Short Bio

Olga Andrini is associated professor in the team "Molecular and cellular neurobiology of C. elegans" at the Institut NeuroMyoGène - CNRS/INSERM/Université Lyon 1 headed by Thomas Boulin. She has worked in various aspects of ionic transport across the plasma membrane of excitable cells and epithelia over the last 15 years. Her research work focuses on channels physiology and channels physiopathology.

During her PhD with Ian C. Forster, Heini Murer and François Verrey at University of Zürich (Switzerland), she studied the structure-function of membrane transport proteins, in particular the renal and intestinal phosphate transporters (Andrini, Channels 2008 and Andrini, Am J of Physiol Cell Physiol 2012). In collaboration with Dr. M. Egli and Prof. P. Dittrich (ETH, Zurich, Switzerland), she developed an elecrophysiological platform for studies in X. laevis conductance at different gravity levels. This system was successfully employed in parabolic flight campaigns of the European Space Agency (ESA) (Schaffhauser, Lab on a Chip 2011).
She moved to Sorbonne University (France), as a post-doc with Prof. Jacques Teulon where she worked on the functional investigation of intracellular regulation and pathological variants of renal chloride channels, ClC-K (Keck, Human Mutation 2013; L’Hoste, BBA-Biomembranes 2013; Andrini, Pflugers Arch. 2014).
In collaboration with Prof. Sepúlveda (University of Valdivia, Chile) she participated in the pharmacological characterization and modelling of a chloride channel, Glutamate-gated chloride channels (GluCls), a member of the Cys-loop receptor family (Corneio, PLoS Pathog. 2014).

Since 2015, she has established her electrophysiology rigs in the “Molecular and cellular neurobiology of C. elegans” where she works on potassium and chloride channels. She has expertise in applying electrophysiological techniques to both Xenopus oocyte and cell lines expressions systems. Her researches are now focusing on functional classification of genetic variants of unknown significance (KCNA1, KCNH2 and CLCNKB) (Seys E, J Am Soc Nephrol. 2017; Bignon, Human Mutation 2019); on the functional characterization of potassium channels in C. elegans (Ben Soussia, Nature Communications 2019) and on the roles of the renal chloride channels in the regulation of the hydrosodium balance (Hennings, J Am Soc Nephrol. 2017; Teulon, Compr Physiol. 2018). She teaches renal physiology to undergraduate students and electrophysiology to graduate students in biology and physiology, University of Lyon. .

Academic Positions & Education

Research Grants

  • 2014 - 2016 Prix « Jeune chercheur Gabriel Richet » – Fondation du Rein – Projet Syndrome de Bartter : une maladie encore à déchiffrer.
  • 2016  Bourse Qualité Recherche UCBL - Projet : « Compréhension de la régulation des canaux K2P »


11| Analysis of CLCNKB mutations at dimer-interface, calcium-binding site, and pore reveals a variety of functional alterations in ClC-Kb channel leading to Bartter syndrome.
Bignon Y, Sakhi I, Bitam S, Bakouh N, Keck M, Frachon N, Paulais M, Planelles G, Teulon J, Andrini O
Human Mutation (2019)
10| Mutation of a single residue promotes gating of vertebrate and invertebrate two-pore domain potassium channels.
Ben Soussia I, El Mouridi S, Kang D, Leclercq-Blondel A, Khoubza L, Tardy P, Zariohi N, Gendrel M, Lesage F, Kim EJ, Bichet D, Andrini O, Boulin T.
Nature Communications (2019) Download PDF here
Mutations that modulate the activity of ion channels are essential tools to understand the biophysical determinants that control their gating. Here, we reveal the conserved role played by a single amino acid position (TM2.6) located in the second transmembrane domain of two-pore domain potassium (K2P) channels. Mutations of TM2.6 to aspartate or asparagine increase channel activity for all vertebrate K2P channels. Using two-electrode voltage-clamp and single-channel recording techniques, we find that mutation of TM2.6 promotes channel gating via the selectivity filter gate and increases single channel open probability. Furthermore, channel gating can be progressively tuned by using different amino acid substitutions. Finally, we show that the role of TM2.6 was conserved during evolution by rationally designing gain-of-function mutations in four Caenorhabditis elegans K2P channels using CRISPR/Cas9 gene editing. This study thus describes a simple and powerful strategy to systematically manipulate the activity of an entire family of potassium channels.

9| Clinical and Genetic Spectrum of Bartter Syndrome Type 3.
Seys E, Andrini O, Keck M, Mansour-Hendili L, Courand PY, Simian C, Deschenes G, Kwon T, Bertholet-Thomas A, Bobrie G, Borde JS, Bourdat-Michel G, Decramer S, Cailliez M, Krug P, Cozette P, Delbet JD, Dubourg L, Chaveau D, Fila M, Jourde-Chiche N, Knebelmann B, Lavocat MP, Lemoine S, Djeddi D, Llanas B, Louillet F, Merieau E, Mileva M, Mota-Vieira L, Mousson C, Nobili F, Novo R, Roussey-Kesler G, Vrillon I, Walsh SB, Teulon J, Blanchard A, Vargas-Poussou R.
J Am Soc Nephrol. (2017)
8| The ClC-K2 Chloride Channel Is Critical for Salt Handling in the Distal Nephron.
Hennings JC, Andrini O, Picard N, Paulais M, Huebner AK, Cayuqueo IK, Bignon Y, Keck M, Cornière N, Böhm D, Jentsch TJ, Chambrey R, Teulon J, Hübner CA, Eladari D.
J Am Soc Nephrol. (2017)
7| Identification and functional expression of a glutamate- and avermectin-gated chloride channel from Caligus rogercresseyi, a southern Hemisphere sea louse affecting farmed fish.
Cornejo I, Andrini O, Niemeyer MI, Marabolí V, González-Nilo FD, Teulon J, Sepúlveda FV, Cid LP.
PLoS Pathog (2014)
6| CLCNKB mutations causing mild Bartter syndrome profoundly alter the pH and Ca2+ dependence of ClC-Kb channels.
Andrini O, Keck M, L'Hoste S, Briones R, Mansour-Hendili L, Grand T, Sepúlveda FV, Blanchard A, Lourdel S, Vargas-Poussou R, Teulon J.
Pflugers Arch. (2014)
5| Characterization of the mouse ClC-K1/Barttin chloride channel.
L'Hoste S, Diakov A, Andrini O, Genete M, Pinelli L, Grand T, Keck M, Paulais M, Beck L, Korbmacher C, Teulon J, Lourdel S.
Biochim Biophys Acta. (2013)
4| Novel CLCNKB mutations causing Bartter syndrome affect channel surface expression.
Keck M, Andrini O, Lahuna O, Burgos J, Cid LP, Sepúlveda FV, L'hoste S, Blanchard A, Vargas-Poussou R, Lourdel S, Teulon J.
Human Mutation (2013)
3| Lithium interactions with Na+-coupled inorganic phosphate cotransporters: insights into the mechanism of sequential cation binding.
Andrini O, Meinild AK, Ghezzi C, Murer H, Forster IC.
Physiol Cell Physiol (2012)
2| Microfluidic platform for electrophysiological studies on Xenopus laevis oocytes under varying gravity levels.
Schaffhauser DF, Andrini O, Ghezzi C, Forster IC, Franco-Obregón A, Egli M, Dittrich PS.
Lab Chip (2011)
1| Chondroitin sulfates act as extracellular gating modifiers on voltage-dependent ion channels.
Vigetti D, Andrini O, Clerici M, Negrini D, Passi A, Moriondo A
Cell Physiol Biochem (2008)


3| Renal Chloride Channels in Relation to Sodium Chloride Transport.
Teulon J, Planelles G, Sepúlveda FV, Andrini O, Lourdel S, Paulais M
Compr Physiol. (2018)
2| ClC-K chloride channels: emerging pathophysiology of Bartter syndrome type 3.
Andrini O, Keck M, Briones R, Lourdel S, Vargas-Poussou R, Teulon J
Am J Physiol Renal Physiol. (2015)
1| The leak mode of type II Na(+)-P(i) cotransporters.
Andrini O, Ghezzi C, Murer H, Forster IC
Channels (Austin) (2008)
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