BB/N007417/1 International Biotechnology & Biosciences Research Council; BB/S00324X/1 International Biotechnology & Biosciences Research Council; BB/M006298/1 International Biotechnology & Biosciences Research Council
Contributed Indexing:: Keywords: Membrane protein; Purification; SMALP; Solubilisation; Stability; Tetraspanin
Substance Nomenclature:: 0 (CD81 protein, human)
0 (Recombinant Proteins)
0 (Tetraspanin 28)
SCR Organism:: Komagataella pastoris
Entry Date(s):: Date Created: 20200801 Date Completed: 20201229 Latest Revision: 20210110
Update Code:: 20240104
PubMed Central ID:: PMC7456796
DOI:: 10.1016/j.bbamem.2020.183419
PMID:: 32735789
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Tetraspanins exert a wide range of cellular functions of broad medical importance. Despite this, their biophysical characteristics are incompletely understood. Only two high-resolution structures of full-length tetraspanins have been solved. One is that of human CD81, which is involved in the infectivity of human pathogens including influenza, HIV, the malarial Plasmodium parasite and hepatitis C virus (HCV). The CD81 crystal structure identifies a cholesterol-binding pocket, which has been suggested to be important in the regulation of tetraspanin function. Here we investigate the use of styrene-maleic anhydride co-polymers (SMA) for the solubilisation and purification of CD81 within a lipid environment. When CD81 was expressed in the yeast Pichia pastoris, it could be solubilised and purified using SMA2000. This SMALP-encapsulated CD81 retained its native folded structure, as determined by the binding of two conformation-sensitive anti-CD81 antibodies. Analysis by size exclusion chromatography revealed two distinct populations of CD81, only one of which bound the HCV glycoprotein, E2. Optimization of expression and buffer conditions increased the proportion of E2-binding competent CD81 protein. Mass spectrometry analysis indicated that the lipid environment surrounding CD81 is enriched with negatively charged lipids. These results establish a platform to study the influence of protein-lipid interactions in tetraspanin biology.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.)

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