Sticholysin I–II oligomerization in the absence of membranes

Sara García-Linares; Rafael Amigot-Sánchez; Carmen García-Montoya; Diego Heras-Márquez; Carlos Alfonso; Juan Román Luque-Ortega; José G. Gavilanes; Álvaro Martínez-del-Pozo; Juan Palacios-Ortega

doi:10.1002/1873-3468.14326

Sticholysin I–II oligomerization in the absence of membranes

Sara García-Linares
, Rafael Amigot-Sánchez
, Carmen García-Montoya
, Diego Heras-Márquez
, Carlos Alfonso
, Juan Román Luque-Ortega
, José G. Gavilanes
, Álvaro Martínez-del-Pozo
, Juan Palacios-Ortega^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Scientific › peer-review

2 Citations (Scopus)

46 Downloads (Pure)

Abstract

Sticholysins are pore-forming toxins produced by the sea anemone Stichodactyla helianthus. When they encounter a sphingomyelin-containing membrane, these proteins bind to it and oligomerize, a process that ends in pore formation. Mounting evidence indicates that StnII can favour the activity of StnI. Previous results have shown that these two isotoxins can oligomerize together. Furthermore, StnII appeared to potentiate the activity of StnI through the membrane-binding step of the process. Hence, isotoxin interaction should occur prior to membrane encounter. Here, we have used analytical ultracentrifugation to investigate the oligomerization of Stns in solution, both separately and together. Our results indicate that while StnI seems to be more prone to oligomerize in water solution than StnII, a small percentage of StnII in StnI–StnII mixtures promotes oligomerization.

Original language	English
Pages (from-to)	1029-1036
Number of pages	8
Journal	FEBS Letters
Volume	596
Issue number	8
DOIs	https://doi.org/10.1002/1873-3468.14326
Publication status	Published - Apr 2022
MoE publication type	A1 Journal article-refereed

Funding

This research was supported by the Juselius Foundation (JP‐O), UCM‐Banco Santander Grants PR75/18‐21561 and PR87/19‐22556, and UnaEuropa (Unano) SF2106 (to AM‐d‐P) and Spanish Ministry of Science and Innovation PID2019‐104544GB‐I00 (CA). JP‐O has a funded doctoral student position from ISB/ÅA. JRL‐O acknowledges support from the Molecular Interactions Facility funds at the CIB‐CSIC. This research was supported by the Juselius Foundation (JP-O), UCM-Banco Santander Grants PR75/18-21561 and PR87/19-22556, and UnaEuropa (Unano) SF2106 (to AM-d-P) and Spanish Ministry of Science and Innovation PID2019-104544GB-I00 (CA). JP-O has a funded doctoral student position from ISB/?A. JRL-O acknowledges support from the Molecular Interactions Facility funds at the CIB-CSIC.

Keywords

actinoporins
analytical ultracentrifugation
pore-forming proteins
sedimentation velocity

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10.1002/1873-3468.14326

Sticholysin I II oligomerization in the absence of membranesFinal published version, 682 KBLicence: CC BY-NC

https://urn.fi/URN:NBN:fi-fe2023022228214

Cite this

@article{25df3501f88440f4b7639cd1a91ea3ff,

title = "Sticholysin I–II oligomerization in the absence of membranes",

abstract = "Sticholysins are pore-forming toxins produced by the sea anemone Stichodactyla helianthus. When they encounter a sphingomyelin-containing membrane, these proteins bind to it and oligomerize, a process that ends in pore formation. Mounting evidence indicates that StnII can favour the activity of StnI. Previous results have shown that these two isotoxins can oligomerize together. Furthermore, StnII appeared to potentiate the activity of StnI through the membrane-binding step of the process. Hence, isotoxin interaction should occur prior to membrane encounter. Here, we have used analytical ultracentrifugation to investigate the oligomerization of Stns in solution, both separately and together. Our results indicate that while StnI seems to be more prone to oligomerize in water solution than StnII, a small percentage of StnII in StnI–StnII mixtures promotes oligomerization.",

keywords = "actinoporins, analytical ultracentrifugation, pore-forming proteins, sedimentation velocity",

author = "Sara Garc{\'i}a-Linares and Rafael Amigot-S{\'a}nchez and Carmen Garc{\'i}a-Montoya and Diego Heras-M{\'a}rquez and Carlos Alfonso and Luque-Ortega, \{Juan Rom{\'a}n\} and Gavilanes, \{Jos{\'e} G.\} and {\'A}lvaro Mart{\'i}nez-del-Pozo and Juan Palacios-Ortega",

note = "Funding Information: This research was supported by the Juselius Foundation (JP‐O), UCM‐Banco Santander Grants PR75/18‐21561 and PR87/19‐22556, and UnaEuropa (Unano) SF2106 (to AM‐d‐P) and Spanish Ministry of Science and Innovation PID2019‐104544GB‐I00 (CA). JP‐O has a funded doctoral student position from ISB/{\AA}A. JRL‐O acknowledges support from the Molecular Interactions Facility funds at the CIB‐CSIC. Funding Information: This research was supported by the Juselius Foundation (JP-O), UCM-Banco Santander Grants PR75/18-21561 and PR87/19-22556, and UnaEuropa (Unano) SF2106 (to AM-d-P) and Spanish Ministry of Science and Innovation PID2019-104544GB-I00 (CA). JP-O has a funded doctoral student position from ISB/?A. JRL-O acknowledges support from the Molecular Interactions Facility funds at the CIB-CSIC. Publisher Copyright: {\textcopyright} 2022 The Authors. FEBS Letters published by John Wiley \& Sons Ltd on behalf of Federation of European Biochemical Societies.",

year = "2022",

month = apr,

doi = "10.1002/1873-3468.14326",

language = "English",

volume = "596",

pages = "1029--1036",

journal = "FEBS Letters",

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number = "8",

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T1 - Sticholysin I–II oligomerization in the absence of membranes

AU - García-Linares, Sara

AU - Amigot-Sánchez, Rafael

AU - García-Montoya, Carmen

AU - Heras-Márquez, Diego

AU - Alfonso, Carlos

AU - Luque-Ortega, Juan Román

AU - Gavilanes, José G.

AU - Martínez-del-Pozo, Álvaro

AU - Palacios-Ortega, Juan

N1 - Funding Information: This research was supported by the Juselius Foundation (JP‐O), UCM‐Banco Santander Grants PR75/18‐21561 and PR87/19‐22556, and UnaEuropa (Unano) SF2106 (to AM‐d‐P) and Spanish Ministry of Science and Innovation PID2019‐104544GB‐I00 (CA). JP‐O has a funded doctoral student position from ISB/ÅA. JRL‐O acknowledges support from the Molecular Interactions Facility funds at the CIB‐CSIC. Funding Information: This research was supported by the Juselius Foundation (JP-O), UCM-Banco Santander Grants PR75/18-21561 and PR87/19-22556, and UnaEuropa (Unano) SF2106 (to AM-d-P) and Spanish Ministry of Science and Innovation PID2019-104544GB-I00 (CA). JP-O has a funded doctoral student position from ISB/?A. JRL-O acknowledges support from the Molecular Interactions Facility funds at the CIB-CSIC. Publisher Copyright: © 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

PY - 2022/4

Y1 - 2022/4

N2 - Sticholysins are pore-forming toxins produced by the sea anemone Stichodactyla helianthus. When they encounter a sphingomyelin-containing membrane, these proteins bind to it and oligomerize, a process that ends in pore formation. Mounting evidence indicates that StnII can favour the activity of StnI. Previous results have shown that these two isotoxins can oligomerize together. Furthermore, StnII appeared to potentiate the activity of StnI through the membrane-binding step of the process. Hence, isotoxin interaction should occur prior to membrane encounter. Here, we have used analytical ultracentrifugation to investigate the oligomerization of Stns in solution, both separately and together. Our results indicate that while StnI seems to be more prone to oligomerize in water solution than StnII, a small percentage of StnII in StnI–StnII mixtures promotes oligomerization.

AB - Sticholysins are pore-forming toxins produced by the sea anemone Stichodactyla helianthus. When they encounter a sphingomyelin-containing membrane, these proteins bind to it and oligomerize, a process that ends in pore formation. Mounting evidence indicates that StnII can favour the activity of StnI. Previous results have shown that these two isotoxins can oligomerize together. Furthermore, StnII appeared to potentiate the activity of StnI through the membrane-binding step of the process. Hence, isotoxin interaction should occur prior to membrane encounter. Here, we have used analytical ultracentrifugation to investigate the oligomerization of Stns in solution, both separately and together. Our results indicate that while StnI seems to be more prone to oligomerize in water solution than StnII, a small percentage of StnII in StnI–StnII mixtures promotes oligomerization.

KW - actinoporins

KW - analytical ultracentrifugation

KW - pore-forming proteins

KW - sedimentation velocity

UR - https://www.scopus.com/pages/publications/85126036594

U2 - 10.1002/1873-3468.14326

DO - 10.1002/1873-3468.14326

M3 - Article

C2 - 35253212

AN - SCOPUS:85126036594

SN - 0014-5793

VL - 596

SP - 1029

EP - 1036

JO - FEBS Letters

JF - FEBS Letters

IS - 8

ER -

Sticholysin I–II oligomerization in the absence of membranes

Abstract

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Keywords

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