Laboratory of Pathogens and Host Immunity

Mini-bio – Laure Yatime

YATIME LAURE

POSITION

INSERM Researcher (CRCN), PhD, HDR

Team “Immunity, Inflammation and Bacterial Virulence” 

Group “Danger signals and chronic inflammation“

CONTACT

E-mail: laure.yatime[at]inserm.fr

Phone: +33 (0)4 67 14 92 03 

BIOGRAPHY

Dr. Laure Yatime has a background training in chemical engineering (Chimie ParisTech). Attracted very early by science at the interface between chemistry and biology, she joined the Laboratory of Biochemistry at Ecole Polytechnique to do her PhD thesis on translation initiation in Eukarya and Archaea. After graduating in 2005, Dr. Yatime joined the group of Prof. Poul Nissen at Aarhus University in Denmark as a post-doctoral fellow. Her work led to the structural characterization of the recognition mode of cardiotonic steroids by the sodium-potassium pump, opening up possibilities to develop more efficient and less toxic cardiotonic compounds in the future. In 2010, she was appointed as a senior adviser in the group of Prof. Gregers Rom Andersen at Aarhus University to develop structure-based approaches to selectively target the Complement system in an inflammatory context. Since 2010, Dr. Yatime’s research has been focused on specific receptors from the innate immune system and their involvement in inflammatory processes through the recognition of damage-associated molecular patterns. In 2013, she started an independent research project at Aarhus University on the receptors for S100 proteins involved in inflammation during cancer. She moved back to France in 2016 where she obtained a permanent position as an Inserm CRCN researcher at University of Montpellier. She is now co-leading the team “Immunity, Inflammation & Bacterial Virulence”, together with Dr. Georges Lutfalla and Dr. Mai Nguyen-Chi, in the Laboratory of Pathogens and Host Immunity (LPHI). Within the team, she heads the group “Danger signals and chronic inflammation” which aims to investigate the biology of S100 alarmins in health and disease as well as the virulence mechanisms of adherent invasive Escherichia coli during Crohn’s disease, using multi-scale approaches ranging from structural biology and biochemistry to in vivo modeling in the zebrafish model, with the goal to develop novel anti-inflammatory drugs applicable in infectious and inflammatory diseases.

PUBLICATIONS

Paris T, Kiss A, Signor L, Lutfalla G, Blaise M, Boeri-Erba E, Chaloin L, Yatime L (2023) The IbeA protein from Adherent-Invasive Escherichia coli is a flavoprotein displaying structural homology with FAD-dependent oxidoreductases. FEBS J. Online ahead of print. doi:10.1111/febs.16969

Leiba J, Ozbilgic R, Hernandez L, Demou M, Lutfalla G, #Yatime L, #Nguyen Chi M (2023) Molecular actors of inflammation and their signaling pathways: mechanistic insights from zebrafish. Biology 12, 153. doi: 10.3390/biology12020153 #Co-last authors

Paris T, Yatime L (2022) Les CEACAM épithéliales, plateformes d’ancrage des microorganismes pathogènes dans les muqueuses. Med Sci 38, 650-653. doi: 10.1051/medsci/2022097

Kowalewski J, Paris T, Gonzalez C, Lelièvre L, Castaño Valencia L, Boutrois M, Augier C, Lutfalla G, Yatime L (2021) Characterization of a member of the CEACAM protein family as a novel marker of proton pump-rich ionocytes on the zebrafish epidermis. PLoS ONE 16, e0254533. doi:10.1371/journal.pone.0254533

Signor L, Paris T, Mas C, Picard A, Lutfalla G, Bori-Erba E, Yatime L (2021) Divalent cations influence the dimerization mode of murine S100A9 protein by modulating its disulfide bond pattern. J Struct Biol 213:107689. doi:10.1016/j.jsb.2020.107689

May O, Yatime L, Merle NS, Delguste F, Howsam M, Daugan M, Constant CP, Billamboz M, Ghinet A, Lancel S, Dimitrov JD, Boulanger E, Roumenina LT, Frimat M (2020) The receptor for advanced glycation end products is a sensor for cell-free heme. FEBS J 288, 3448-3464. doi:10.1111/febs.15667

Yatime L (2019) Structural analysis of S100A8 complex with zinc and calcium: a general protocol for the study of S100 proteins in the presence of divalent cations by X-ray crystallography. In C. Heizmann (eds.), Calcium-Binding Proteins of the EF-Hand Superfamily (pp. 417-435). Methods in Molecular Biology, vol. 1929, Humana Press, New York, NY. doi:10.1007/978-1-4939-9030-6_26

Yatime L, Merle NS, Hansen AG, Friis NA, Østergaard JA, Bjerre M, Roumenina LT, Thiel S, Kristensen P, Andersen GR (2018) A single-domain antibody targeting complement component C5 acts as a selective inhibitor of the terminal pathway of the complement system and thus functionally mimicks the C-terminal domain of the Staphylococcus aureus SSL7 protein. Front Immunol 9:2822. doi:10.3389/fimmu.2018.02822

Yatime L (2017) A cystein-dependent activation mechanism for the pro-inflammatory ligands of RAGE? Med Sci 33, 351-354. doi:10.1051/medsci/20173303026

Yatime L, Betzer C, Jensen RK, Mortensen S, Jensen PH, Andersen GR (2016) The structure of the RAGE:S100A6 complex reveals a new mode of homodimerization for S100 proteins. Structure 24, 2043-2052. doi:10.1016/j.str.2016.09.011

Lin H, Andersen GR, Yatime L(2016) Crystal structure of human S100A8 in complex with zinc and calcium. BMC Struct Biol 16:8. doi:10.1186/s12900-016-0058-4

Yatime L, Bajic G, Schatz-Jakobsen JA, Andersen GR (2016) Complement regulators and inhibitors in health and disease: a structural perspective. In K.A. Howard, T. Vorup-Jensen and D. Peer (eds.), Nanomedicine (pp. 13-42). CRS Book Series Advances in Delivery Science and Technology, Springer-Verlag New York. doi:10.1007/978-1-4939-3634-2_2

Yatime L, Maasch C, Hoehlig K, Klussmann S, Andersen GR, Vater A (2015) Structural basis for the inhibition of complement anaphylatoxin C5a using a mixed L-RNA/L-DNA aptamer. Nat Commun 6:6481. doi:10.1038/ncomms7481

Laursen M, Gregersen JL, Yatime L, Nissen P, Fedosova NU (2015) Structures and characterization of digoxin- and bufalin-bound Na+,K+-ATPase compared to the ouabain-bound complex. Proc Natl Acad Sci USA 112, 1755-1760. doi:10.1073/pnas.1422997112

Schatz-Jacobsen JA, Yatime L, Larsen C, Petersen SV, Klos A, Andersen GR (2014) Structural and functional characterization of human and murine C5a anaphylatoxins. Acta Cryst D70, 1704-1717. doi:10.1107/S139900471400844X

 

Yatime L, Andersen GR (2014) The specificity of DNA recognition by the RAGE receptor. J Exp Med 211, 749-750. doi:10.1084/jem.20132526

Yatime L, Andersen GR (2013) Structural insights into the oligomerization mode of the human Receptor for Advanced Glycation End-products (RAGE). FEBS J 280, 6556-6568. doi:10.1111/febs.12556

Bajic G, Yatime L, Sim RB, Vorup-Jensen T, Andersen GR (2013) Structural insight on the recognition of surface-bound opsonins by the integrin I-domain of complement receptor 3. Proc Natl Acad Sci USA 110, 16426-16431. doi:10.1073/pnas.1311261110

Laursen M, Yatime L, Nissen P, Fedosova NU (2013) Crystal structure of the high-affinity Na+,K+-ATPase – ouabain complex with Mg2+ bound in the cation binding site. Proc Natl Acad Sci USA 110, 10958-10963. doi:10.1073/pnas.1222308110

Bajic G, Yatime L, Klos A, Andersen GR (2013) Human C3a and C3a desArg anaphylatoxins have conserved structures, in contrast to C5a and C5a desArg. Protein Sci 22, 204-212. doi:10.1002/pro.2200

Kidmose RT, Laursen NS, Dobó J, Kjaer TR, Sirotkina S, Yatime L, Sottrup-Jensen L, Thiel S, Gál P, Andersen GR (2012) Structural basis for activation of the complement system by component C4 cleavage. Proc Natl Acad Sci USA 109, 15425-15430. doi:10.1073/pnas.1208031109

Yatime L, Hein KL, Nilsson J, Nissen P (2011) Structure of the RACK1 dimer from Saccharomyces cerevisiae. J Mol Biol 411, 486-498. doi:10.1016/j.jmb.2011.06.017

Gourdon P, Andersen JL, Hein KL, Bublitz M, Pedersen BP, Liu XY, Yatime L, Nyblom M, Nielsen TT, Olesen C, Møller JV, Nissen P, Morth JP (2011) HiLiDe – Systematic Approach to Membrane Protein Crystallization in Lipid and Detergent. Crystal Growth & Design 11, 2098-2106. doi:10.1021/cg101360d

Yatime L, Laursen M, Morth JP, Esmann M, Nissen P, Fedosova NU (2011) Structural insights into the high affinity binding of cardiotonic steroids to the Na,K-ATPase. J Struct Biol 174, 296-306. doi:10.1016/j.jsb.2010.12.004

Yatime L, Buch-Pedersen MJ, Musgaard M, Morth JP, Lund Winther AM, Pedersen BP, Olesen C, Andersen JP, Vilsen B, Schiøtt B, Palmgren MG, Møller JV, Nissen P, Fedosova N (2009) P-type ATPases as drug targets: tools for medicine and science. Biochim Biophys Acta 1787, 207-220. Review. doi:10.1016/j.bbabio.2008.12.019

Yatime L, Mechulam Y, Blanquet S, Schmitt E (2007) Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states. Proc Natl Acad Sci USA 104, 18445-18450. doi:10.1073/pnas.0706784104

Mechulam Y, Guillon L, Yatime L, Blanquet S, Schmitt E (2007) Protection-based assays to measure aminoacyl-tRNA binding to translation initiation factors. Methods Enzymol 430, 265-281. doi:10.1016/S0076-6879(07)30011-6

Yatime L, Mechulam Y, Blanquet S, Schmitt E (2006) Structural switch of the g subunit in an archaeal aIF2ag heterodimer. Structure 14, 119-128. doi:10.1016/j.str.2005.09.020

Yatime L, Schmitt E, Blanquet S, Mechulam Y (2005) Structure-function relationships of the intact aIF2a subunit from the archaeon Pyrococcus abyssi. Biochemistry 44, 8749-8756. doi:10.1021/bi050373i

Yatime L, Schmitt E, Blanquet S, Mechulam Y (2004) Functional molecular mapping of archaeal translation initiation factor 2. J Biol Chem 279, 15984-15993. doi:10.1074/jbc.M311561200