http://icim.marseille.inserm.fr/spip.php?article97

IPC - CRCM - Marseille

Mélange de protéomes: étude du Microbiote

Imagerie par spectrométrie de masse

Echange Hydrogène Deutérium

Protéomique Top Down

Marquage isobarique

Glycoprotéomique

Protéomique ciblée

Interactome

Next generation proteomics

VIIIème Rencontre du réseau des plates-formes protéomiques

de la région Provence Alpes Côte d’Azur

29 Juin 2017

Nos soutiens académiques

Nos soutiens privés

PROTEOPACA 2017

Sommaire

Programme 6 Résumé des conférences. - Stéphane AUDEBERT, CRCM, Marseille. 9 - Julien PELTIER, Newcastle University, UK. 10 - Nicolas AUTRET – Somalogic 11 - Séga NDIAYE – Thermo-Scientific 12 - Julia CHAMOT-ROOKE, Institut Pasteur, Paris. 13 - Jean-Baptiste VINCENDET – Sciex 14 - Mourad FERHAT – Promega 15 - Céline HENRY, INRA PAPPSO, Jouy-en-Josas. 16 - Sébastien BRIER, Institut Pasteur, Paris. 17 - Luc CAMOIN, CRCM, Marseille. 18 - Thibaut LEGER, Institut Jacques Monod, Paris. 19 - Anaïs BAUDOT, I2M, Marseille. 20 - Angeline KERNALLEGUEN, CRO2, Marseille. 21

Liste des inscrits. 22

29 Juin 2017

6

Résumés des conférences

PROTEOPACA 2017

Stéphane Audebert Marseille Protéomique,

Centre de Recherche en Cancérologie de Marseille

INSERM U1068 - CNRS UMR7258 - Aix-Marseille

Université UM105

Marseille, France

Interactome: new tools for protein complexes identification

The Proteomic platform at CRCM emerged from Jean-Paul Borg’s team that works for

several years in the field of protein-protein interactions, cell polarity and its deregulation

in cancer development. Our platform developed a very strong expertise in the discovery of

novel protein-protein interactions and identification of protein complexes using affinity-

purification mass spectrometry (AP-MS) approaches. I will illustrate my talk with a few

examples of protein complexes identified by immunoprecipitation, pulldown, or peptides

pulldown these last years and will present the last strategies we favour since more

efficient precipitation tools called nanobodies are available. New strategies as BirA or

APEX approaches allowing the identification of low affinity or transient partners will also

be presented.

Besides biochemical development, improvement of mass spectrometers with higher scan

speed, higher sensitivity and dynamic range as well as choice of quantitative strategies

allow us to go deeper and faster into the proteomes to detect low abundant interactors.

References

- Audebert S, et al. Mammalian Scribble forms a tight complex with the betaPIX exchange factor. Curr

Biol. (2004).

- Puvirajesinghe TM, et al. Identification of p62/SQSTM1 as a component of non-canonical Wnt

VANGL2-JNK signalling in breast cancer. Nat Commun. (2016).

- Daulat A.M., et al. PRICKLE1 contributes to cancer cell dissemination through its interaction with

mTORC2. Developmental Cell, (2016).

- Cartier-Michaud A, et al. Genetic, structural, and chemical insights into the dual function of GRASP55

in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis. PLoS Genet.

(2017).

- Belotti E, et al. The human PDZome: a gateway to PSD95-Disc large-zonula occludens (PDZ)-mediated

functions. Mol Cell Proteomics. (2013).

- Daou P, et al. Essential and nonredundant roles for Diaphanous formins in cortical microtubule capture

and directed cell migration. Mol Biol Cell. (2014).

- Verdier-Pinard P, et al. Septin 9_i2 is downregulated in tumors, impairs cancer cell migration and alters

subnuclear actin filaments. Sci Rep. (2017).

9

10

Julien Peltier Institute for Cell and Molecular Biosciences (ICAMB)

Faculty of Medical Sciences, Newcastle University

Newcastle Upon Tyne, NE2 4HH

Thermal profiling of Breast cancer cells reveals proteasomal

activation by CDK4/6 inhibitor Palbociclib [1]

Palbociclib (Ibrance®, Pfizer) is a recent drug approved by the FDA for phase III clinical

trials in treating estrogen-receptor-positive and HER2-negative breast cancer. In vitro,

palbociclib, a selective inhibitor of CDK4 and CDK6, was shown to reduce cellular

proliferation of breast cancer cell lines by blocking progression of cells from G1 into S

phase of the cell cycle. While the primary targets of palbociclib have been deciphered, the

molecular mechanisms leading to off-targets effects as well as drug resistance are not

known. To identify new palbociclib protein targets we applied a Cellular Thermal Shift

Assay and a quantitative proteomic analysis (MS-CeTSA) that works under the

assumption that protein-drug interaction stabilises proteins thus, leading to an increase in

thermostability. MCF-7 breast cancer cells were cultured under palbociclib treatment or

DMSO and heated from 37°C to 68°C. Supernatants from 10 different temperatures were

collected for quantitative proteomic analysis using Tandem Mass Tag (TMT-10plex) on an

Orbitrap Fusion Tribrid instrument. The calculated fold changes, as a function of

temperature, follow a sigmoidal trend reflecting the thermal stability of proteins and their

disappearance with increasing temperature.

Large scale proteomic analysis on the Orbitrap Fusion Tribrid instrument allowed the

identification and the quantification of 38,498 peptides corresponding to 5,516 proteins.

As expected, CDK4 and CDK6, the molecular targets of palbociclib were among the 10

most-changing proteins and showed a shift in the temperature (∆tm) of 4.9°C and 3.7°C.

Validation by WB-CeTSA confirmed CDK4/6 stabilisation. Interestingly, classification of

identified protein kinases according to the calculated ∆tm revealed new potential targets of

palbociclib such as CAMK2D, AKT1 and MTOR proteins. Preliminary validation in-vitro

indicated that the MTOR-PI3K signalling pathway may be impaired by the action of

palbociclib. In addition, the MS-CeTSA also revealed a stabilisation of several

proteasomal proteins of the 20S core proteasome through the inhibition of the proteasome-

associated scaffolding protein ECM29. Taken together, these data suggest that off-targets

effects during palbociclib treatment may positively participate in the global response by

blocking tumor progression from G1 into S phase of the cell cycle.

References [1] *Peltier J, *Miettinen T, Härtlova A, Gierliński M, †Björklund M. and †Trost M, Thermal profiling of Breast

cancer cells reveals proteasomal activation by CDK4/6 inhibitor Palbociclib, Nat Commun, Under revision.

Nicolas Autret, PhD

SomaLogic, Ltd.

Regional Manager, Southern Europe

SOMAmers: use of modified aptamers as a new proteomics tool

for unprecedented multiplex assay - the SOMAscan

Even though proteins are the targets of 95% of all known drugs, and downstream of

both genetics and the environment, proteomics has failed to generate even a fraction of the

excitement that drives the genomics revolution. This has been justifiable until now

because large scale, high throughput, highly multiplexed protein measurements have not

been possible.

With the availability of the SOMAscan 1.3k assay, using modified DNA-based

reagents which form highly specific complexes with proteins, we have re-purposed genetic

technologies to measure proteins at unprecedented scale and performance: sub-picogram

simultaneous detection of thousands of proteins with high precision and tiny volumes of

sample.

Examples from cancer, neurological disorders up to cardiovascular diseases will be

shown of how the individual novel reagents as well as the SOMAscan assay are being

used to uncover new biology, validate new targets and deliver actionable information for

medical practice and drug development.

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Séga NDIAYE Life Sciences MS Proteomics Sales Specialist

Chromatography and Mass Spectrometry

Thermo Fisher Scientific.

New innovations implemented on the Q Exactive HF mass

spectrometer.

Orbitrap-based mass spectrometers are increasingly being used for many different

applications. Each application imposes special requirements on the mass spectrometer.

Modern mass spectrometers have improved sensitivity, accuracy, high resolution, and/or

increased scanning speed. These directly result in significant benefits for applications such

as proteomics, environmental and food safety, metabolomics, lipidomics and many more.

Though we have come these far, further technical improvements or next-generation mass

spectrometers are desired by the mass spectrometric community. To further address

existing and new requirements from a broad field of applications, new technological

developments and performance improvements on the existing Thermo Scientific™ Q

Exactive™ HF instrument were undertaken.

We made both hardware and software changes to enhance the performance of the Q

Exactive HF instrument. A brighter ion source interface was realized by replacing the

heated capillary with a modified design with higher throughput, and replacing the S-lens

with an ion funnel for improved ion transmission. To accommodate both changes, the

fore-vacuum system was adapted for higher pumping capacity. Furthermore, the bent

flatapole was modified in order to maintain correct operating pressure and minimize

unwanted solvent cluster formation. Further changes were aimed at reducing the overhead

time between scans.

Tabiwang N. Array; Eugen Damoc; Erik Couzijn; Jens Grote; Oliver Lange; Christian Thoeing; Kerstin

Strupat; Catherina Crone; Anastassios Giannakopulos; Thomas Moehring and Alexander Harder

Thermo Fisher Scientific, Bremen, GERMANY

Julia Chamot-Rooke Mass Spectrometry for Biology Unit

Department of Structural Biology and Chemistry

Institut Pasteur, CNRS

Paris, France

Top-down proteomics: the next step in clinical microbiology. In the last decade, the introduction of MALDI-TOF Mass Spectrometry (MS) for rapid microbial

identification has revolutionized the field of clinical microbiology. The approach has been widely

embraced by hospitals as it is faster, more accurate, and less expensive than conventional

phenotypic or genotypic methods. However, it suffers from important limitations. The

discriminatory power of the technique is insufficient to differentiate closely related bacteria or

sub-species and more importantly resistance and virulence cannot be addressed. There is

therefore a crucial need for innovative analytical approaches allowing an efficient and more

accurate bacterial identification based on protein analysis.

Top-down proteomics is an emerging technology based on the analysis of intact proteins using

very high-resolution mass spectrometry [1]. It provides the highest molecular precision for

analyzing primary structures by examining proteins in their intact state, leading to more

straightforward and reliable results than the classical bottom-up approach based on protein

enzymatic digestion.

Top-down proteomics is particularly suited to the analysis of bacterial proteins, which are of

small size (< 30 kDa) and produced in large amount by bacterial pathogens [2,3].

In order to use top-down proteomics for clinical microbiology applications [4], we set up an

integrated platform in which all steps have been carefully optimized: bacterial lysis, protein

extraction, LC-MS/MS analysis of intact proteins and data processing. For this last point, a new

software tool, which branches from an existing one [5], but tailored towards top-down proteomics

data, has been developed. This new software, based on machine learning, can rapidly cluster the

thousands of MS/MS spectra obtained in top-down LC-MS/MS experiments, compare datasets

obtained from various bacterial pathogens and identify discriminative spectra.

Using this integrated top-down platform, we show that it is now possible to differentiate closely-

related pathogens that are impossible to distinguish with MALDI-TOF MS, in only a few hours

after bacterial culture. We also highlight the great potential of top-down approaches to delineate

complete protein sequences (including C-terminal and N-terminal extremities) and detect single

nucleotide polymorphisms. References

[1] Proteoform: a single term describing protein complexity. L.M. Smith, N. L. Kelleher and the Consortium for

Top-Down Proteomics, Nature Methods (2013).

[2] Posttranslational Modification of Pili upon Cell Contact Triggers N. meningitidis Dissemination. J. Chamot-

Rooke et al., Science, (2011).

[3] Complete posttranslational modification mapping of pathogenic Neisseria meningitidis pilins requires top-down

mass spectrometry. J. Gault et al., Proteomics (2014).

[4] Top-down proteomics in the study of microbial pathogenicity. J. Gault et al. in MALDI-TOF and Tandem MS

for Clinical Microbiology, Wiley (2017).

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Jean Baptiste VINCENDET Life Sciences Holdings France SAS

SCIEX.

High Throughput 1h injection SWATH : Enabling the path to

Personalized Medicine with Industrialized and Integrated Omics.

Enabling industrialized Proteomics makes possible the fast and very reproducible

quantitative and qualitative analysis of 100s of samples. Thus it makes possible to analyze

in a reasonable time frame big patient cohorts and to get the most of them. Additionally,

integrating other omics sciences in the same environment opens the door to a more

comprehensive biology view of the samples.

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Mourad FERHAT, PhD, MBA Promega France.

Product manager, cellular analysis and Proteomics

Overcoming Key Challenges of Protein Mass Spectrometry

Sample Preparation

Bottom-up proteomics is widely accepted as a primary method to characterize

proteins. To ensure efficient protein analysis researchers must optimize key steps in the

workflow to avoid potential pitfalls such as poor protein sample preparation and

inconsistent LC-MS instrument performance. In this presentation, we will:

• Investigate the cause of incomplete trypsin digestion and solution to this problem.

• Discuss the advantage of alternative proteases for mass spec protein analysis.

• Review the impact of mass spec compatible surfactants on protein digestion in gel and

protein extraction from animal tissues.

• Detail new reference mass spec protein and peptide materials designed to optimize

protein sample preparation steps and monitor key instrument performance parameters

The presentation should prove valuable to any researcher using bottom-up proteomics, and

who is concerned with improving protein mass spec sample preparation and mass spec

instrument performance.

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Céline HENRY PAPPSO, Micalis Institute, INRA, AgroParisTech,

Université Paris-Saclay,

78350 Jouy-en-Josas, France

The winning trio in Metaproteomic : 75 cm column, Orbitrap

Fusion™ Lumos™ Tribrid™ and

X !TandemPipeline

Bottom-up approach was fully used in quantitative proteomics strategy. The last

development in shotgun approach was mentioned in the article «The one hour yeast

proteome» (Hebert et al (2014)), in which 3,977 proteins were identified (1,3 hours of run,

35 cm column, Orbitrap Fusion™Tribrid™). This let us to imagine what we could be able

to achieve if we could improve the column size and the time of run with a fast and

sensitive mass spectrometer.

PAPPSO platform works since a long time with complex samples in the Metaproteomic

field, using 50 cm column with sensitive mass spectrometers (Juste, C., et al. (2014)).

Metaproteomic samples are extremely complex and have a particular dynamic range, that

makes the mass spectrometry analysis more difficult than with others samples. Recently

outfitted with an Orbitrap Fusion™ Lumos™ Tribrid™, we have used 75 cm column

(Thermo Scientific) to improve the number of identified peptides while keeping an

acceptable run time.

Different methods of sample preparations with patient heart disease were tested. This new

column allowed us to improve by 30 to 50 % the number of identified proteins.

The results will be discussed with X!TandemPipeline (Langella, O. et al. (2017)), a house

made software and designed to perform protein inference and to manage the redundancy

of peptides identification results after the database search. This software, free and open

source is the only one able to deal with very large raw data sets and huge database,

yielding possible the treatment of hundreds of complex samples in a short time.

A new generation mass spectrometer, a longer column and efficient analysis software have

made available the microbiota analyses of more than 500 patients. This big cohort, allows

us to have a better comprehension of the metabolism among ill individuals in order to

discover future therapeutics targets against metabolic disorders.

17

Sébastien Brier Department of Structural Biology and Chemistry

Mass Spectrometry for Biology Unit, CITECH, CNRS USR

2000,

Institut Pasteur, Paris, France

Probing hydrogen exchange in proteins by mass spectrometry

Hydrogen/Deuterium eXchange measured by Mass Spectrometry (HDX-MS) is a

powerful tool to probe the structure and dynamics of proteins in solution. Significant

improvements in the past decade have resulted in the technology becoming an invaluable

resource in both the academic and pharmaceutical sector. In particular, the implementation

of robotics for sample handling and preparation, and the automation of the labor intensive

data processing step have greatly expedited current HDX-MS strategies.

In this talk, a brief introduction to the technology will be presented, along with the

major advances which have led to the streamline HDX-MS workflow which is

commercially available today. As an example, two applications will be discussed.

Specifically, the use of HDX-MS for both epitope mapping and to probe conformational

changes associated with small ligand binding in a human integral membrane protein will

described in detail.

References [1] Wales T.E, and Engen J.R. Hydrogen exchange mass spectrometry for the analysis of protein

dynamics, Mass Spectrom. Rev., 25(1), 2006: 158-70

[2] Ahn J., and Engen J.R. The use of hydrogen/deuterium exchange mass spectrometry in epitope

mapping, Chemistry Today, 31 (1), 2013: 25-28

[3] Malito E., et al. Defining a protective epitope on factor H binding protein, a key meningococcal

virulence factor and vaccine antigen, PNAS, 110(9), 2013: 3304-09

[4] Canul-Tec J.C., Reda A., et al. Structure and allosteric inhibition of excitatory amino acid transporter

1, Nature, 544, 2017: 446-51

18

Luc Camoin Marseille Protéomique,

Centre de Recherche en Cancérologie de Marseille

INSERM U1068 - CNRS UMR7258 - Aix-Marseille

Université UM105

Marseille, France

Clinical Proteomics: identification of potential biomarkers

The determination of differences in relative protein abundance is a critical aspect of

proteomics research that is increasingly used to answer diverse biological questions.

However, detection of differences between two or more physiological/pathological states

of a biological system is among the most challenging technical tasks in proteomics.

In my lecture I will briefly describe differents quantitative proteomics analysis that we will

develop in different projects associated with cancer research. Firstly, I will discuss how a

serological biomarker may be used for the selection of patients in colorectal cancer (1).

Secondly, I will show how targeted quantitative proteomics can be used to profile breast

cancer tumors to predict the efficacy of targeted therapies (2).

References [1] Guerin M, Gonçalves A, Toiron Y, Baudelet E, Audebert S, Boyer JB, Borg JP, Camoin L. How may

targeted proteomics complement genomic data in breast cancer? Expert Rev Proteomics. 2016 Nov 4; 14:

43-54

[2] Peltier J, Roperch JP, Audebert S, Borg JP, Camoin L. Quantitative proteomic analysis exploring

progression of colorectal cancer: Modulation of the serpin family. J Proteomics. 2016 Aug 2;148: 139-

148

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Thibaut Léger Institut Jacques Monod, UMR7592

Université Paris Diderot/CNRS,

Sorbonne Paris Cité, FRANCE

The metacaspase Mca1p as a link between proteolysis, apoptosis

and glycosylation in the human pathogenic yeast Candida albicans

Candida albicans is a commensal fungus of the gut flora, mucous and epithelia and an

opportunistic human pathogen causing benign infections, such as oral or genital

candidiasis, and more severe life-threatening systemic infections, particularly in

immunocompromised patients. An understanding of the pathways giving rise to cell death

is required, to improve our comprehension and control of the process of apoptosis in this

pathogen. The metacaspase Mca1p has been described as a key protease for apoptosis in

C. albicans but little is known about its cleavage specificity and substrates. To

characterize its functions, we subjected wild-type and mca1-deletion strains to the quorum

sensing molecule farnesol and then studied the early phase of apoptosis release in

innovative quantitative proteomics, glycoproteomics and glycomics experiments. The

combination of the deletion and the farnesol molecule led to the strong overexpression of

proteins implicated in the general stress. We found the Mca1p cleavage specificity “K/R”

in P1 and D/E in P2 and identified 57 potential substrates of Mca1p, implicated in protein

folding, protein aggregate resolubilization, glycolysis, glycosylation machinery and a

number of mitochondrial functions. By several glycoproteomics approaches, we identified

76 glycosylations (17 N- and 58 O-glycosylations), 100 sites of N-glycosylations and we

showed a general increase in the O-glycosylation of proteins in the deleted strains treated

with farnesol. Our findings highlight new roles of the metacaspase in amplifying cell death

processes by degrading several major Heat Shock Proteins, by contributing significantly to

the control of mitochondria biogenesis and degradation, by affecting several critical

protein quality control systems and altering the protein glycosylation machinery. These

findings open up unexpected new possibilities for developing targeted inhibitors of C.

albicans growth.

References 1. Leger T. et al. The Metacaspase (Mca1p) Restricts O-glycosylation During Farnesol-induced

Apoptosis in Candida albicans. Molecular & cellular proteomics (2016): MCP 15, 2308-2323

2. Leger T. et al. Label-Free Quantitative Proteomics in Yeast. Methods Mol Biol (2016) 1361, 289-307

3. Leger T. et al. The metacaspase (Mca1p) has a dual role in farnesol-induced apoptosis in Candida

albicans. Molecular & cellular proteomics (2015): MCP 14, 93-108

20

Anaïs Baudot I2M,

AMU-CNRS,

Marseille, France

Bioinformatics and interactome in proteomics, application to

prostate cancer cell lines

Networks, in which the nodes represent proteins, and the edges different categories of

interactions, are widely used in proteomics. They are useful for instance to visualize

discovered physical interactions by drawing interactome data. They can also picture

functional interactions, derived from other –omics data, such as gene or protein

expression. Finally, they can be used to integrate different type of large-scale data, such as

proteomics and phosphoproteomics. In any cases, the obtained networks are large and

complex, and call for the development of new tools and approaches to extract the

functional knowledge they contain [1-3].

Following the interactomics [4], proteomics and phosphoproteomics data we have

generated to study prostate cancer cell lines and their resistance behaviors, I will present

different application of these network-based bioinformatics approaches.

References [1] Spinelli L, Gambette P, Chapple CE, Robisson B, Baudot A, Garreta H, Tichit L, Guénoche A, Brun

C (2013) Clust&See: A Cytoscape plugin for the identification, visualization and manipulation of

network clusters. BioSystems 113: 91–95.

[2] Didier G, Brun C, Baudot A (2015) Identifying Communities from Multiplex Biological Networks.

PeerJ 3: 1–9.

[3] Valdeolivas A, Tichit L, Navarro C, Perrin S, Odelin G, Levy N, Cau P, Remy E, Baudot A (2017)

Random Walk With Restart On Multiplex And Heterogeneous Biological Networks. bioRxiv.

[4] Katsogiannou et al. (2014) The Functional Landscape of Hsp27 Reveals New Cellular Processes such

as DNA Repair and Alternative Splicing and Proposes Novel Anticancer Targets. Mol Cell Proteomics

13: 3585–3601.

21

Angéline KERNALLÉGUEN Inserm, CRO2, UMR_S 911, PIT2,

Faculty of Pharmacy,

Marseille, France

Drugs distribution profile in the hair by MALDI imaging

Already widely demonstrated, hair strands analysis documents punctual or regular

consumption of drugs of abuse (DOA). With the introduction of the Matrix Assisted Laser

Desorption Ionization mass spectrometry (MALDI), new opportunities appear, such as

high-throughput profiling and drugs monitoring [1]. Mass spectrometry imaging (MSI)

coupled to MALDI offers the unique possibility to map with high spatial resolution several

tens of species into only one intact hair [2–4]. Current conventional and destructive

methods (GC-MS, LC-MS) usually require a great amount of hair samples to ensure the

identification of various DOA families, which is not compatible with low hair availability

case.

In this presentation, a brief introduction to the MALDI technology will be done, followed

to a discussion on the pitfalls to avoid in hair samples preparation. To conclude, several

drugs distribution profiles by MALDI imaging in various MS stage will be discussed.

References [1] Vogliardi S, Favretto D, Frison G, Maietti S, Viel G, Seraglia R, et al. Validation of a fast screening

method for the detection of cocaine in hair by MALDI-MS. Anal Bioanal Chem. (2010); 396(7):2435–40.

[2] Poetzsch M, Steuer AE, Roemmelt AT, Baumgartner MR, Kraemer T. Single Hair Analysis of Small

Molecules Using MALDI-Triple Quadrupole MS Imaging and LC-MS/MS: Investigations on

Opportunities and Pitfalls. Anal Chem. (2014); 86 (23):11758–65.

[3] Kamata T, Shima N, Sasaki K, Matsuta S, Takei S, Katagi M, et al. Time-Course Mass Spectrometry

Imaging for Depicting Drug Incorporation into Hair. Anal Chem. (2015); 87(11):5476–81.

[4] Beasley E, Francese S, Bassindale T. Detection and Mapping of Cannabinoids in Single Hair Samples

through Rapid Derivatization and Matrix-Assisted Laser Desorption Ionization Mass Spectrometry. Anal

Chem. (2016); 88(20):10328–34.

ABOUSERHALDAOU Pascale Thermofisher scientific Pascale.AbouSerhalDaou@thermofisher.com ALMERAS Lionel IRBA almeras.lionel@gmail.com AUDEBERT Stéphane - Intervenant CRCM-MaP stephane.audebert@inserm.fr AUTRET Nicolas - Intervenant SOMALOGIC nautret@somalogic.com BAUDOT Anaïs - Intervenante I2M anais.baudot@univ-amu.fr BEBIEN-LAWRENCE Magali CIML bebien@ciml.univ-mrs.fr BELGHAZI Maya CRN2M-MaP maya.belghazi@univ-amu.fr BIRG Françoise CRCM francoise.birg@inserm.fr BOUGIS Pierre CRN2M-MaP pierre-edouard.bougis@univ-amu.fr BRES Anne-Sophie GE Healthcare Anne-Sophie.Bres@ge.com

BRIER Sébastien - Intervenant Institut Pasteur sebastien.brier@pasteur.fr BROUSSE Carine CRCM-TrGET carine.brousse@inserm.fr BRUSCHI Mireille IMM-CNRS bruschi@imm.cnrs.fr BUHOT-ROCHE Blandine GE Healthcare blandine.Buhot-roche@ge.com CABANTOUS Sandrine INSERM sandrine.ambard@univ-amu.fr CAMOIN Luc - Intervenant CRCM-MaP luc.camoin@inserm.fr CAU Pierre ProGeLife pierre.cau@univ-amu.fr CHAMOT ROOKE Julia - Intervenante Institut Pasteur julia.chamot-rooke@pasteur.fr CSATETS Francis IBDM francis.castets@univ-amu.fr DAULAT Avais CRCM avais.daulat@inserm.fr

Liste des participants

PROTEOPACA 2017

22

DESCHANEL Louis Thermofisher scientific louis.deschanel@thermofisher.com DE SEPULVEDA Paulo CRCM sepulveda@inserm.fr DEBAYLE Delphine IPMC debayle@ipmc.cnrs.fr DUBOIS Cécile IRSN cecile.dubois@irsn.fr EL KOULALI Khadija CRCM khadija.elkoulali@inserm.fr FERHAT Mourad - Intervenant PROMEGA mourad.ferhat@promega.com FERRACCI Geraldine CRN2M-MaP geraldine.ferracci@univ-amu.fr FOURQUET Patrick CRCM-MaP patrick.fourquet@inserm.fr FRELON Sandrine IRSN sandrine.frelon@irsn.fr GAUTHIER Laurent INNATE PHARMA laurent.gauthier@innate-pharma.fr GAY Anne-Sophie IPMC-CNRS gay@ipmc.cnrs.fr GONTERO MEUNIER Brigitte BIP2-MaP bmeunier@imm.cnrs.fr

GRANJEAUD Samuel CRCM-MaP samuel.granjeaud@inserm.fr GUERIN Mathilde CRCM-MaP mathilde.guerin@inserm.fr GUIGONIS Jean-Marie Faculté de Médecine Nice guigonis@unice.fr HENRY Céline - Intervenante PAPPSO celine.henry@inra.fr HUTINEL Olivier ABSciex olivier.hutinel@absciex.com IMBERT Isabelle CNRS AFMB isabelle.imbert@afmb.univ-mrs.fr JHUMKA Anissa IBDM jhumka.anissa@gmail.com KELLER Lionel Thermo Fisher Scientific lionel.keller@thermofisher.com KERNALLEGUEN Angéline - Intervenante FACULTE PHARMACIE PIT2-MaP angeline.kernalleguen@hotmail.fr KHANTANE Sabrina Thermofisher scientific sabrina.khantane@thermofisher.com KUZMIC Mira IRSN mira.kuzmic@gmail.com LAN Wenjun CRCM wenjun.lan@inserm.fr

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LEBRUN Régine IMM-MaP rlebrun@imm.cnrs.fr LEE Lara CRCM lara.lee@inserm.fr LEGER Thibaut - Intervenant Institut Jacques Monod thibaut.leger@ijm.fr LEGOUPIL Thierry SHIMADZU tl@shimadzu.fr LELLOUCH Anne-marie IBDM annemarie.lellouch@univ-amu.fr LEQUEUE Charlotte CRCM charlotte.lequeue@inserm.fr LLOUBES roland IMM-CNRS roland.lloubes@imm.cnrs.fr LOPEZ Sophie CRCM sophie.lopez@inserm.fr MAGLIANO Marc INRA marc.magliano@inra.fr MALAPERT Pascale IBDM pascale.malapert@univ-amu.fr MANSUELLE Pascal IMM-MaP pascal.mansuelle@imm.cnrs.fr MAO Qiyan IBDM qiyan.mao@univ-amu.fr

MARFISI Claude Bruker claude.marfisi@bruker.com MASSEY-HARROCHE Dominique IBDM dominique.massey-harroche@univ-amu.fr MEHUL Bruno GALDERMA bruno.mehul@galderma.com MIGNOT Florian PROMEGA France florian.mignot@promega.com MOAL Stéphane Cell Signaling stephane.moal@cellsignal.com MONDIELLI Grégoire CRN2M gregoire.mondielli@univ-amu.fr MOQRICH Aziz IBDM aziz.moqrich@univ-amu.fr NDIAYE Séga – Intervenant Thermofisher scientific sega.ndiaye@thermofisher.com NORMANNO Davide CRCM davide.normanno@inserm.fr NUCCIO Christopher FACULTE PHARMACIE PIT2 christopher.nuccio@univ-amu.fr OUNOUGHENE Youcef CIML ounoughene@ciml.univ-mrs.fr PASQUIER Eddy CRCM eddy.pasquier@inserm.fr

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PELTIER Julien - Intervenant Newcastle University julien.peltier@ncl.ac.uk PICLIN Nadége GE Healthcare Nadege.piclin@ge.com POPHILLAT Matthieu CRCM-MaP matthieu.pophillat@inserm.fr POPOVIC Luksa CRCM luksa.popovic@inserm.fr PYR dit Ruys Sébastien IRSN sebastien.pyrditruys@hotmail.com RESCH Sylvain SHIMADZU sr@shimadzu.fr RISSO-MOREAU DE FAVE Christine UCAPolytech Nice-Sophia christine.risso@unice.fr ROCCHI Palma CRCM palma.rocchi@inserm.fr ROSSI Benjamin INNATE PHARMA benjamin.rossi@innate-pharma.fr RUMINSKI Kilian CIML ruminski@ciml.univ-mrs.fr SANTOS Catarina IBDM catarina.de-pais-paiva-santos@univ-amu.fr SAVARD-CHAMBARD GAS Sandra INNATE PHARMA sandra.savard-chambard-gas@innate-pharma.fr 25

SCHEMBRI Thérèse FACULTE PHARMACIE PIT2 therese.schembri@univ-amu.fr SEASSAU Aurelie INRA PACA aurelie.seassau@inra.fr SEBBAGH Michael CRCM michael.sebbagh@inserm.fr SILVIERA de MORAIS Ana Theresa AFMB Lab, Polytech ana-theresa.morais@afmb.univ-mrs.fr SILVEIRA WAGNER Monica CRCM monica.silveira-wagner@inserm.fr TERRAL Guillaume INNATE PHARMA guillaume.terral@innate-pharma.fr TINLAND Marie-France CRCM TOIRON YVES IPC/CRCM-MaP yves.toiron@inserm.fr VILLARD claude UMR INSERM 911 claude.villard@univ-amu.fr VINCENDET Jean-Baptiste - Intervenant ABSciex jean-baptiste.vincendet@absciex.com

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PROTEOPACA 2017

Organisation

Plateforme protéomique CRCM-IPC

Directeur Jean-Paul Borg

Comité local d’organisation :

Audebert Stéphane

Borg Jean-Paul Camoin Luc

Fourquet Patrick Granjeaud Samuel Pophillat Matthieu

Avec le soutien de Michel Baccini; Françoise Birg; François Coulier; Valérie Depraetère; Laurence Duvivier; Amandine Gazull; Laurence

Laloum; Claude Roux; Marie-France Tinland et Patrice Viens.

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PROTEOPACA 2017