{"id":713,"date":"2014-02-14T15:06:00","date_gmt":"2014-02-14T14:06:00","guid":{"rendered":"https:\/\/www.egce.universite-paris-saclay.fr\/?p=713"},"modified":"2025-04-10T16:26:26","modified_gmt":"2025-04-10T14:26:26","slug":"jean-luc-da-lage","status":"publish","type":"post","link":"https:\/\/www.egce.universite-paris-saclay.fr\/?p=713","title":{"rendered":"Jean-Luc Da Lage"},"content":{"rendered":"

\"da-lage\"
\nMembre du p\u00f4le G\u00e9nomes<\/strong>
\nCharg\u00e9 de recherches CNRS
\nDoctorat Universit\u00e9 Paris VII (1990), HDR (2003)<\/p>\n

\"1397745702_aiga_telephone\"<\/a> +33 (0)1 69 15 49 72
\n\"1397745614_print\"<\/a>
\n\"1397745633_aiga_mail\"<\/a> Jean-Luc.Da-Lage[@]universite-paris-saclay.fr<\/p>\n

Th\u00e8mes de Recherche<\/h2>\n

<\/h3>\n

Evolution mol\u00e9culaire des g\u00e8nes et de la prot\u00e9ine d’alpha-amylase chez les m\u00e9tazoaires. Evolution fonctionnelle de l’enzyme, duplications et famille multig\u00e9nique, origine et \u00e9volution des introns, transferts horizontaux.<\/p>\n

L’alpha-amylase est une des enzymes majeures du m\u00e9tabolisme de la nutrition. Elle permet l’hydrolyse de l’amidon et d’autres substrats comme le glycog\u00e8ne, en mol\u00e9cules plus simples (maltose, maltotriose, maltodextrines). Elle est pr\u00e9sente dans l’ensemble du monde vivant, Bact\u00e9ries, Archae, Plantes, Champignons, Animaux.<\/p>\n

Chez de tr\u00e8s nombreux organismes, on a constat\u00e9 que le g\u00e8ne codant cette prot\u00e9ine existe en plusieurs copies, et ces duplications peuvent intervenir de fa\u00e7on ind\u00e9pendante, m\u00eame dans des lign\u00e9es \u00e9volutivement proches. Nous cherchons \u00e0 comprendre la signification \u00e9volutive de cette tendance \u00e0 la multiplicit\u00e9 des copies, au regard de la fonction de l’enzyme, et de la divergence des g\u00e8nes dans leur s\u00e9quence et leur profil d’expression (sp\u00e9cificit\u00e9 tissulaire et temporelle de la production d’amylase).<\/p>\n

Certaines esp\u00e8ces peuvent servir de mod\u00e8le dans cette \u00e9tude. C’est le cas de Drosophila ananassae, chez qui on a clon\u00e9 7 g\u00e8nes, plus ou moins divergents entre eux, localis\u00e9s sur plusieurs chromosomes et ayant des profils d’expression diff\u00e9rents. La structure intron\/exon peut varier non seulement entre esp\u00e8ces mais aussi entre copies d’une m\u00eame esp\u00e8ce. Cela nous a conduit \u00e0 nous int\u00e9resser \u00e0 l’histoire \u00e9volutive de la structure de ce g\u00e8ne chez les Animaux, et plus g\u00e9n\u00e9ralement \u00e0 la dynamique des introns.<\/p>\n

Nous nous int\u00e9ressons aussi \u00e0 l’\u00e9volution de la prot\u00e9ine alpha-amylase elle-m\u00eame et \u00e0 son adaptation. Pour cela, nous avons recherch\u00e9 des motifs prot\u00e9iques ou des r\u00e9sidus dont les variations dans le r\u00e8gne animal peuvent indiquer un r\u00f4le adaptatif, et en quoi peut consister cette adaptation. Apr\u00e8s avoir rep\u00e9r\u00e9 quelques motifs d’int\u00e9r\u00eat, nous tentons une approche fonctionnelle, en produisant in vitro une amylase-t\u00e9moin, puis des variants reproduisant les variations observ\u00e9es de fa\u00e7on r\u00e9currente dans la nature. La comparaison devrait permettre de cerner le caract\u00e8re adaptatif de ces variations<\/p>\n

Le g\u00e8ne Amyrel,<\/em> paralogue de l’amylase chez les Dipt\u00e8res Muscomorphes, pr\u00e9sente un tr\u00e8s bon signal phylog\u00e9n\u00e9tique et biog\u00e9ographique. Il peut donc \u00eatre utilis\u00e9 pour reconstruire la phylog\u00e9nie des Drosophiles mais aussi en g\u00e9n\u00e9tique des populations. Nous l’avons utilis\u00e9 pour produire une phylog\u00e9nie mol\u00e9culaire comprenant plus de 165 esp\u00e8ces de drosophiles. La fonction de la prot\u00e9ine Amyrel demeure inconnue. Nous \u00e9tudions ses propri\u00e9t\u00e9s et son expression chez les drosophiles.<\/p>\n

\n

Publications<\/h2>\n<\/div>\n

GUILLAUME J. B., DA LAGE J.-L.<\/strong>, MEZDOUR S., MARION-POLL F., TERROL C., BROUZES C. M. C., SCHMIDELY P. (2024)<\/strong>. Amylase activity across black soldier fly larvae development and feeding substrates: insights on starch digestibility and external digestion. Animal, <\/em>18 (11)\u00a0: 101337. https:\/\/doi.org\/10.1016\/j.animal.2024.101337<\/a><\/p>\n

DA LAGE J.-L.<\/strong>, FONTENELLE A., FIL\u00c9E J., MERLE M., B\u00c9RANGER J.-M., ALMEIDA C. E., FOLLY RAMOS E., and HARRY M. <\/em>(2024)<\/strong>. <\/em>Evidence that hematophagous triatomine bugs may eat plants in the wild. Insect Biochem. Mol. Biol.,<\/em> 165:104059. doi.org\/10.1016\/j.ibmb.2023.104059.<\/em><\/p>\n

RHIMI M., DA LAGE J.-L<\/strong>., HASER R., FELLER G. and AGHAJARI N. (2023)<\/strong>. Structural and functional characterization of Drosophila melanogaster<\/em> \u03b1-amylase. Molecules<\/em>, 28 (14) :5327. doi.org\/10.3390\/molecules28145327.<\/p>\n

\n

\"iconePdf\"<\/a> FELLER G., BONNEAU M. and DA LAGE, J.-L. (2021)<\/strong>. Amyrel, a novel glucose-forming \u03b1-amylase from Drosophila<\/em> with 4-\u03b1-glucanotransferase activity by disproportionation and hydrolysis of maltooligosaccharides. Glycobiology<\/em>. 31 (9):1134-1144. doi: 10.1093\/glycob\/cwab036.<\/span><\/p>\n

\"iconePdf\"<\/a> MULLER H., OGEREAU D., DA LAGE J.-L<\/strong>., CAPDEVIELLE C., POLLET N., FORTUNA T., JEANNETTE R., KAISER L. and GILBERT C. (2021)<\/strong>. Draft genome of the Mediterranean corn borer, Sesamia nonagrioides<\/em>, a major pest of maize. Genes, Genomes, Genetics<\/em>. 11(7):jkab155. doi: <\/span><\/span> 10.1093\/g3journal\/jkab155.<\/p>\n

BICHANG’A G. B., DA LAGE J.-L<\/strong>., SAMBAI K., MULE S., LE RU B., KAISER L., JUMA G., MAINA, E. N. and CALATAYUD P.-A. (2020)<\/strong>. Salivary \u03b1-amylase of stem borer hosts determines host recognition and acceptance for oviposition by Cotesia<\/em> spp. (Hymenoptera, Braconidae). In\u00a0: Calatayud, P.-A., Clarke, C. W., Sforza, R. F. H., Ndemah, R. N., Nyamukondiwa, C., eds. (2020). Parasitoids\u2019 Ecology and Evolution. Lausanne: Frontiers Media SA. doi: 10.3389\/978-2-88963-480-4.<\/p>\n

\"iconePdf\"<\/a>DESIDERATO A., BARBEITOS M., GILBERT C. and DA LAGE J.-L.<\/strong> (2020)<\/strong>. Horizontal transfer and gene loss shaped the evolution of alpha-amylases in bilaterians. Genes, Genomes, Genetics<\/em>. 10<\/strong>(2):709-719.<\/p>\n

\"iconePdf\"<\/a><\/strong>DA LAGE J.-L.<\/strong>, THOMAS G. W. C., BONNEAU M. and COURTIER-ORGOGOZO V. (2019)<\/strong>. Evolution of salivary glue genes in Drosophila<\/em> species. BMC Evol. Biol<\/em>. 19\u00a0:36. doi.org\/10.1186\/s12862-019-1364-9.<\/p>\n

\"iconePdf\"<\/a><\/strong>BICHANG’A G., DA LAGE J.-L.<\/strong>, SAMBAI K., MULE S., LE RU B., KAISER-ARNAULD L., JUMA G., MAINA E. N. and CALATAYUD P.-A. (2018)<\/strong>. Salivary \u03b1-amylase of stem borer hosts determines host recognition and acceptance for oviposition by Cotesia<\/em> spp. (Hymenoptera, Braconidae). Front. Ecol. Evol.<\/em> 6\u00a0: doi: 10.3389\/fevo.2018.00228.<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L.<\/strong> (2018)<\/strong> The amylases of insects. Int. J. Insect Sci.<\/i> 10:1-14<\/p>\n

\"iconePdf\"<\/a><\/strong>BICHANG’A G., DA LAGE J-L.<\/strong>, CAPDEVIELLE-DULAC C., ZIVY M., BALLIAU T., SAMBAI K., LE RU B., KAISER-ARNAULD L., JUMA G., NJOKI MWANGI MAINA E., and CALATAYUD P.-A. (2018)<\/strong> \u03b1-Amylase Mediates Host Acceptance in the Braconid Parasitoid Cotesia flavipes<\/i>. J. Chem Ecol.<\/i> 44 (11) :1030-1039.<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L.<\/strong> (2017)<\/strong> An optional C-terminal domain is ancestral in \u03b1-amylases of bilaterian animals. Amylase <\/em> 1:24-36<\/p>\n

\"iconePdf\"<\/a> CLAISSE G., FELLER G., BONNEAU M., DA LAGE J-L.<\/strong> (2016)<\/strong> A single amino-acid substitution toggles chloride dependence of the alpha-amylase paralog amyrel in Drosophila melanogaster<\/i> and Drosophila virilis <\/i> species. Insect Biochem. Mol. Biol. <\/em> 75:70-77<\/p>\n

\"iconePdf\"<\/a> COMMIN C., AUMONT-NICAISE M., CLAISSE G., FELLER G., DA LAGE J-L.<\/strong> (2013)<\/strong> Enzymatic characterization of recombinant \u03b1-amylase in the Drosophila melanogaster<\/em> species subgroup: is there an effect of specialization on digestive enzyme? Genes Genet. Sys. <\/em> 88:251-259<\/p>\n

\"iconePdf\"<\/a> DA LAGE J.-L.<\/strong>, BINDER M., HUA VAN A., JANECEK S., CASANE D. (2013)<\/strong> Gene make-up: rapid and massive intron gains after horizontal transfer of a bacterial alpha-amylase gene to Basidiomycetes. BMC Evol. Biol. <\/em> 13: 40<\/p>\n

\"iconePdf\"<\/a> CHAUMOT A., DA LAGE J-L.<\/strong>, MAESTRO O., MARTIN D., IWEMA T., BRUNET F., BELLES X., LAUDET V., BONNETON F. ( 2012)<\/strong> Molecular adaptation and resilience of the insect’s nuclear receptor USP. BMC Evol. Biol.<\/em> 12: 199<\/p>\n

\"iconePdf\"<\/a> CIPOLLA A., DELBRASSINE F., DA LAGE J-L.<\/strong>, FELLER G. (2012)<\/strong> Temperature adaptation in psychrophilic, mesophilic and thermophilic chloride-dependent alpha-amylases. Biochimie<\/em> 94(9): 1943-1950<\/p>\n

\"iconePdf\"<\/a>FELLER G., DEHARENG D., DA LAGE J-L. (2011)<\/strong> How to remain non-folded and pliable: the linkers in modular alpha-amylases as a case study. FEBS J.<\/em> 278: 2333. doi: 10.1111\/j.1742-4658.2011.08154.x.<\/span><\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L.<\/strong>, MACZKOWIAK F. , CARIOU M-L. (2011)<\/strong> Phylogenetic distribution of intron positions in alpha-amylase genes of Bilateria suggests numerous gains and losses. PLoS ONE<\/em> 6(5): e19673<\/p>\n

\"iconePdf\"<\/a>YASSIN A.,DA LAGE J.L.<\/strong>, DAVID J.R., KONDO M., MADI-RAVAZZI L., PRIGENT S., TODA M.J. (2010)<\/strong> Polyphyly of the Zaprionus<\/em> Genus Group (Diptera: Drosophilidae). Molecular Phylogenetics and Evolution<\/em> 55: 335<\/p>\n

\"iconePdf\"<\/a>YASSIN A., AMABIS J.M., DA LAGE J-L.<\/b>, DEBIAIS-THIBAUD M., DAVID J.R. (2010)<\/strong>. On the relationship between Zaprionus spinipilus<\/i> Chassagnard & McEvey and Z. vittiger<\/i> Coquillett, the type species of the genus Zaprionus<\/i> (Diptera: Drosophilidae). Ann. Soc. Entomol. Fr.<\/i> 46 (3-4)<\/p>\n

\"iconePdf\"<\/a>MCEVEY S. F., SCHIFFER M., DA LAGE J-L.<\/strong>, DAVID J. R., LEMEUNIER F., JOLY D., CAPY P. , CARIOU M-L. (2008) <\/strong>Comments on the proposed conservation of usage of Drosophila Fall\u00e9n, 1823 (Insecta, Diptera). Bulletin of Zoological Nomenclature<\/em> 65(2): 147<\/p>\n

\"iconePdf\"<\/a>LEGENDRE A., MIAO X.X., DA LAGE J.-L.<\/strong>, WICKER-THOMAS, C. (2008) <\/strong>Evolution of a desaturase involved in female pheromonal cuticular hydrocarbon biosynthesis and courtship behavior in Drosophila. Insect Biochem Mol. Biol.<\/em> 38(2): 244<\/p>\n

\"iconePdf\"<\/a> SCH\u00c4RER L., DA LAGE J.-L., <\/strong>JOLY D. (2008) <\/strong>Evolution of testicular architecture in the Drosophilidae: a role for sperm length. BMC Evol. Biol.<\/em> 8: 143<\/p>\n

\"iconePdf\"<\/a> YASSIN, A., ARARIPE, L.O., CAPY, P., DA LAGE, J-L.<\/strong>, KLACZKO L.B., MAISONHAUTE C., OGEREAU D., DAVID J.R. (2008) <\/strong>Grafting the molecular phylogenetic tree with morphological branches to reconstruct the evolutionary history of the genus Zaprionus (Diptera : Drosophilidae). Molecular Phylogenetics and Evolution<\/em> 47: 903<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L, <\/strong>DANCHIN E.G.J., CASANE D. (2007)<\/strong> Where do animal alpha-amylases come from? An interkingdom trip. FEBS Letters 581(21)<\/em>: 3927-3935<\/p>\n

\"iconePdf\"<\/a>DA LAGE, J-L., <\/strong>KERGOAT, G. J., MACZKOWIAK, F., SILVAIN, J-F., CARIOU, M-L. and LACHAISE, D. (2007)<\/strong> A phylogeny of Drosophilidae using the Amyrel gene: questioning the Drosophila melanogaster species group boundaries. Journal of Zoological Systematics and Evolutionary Research<\/em> 45(1): 47<\/p>\n

\"iconePdf\"<\/a> PREAT, T., DA LAGE, J-L., <\/strong>COLLEAUX, L., DIDELOT, G., MOLINARI, F., TCHENIO, P., MILHIET, E., MUNNICH, A., AND CARIOU, M-L. (2007)<\/strong> Response to comment on \u00ab\u00a0Tequila, a neurotrypsin ortholog, regulates long-term memory formation in Drosophila. Science<\/em> 316: 1698<\/p>\n

\"iconePdf\"<\/a>MACZKOWIAK, F.,DA LAGE, J-L. (2006) <\/strong>Origin and evolution of the Amyrel<\/em> gene in the alpha-amylase family of Diptera. Genetica<\/em> 128: 145<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L.<\/strong>, FELLER G., JANECEK S. (2004)<\/strong> Horizontal gene transfer from Eukarya to Bacteria: the alpha-amylase model. Cell. Mol. Life Sci.<\/em> 61(1): 97<\/p>\n

\"iconePdf\"<\/a>DA LAGE, J-L<\/strong>, MAISONHAUTE, C., MACZKOWIAK, F., CARIOU, M-L. (2003)<\/strong> A nested alpha-amylase gene in Drosophila ananassae<\/em>. J. Mol. Evol.<\/em> 57(3): 355<\/p>\n

\"iconePdf\"<\/a> ZHANG Z., INOMATA N., CARIOU M-L, DA LAGE J-L., <\/strong>YAMAZAKI, T. (2003) <\/strong>Phylogeny and evolution of the amylase multigenes in Drosophila montium<\/em> species subgroup. J. Mol. Evol.<\/em> 56: 121<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L<\/strong>, VAN WORMHOUDT A., CARIOU M-L (2002)<\/strong> Diversity and evolution of the alpha-amylase genes in animals. Biologia, Bratislava<\/em> 57: 181<\/p>\n

\"iconePdf\"<\/a> CARIOU ML., SILVAIN J-F., DAUBIN V., DA LAGE J-L., <\/strong>LACHAISE D. (2001) <\/strong>Divergence between Drosophila santomea<\/em> and allopatric or sympatric populations of D. yakuba<\/em> using paralogous amylase genes and migration scenarios along the Cameroon volcanic line. Mol. Ecol.<\/em> 10: 649<\/p>\n

\"iconePdf\"<\/a>DA LAGE, J.-L.<\/strong>, MACZKOWIAK, F., CARIOU, M.-L. (2000)<\/strong> Molecular characterization and evolution of the amylase multigene family of Drosophila ananassae.<\/em> J. Mol. Evol<\/em> 51: 391<\/p>\n

\"iconePdf\"<\/a>RICHARDS G., DA LAGE J-L.<\/strong>, HUET F. and RUIZ C. (1999)<\/strong> The acquisition of competence to respond to ecdysone in Drosophila is transcript specific.\u00a0 Mech. Dev.<\/em> 82(82): 131<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L<\/strong>, RENARD E, CHARTOIS F, LEMEUNIER F, CARIOU M-L (1998)<\/strong> Amyrel<\/em>, a paralogous gene of the amylase gene family in Drosophila melanogaster<\/em> and the Sophophora<\/em> subgenus. Proc. Natl. Acad. Sci.<\/em> USA<\/em> 95: 6848<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L.<\/strong>, KLARENBERG A., CARIOU M-L. (1996)<\/strong> Sex-, stage- and tissue-specific expression of amylase genes in Drosophila ananassae<\/em>. Heredity<\/em> 76: 9<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L.<\/strong>, WEGNEZ M., CARIOU M-L.(1996)<\/strong> Distribution and evolution of introns in Drosophila amylase genes. J. Mol. Evol.<\/em> 43: 334<\/p>\n

\"iconePdf\"<\/a>HUET F., DA LAGE J-L.<\/strong>, RUIZ C., RICHARDS G. (1996)<\/strong> The role of ecdysone in the induction and maintenance of hsp27 transcripts during larval and prepupal development of Drosophila. Dev. Genes Evol.<\/em> 206: 326<\/p>\n

CARIOU M-L., DA LAGE J-L. (1993)<\/strong> Isozyme polymorphisme. In: Drosophila ananassae, genetical and biological aspects. YN Tobari, Ed., Japan Scientific Societies Press, Karger, Tokyo 0: 160<\/p>\n

DA LAGE J-L.<\/strong>, CARIOU M-L. (1993)<\/strong> Organisation and structure of the amylase gene cluster. In: Drosophila ananassae, genetical and biological aspects. YN Tobari, Ed., Japan Scientific Societies Press, Karger, Tokyo 0: 171<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L.<\/strong>, LEMEUNIER F., CARIOU M-L., DAVID J.R. (1992)<\/strong> Multiple amylase genes in Drosophila ananassae<\/em> and related species. Genet. Res. Camb.<\/em> 59: 85<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L, <\/strong>CAPY, P., DAVID, J.R. (1990) <\/strong>Starvation and desiccation tolerance in Drosophila melanogaster<\/em>: differences between European, North African and Afrotropical populations. Genet. Sel. Evol.<\/em> 22: 381<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L.<\/strong>, CAPY P., DAVID J.R. (1989)<\/strong> Starvation and desiccation tolerance in Drosophila melanogaster<\/em> adults: effects of environmental temperature. J. Insect Physiol.<\/em> 35(6): 453<\/p>\n

\"iconePdf\"<\/a>DA LAGE J-L.<\/strong>, CARIOU M-L., DAVID J.R. (1989)<\/strong> Geographical polymorphism of amylase in Drosophila ananassae<\/em> and its relatives. Heredity<\/em> 63: 67<\/p>\n<\/div>\n","protected":false},"excerpt":{"rendered":"

Membre du p\u00f4le G\u00e9nomes Charg\u00e9 de recherches CNRS Doctorat Universit\u00e9 Paris VII (1990), HDR (2003) +33 (0)1 69 15 49 72 Jean-Luc.Da-Lage[@]universite-paris-saclay.fr Th\u00e8mes de Recherche Evolution mol\u00e9culaire des g\u00e8nes et de la prot\u00e9ine d’alpha-amylase chez les m\u00e9tazoaires. Evolution fonctionnelle de l’enzyme, duplications et famille multig\u00e9nique, origine et \u00e9volution des introns, transferts horizontaux. L’alpha-amylase est une […]<\/p>\n","protected":false},"author":27,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"site-sidebar-layout":"default","site-content-layout":"","ast-site-content-layout":"default","site-content-style":"default","site-sidebar-style":"default","ast-global-header-display":"","ast-banner-title-visibility":"","ast-main-header-display":"","ast-hfb-above-header-display":"","ast-hfb-below-header-display":"","ast-hfb-mobile-header-display":"","site-post-title":"","ast-breadcrumbs-content":"","ast-featured-img":"","footer-sml-layout":"","ast-disable-related-posts":"","theme-transparent-header-meta":"","adv-header-id-meta":"","stick-header-meta":"","header-above-stick-meta":"","header-main-stick-meta":"","header-below-stick-meta":"","astra-migrate-meta-layouts":"set","ast-page-background-enabled":"default","ast-page-background-meta":{"desktop":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"tablet":{"background-color":"","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"mobile":{"background-color":"","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""}},"ast-content-background-meta":{"desktop":{"background-color":"var(--ast-global-color-5)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"tablet":{"background-color":"var(--ast-global-color-5)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"mobile":{"background-color":"var(--ast-global-color-5)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""}},"_themeisle_gutenberg_block_has_review":false,"_jetpack_memberships_contains_paid_content":false,"footnotes":""},"categories":[12],"tags":[],"class_list":["post-713","post","type-post","status-publish","format-standard","hentry","category-personnels"],"jetpack_featured_media_url":"","jetpack_sharing_enabled":true,"_links":{"self":[{"href":"https:\/\/www.egce.universite-paris-saclay.fr\/index.php?rest_route=\/wp\/v2\/posts\/713","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.egce.universite-paris-saclay.fr\/index.php?rest_route=\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.egce.universite-paris-saclay.fr\/index.php?rest_route=\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.egce.universite-paris-saclay.fr\/index.php?rest_route=\/wp\/v2\/users\/27"}],"replies":[{"embeddable":true,"href":"https:\/\/www.egce.universite-paris-saclay.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=713"}],"version-history":[{"count":7,"href":"https:\/\/www.egce.universite-paris-saclay.fr\/index.php?rest_route=\/wp\/v2\/posts\/713\/revisions"}],"predecessor-version":[{"id":20293,"href":"https:\/\/www.egce.universite-paris-saclay.fr\/index.php?rest_route=\/wp\/v2\/posts\/713\/revisions\/20293"}],"wp:attachment":[{"href":"https:\/\/www.egce.universite-paris-saclay.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=713"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.egce.universite-paris-saclay.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=713"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.egce.universite-paris-saclay.fr\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=713"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}