Lipid binding attenuates channel closure of the outer membrane protein OmpF.

التفاصيل البيبلوغرافية
العنوان:	Lipid binding attenuates channel closure of the outer membrane protein OmpF.
المؤلفون:	Liko I; Department of Chemistry, University of Oxford, Oxford OX1 5QY, United Kingdom.; OMass Technologies, Begbroke Science Park, Kidlington OX5 1PF, United Kingdom., Degiacomi MT; Department of Chemistry, University of Oxford, Oxford OX1 5QY, United Kingdom., Lee S; Department of Chemistry, University of Oxford, Oxford OX1 5QY, United Kingdom., Newport TD; Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom., Gault J; Department of Chemistry, University of Oxford, Oxford OX1 5QY, United Kingdom., Reading E; Department of Chemistry, University of Oxford, Oxford OX1 5QY, United Kingdom., Hopper JTS; Department of Chemistry, University of Oxford, Oxford OX1 5QY, United Kingdom.; OMass Technologies, Begbroke Science Park, Kidlington OX5 1PF, United Kingdom., Housden NG; Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom., White P; Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom., Colledge M; Institute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, United Kingdom., Sula A; Institute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, United Kingdom., Wallace BA; Institute of Structural and Molecular Biology, Birkbeck College, University of London, London WC1E 7HX, United Kingdom., Kleanthous C; Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom., Stansfeld PJ; Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom., Bayley H; Department of Chemistry, University of Oxford, Oxford OX1 5QY, United Kingdom., Benesch JLP; Department of Chemistry, University of Oxford, Oxford OX1 5QY, United Kingdom., Allison TM; Department of Chemistry, University of Oxford, Oxford OX1 5QY, United Kingdom; timothy.allison@canterbury.ac.nz carol.robinson@chem.ox.ac.uk., Robinson CV; Department of Chemistry, University of Oxford, Oxford OX1 5QY, United Kingdom; timothy.allison@canterbury.ac.nz carol.robinson@chem.ox.ac.uk.; OMass Technologies, Begbroke Science Park, Kidlington OX5 1PF, United Kingdom.
المصدر:	Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2018 Jun 26; Vol. 115 (26), pp. 6691-6696. Date of Electronic Publication: 2018 Jun 11.
نوع المنشور:	Journal Article; Research Support, Non-U.S. Gov't
اللغة:	English
بيانات الدورية:	Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
أسماء مطبوعة:	Original Publication: Washington, DC : National Academy of Sciences
مواضيع طبية MeSH:	Phosphatidylcholines/metabolism , Phosphatidylglycerols/metabolism , Porins/*metabolism, Bacterial Outer Membrane Proteins/chemistry ; Bacterial Outer Membrane Proteins/metabolism ; Cation Transport Proteins/chemistry ; Cation Transport Proteins/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/metabolism ; Hydrogen-Ion Concentration ; Models, Chemical ; Models, Molecular ; Molecular Dynamics Simulation ; Porins/chemistry ; Protein Binding ; Protein Conformation ; Spectrometry, Mass, Electrospray Ionization ; Voltage-Dependent Anion Channels/chemistry ; Voltage-Dependent Anion Channels/metabolism ; Voltage-Gated Sodium Channels/chemistry ; Voltage-Gated Sodium Channels/metabolism
مستخلص:	Strong interactions between lipids and proteins occur primarily through association of charged headgroups and amino acid side chains, rendering the protonation status of both partners important. Here we use native mass spectrometry to explore lipid binding as a function of charge of the outer membrane porin F (OmpF). We find that binding of anionic phosphatidylglycerol (POPG) or zwitterionic phosphatidylcholine (POPC) to OmpF is sensitive to electrospray polarity while the effects of charge are less pronounced for other proteins in outer or mitochondrial membranes: the ferripyoverdine receptor (FpvA) or the voltage-dependent anion channel (VDAC). Only marginal charge-induced differences were observed for inner membrane proteins: the ammonia channel (AmtB) or the mechanosensitive channel. To understand these different sensitivities, we performed an extensive bioinformatics analysis of membrane protein structures and found that OmpF, and to a lesser extent FpvA and VDAC, have atypically high local densities of basic and acidic residues in their lipid headgroup-binding regions. Coarse-grained molecular dynamics simulations, in mixed lipid bilayers, further implicate changes in charge by demonstrating preferential binding of anionic POPG over zwitterionic POPC to protonated OmpF, an effect not observed to the same extent for AmtB. Moreover, electrophysiology and mass-spectrometry-based ligand-binding experiments, at low pH, show that POPG can maintain OmpF channels in open conformations for extended time periods. Since the outer membrane is composed almost entirely of anionic lipopolysaccharide, with similar headgroup properties to POPG, such anionic lipid binding could prevent closure of OmpF channels, thereby increasing access of antibiotics that use porin-mediated pathways. Competing Interests: Conflict of interest statement: I.L. and J.T.S.H. are employees of OMass Technologies. Carol Robinson is a cofounder and member of the board of directors of OMass Technologies. (Copyright © 2018 the Author(s). Published by PNAS.)
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معلومات مُعتمدة:	BB/L006790 United Kingdom Biotechnology and Biological Sciences Research Council; 104633/Z/14/Z United Kingdom Wellcome Trust; United Kingdom Medical Research Council; BB/L021234/1 United Kingdom Biotechnology and Biological Sciences Research Council; BB/L026251 United Kingdom Biotechnology and Biological Sciences Research Council; United Kingdom Wellcome Trust
فهرسة مساهمة:	Keywords: OmpF; lipids; mass spectrometry
المشرفين على المادة:	0 (AmtB protein, E coli) 0 (Bacterial Outer Membrane Proteins) 0 (Cation Transport Proteins) 0 (Escherichia coli Proteins) 0 (FpvA protein, Pseudomonas aeruginosa) 0 (OmpF protein) 0 (Phosphatidylcholines) 0 (Phosphatidylglycerols) 0 (Porins) 0 (Voltage-Dependent Anion Channels) 0 (Voltage-Gated Sodium Channels) 81490-05-3 (1-palmitoyl-2-oleoylglycero-3-phosphoglycerol) TE895536Y5 (1-palmitoyl-2-oleoylphosphatidylcholine)
تواريخ الأحداث:	Date Created: 20180613 Date Completed: 20180907 Latest Revision: 20181114
رمز التحديث:	20231215
مُعرف محوري في PubMed:	PMC6042154
DOI:	10.1073/pnas.1721152115
PMID:	29891712
قاعدة البيانات:	MEDLINE

الوصف
تدمد:	1091-6490
DOI:	10.1073/pnas.1721152115