Cys mutants as tools to study the oligomerization of the pore-forming toxin sticholysin I
DC Element | Wert | Sprache |
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dc.contributor.author | Hervis, Yadira P. | |
dc.contributor.author | Valle, Aisel | |
dc.contributor.author | Canet, Liem | |
dc.contributor.author | Rodriguez, Azalia | |
dc.contributor.author | Lanio, Maria E. | |
dc.contributor.author | Alvarez, Carlos | |
dc.contributor.author | Steinhoff, Heinz J. | |
dc.contributor.author | Pazos, Isabel F. | |
dc.date.accessioned | 2023-07-12T06:57:24Z | - |
dc.date.available | 2023-07-12T06:57:24Z | - |
dc.date.issued | 2023 | |
dc.identifier.issn | 0041-0101 | |
dc.identifier.uri | http://osnascholar.ub.uni-osnabrueck.de/handle/unios/71994 | - |
dc.description.abstract | Sticholysin I (StI) is a water-soluble protein with the ability to bind membranes where it oligomerizes and forms pores leading to cell death. Understanding the assembly property of this protein may be valuable for designing potential biotechnological tools, such as stable or structurally defined nanopores. In order to get insights into the stabilization of StI oligomers by disulfide bonds, we designed and characterized single and double cysteine mutants at the oligomerization interface. The oligomer formation was induced in the presence of lipid membranes and visualized by SDS-PAGE. The contribution of the oligomeric structures to the membrane binding and pore-forming capacities of StI was assessed. Single and double cysteine introduction at the protein-protein oligomerization interface does not considerably affect the conformation and function of the monomeric protein. In the presence of membranes, a cysteine double mutation at positions 15 and 59 favored formation of different size oligomers stabilized by disulfide bonds. The results of this work highlight the relevance of these positions (15 and 59) to be considered for developing biosensors based on nanopores from StI. | |
dc.description.sponsorship | International Foundation for Science [F/4574-1, F/4574-2]; EMBO [ASTF 157-2015]; DAAD [57214227]; IUBMB Wood-Whelan fellowship; We acknowledge the financial support for this research provided by International Foundation for Science (IFS Grant F/4574-1 and F/4574-2 to A V.) . YP H. was recipient of EMBO (ASTF 157-2015) and DAAD (57214227) Short Term Fellowships, as well as the IUBMB Wood-Whelan fellowship. | |
dc.language.iso | en | |
dc.publisher | PERGAMON-ELSEVIER SCIENCE LTD | |
dc.relation.ispartof | TOXICON | |
dc.subject | ACTINOPORINS | |
dc.subject | Cys mutants | |
dc.subject | disulfide bond formation | |
dc.subject | DISULFIDE BONDS | |
dc.subject | EQUINATOXIN-II | |
dc.subject | FRAGACEATOXIN C | |
dc.subject | FUNCTIONAL-CHARACTERIZATION | |
dc.subject | MECHANISM | |
dc.subject | MEMBRANE PERMEABILIZATION | |
dc.subject | MULTIGENE FAMILIES | |
dc.subject | Oligomerization | |
dc.subject | Pharmacology & Pharmacy | |
dc.subject | Pore-forming protein | |
dc.subject | SEA-ANEMONE STICHODACTYLA | |
dc.subject | ST-II | |
dc.subject | Sticholysins | |
dc.subject | Toxicology | |
dc.title | Cys mutants as tools to study the oligomerization of the pore-forming toxin sticholysin I | |
dc.type | journal article | |
dc.identifier.doi | 10.1016/j.toxicon.2022.106994 | |
dc.identifier.isi | ISI:000912528800001 | |
dc.description.volume | 222 | |
dc.identifier.eissn | 1879-3150 | |
dc.publisher.place | THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND | |
dcterms.isPartOf.abbreviation | Toxicon | |
local.import.remains | affiliations : Universidad de la Habana; University Osnabruck; Centre National de la Recherche Scientifique (CNRS); UDICE-French Research Universities; Sorbonne Universite; Universite PSL; Ecole Normale Superieure (ENS); Le Reseau International des Instituts Pasteur (RIIP); Institut Pasteur de Montevideo | |
local.import.remains | earlyaccessdate : DEC 2022 | |
local.import.remains | web-of-science-index : Science Citation Index Expanded (SCI-EXPANDED) | |
crisitem.author.dept | FB 04 - Physik | - |
crisitem.author.deptid | fb04 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | StHe633 | - |
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geprüft am 06.06.2024