{"id":283487,"date":"2026-08-31T15:14:42","date_gmt":"2026-08-31T14:14:42","guid":{"rendered":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/?p=283487"},"modified":"2026-08-31T15:14:43","modified_gmt":"2026-08-31T14:14:43","slug":"bmp26-01-poster-prizes","status":"publish","type":"post","link":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/2026\/08\/bmp26-01-poster-prizes\/","title":{"rendered":"Meet the best poster prize winners of ‘BioMalPar XXII: biology and pathology of the malaria parasite’"},"content":{"rendered":"\n

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From 27 \u2013 29 May, we welcomed 228 on-site and 50 virtual participants from around the world to the EMBL Conference ‘BioMalPar XXII: biology and pathology of the malaria parasite<\/a>‘.<\/p>\n\n\n\n

Every year, the malaria research community comes together in Heidelberg to exchange knowledge and drive forward the innovations and strategies needed to advance the field. This year\u2019s conference highlighted recent developments in basic and translational malaria research, from the biology of malaria parasites, their interactions with mammalian hosts and mosquito vectors, and the development of new interventions.<\/p>\n\n\n\n

Throughout the conference, participants presented 180 posters sharing their latest research. Ten presenters were recognised with poster prizes for their excellent contributions. Read on to learn more about their work and join us in congratulating eight of this year\u2019s winners!<\/p>\n\n\n\n

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From fusion to conquest: how Plasmodium falciparum SNARE proteins orchestrate erythrocyte<\/strong><\/h2>\n\n\n\n

Presenter: Robert Dom\u00e8nech Eres<\/a><\/strong><\/strong><\/p>\n\n\n\n

Authors: Robert Dom\u00e8nech Eres, Anna-Lena Sandtmann, Monja Paasche, Victor Alonso Meyer, Joachim Michael Matz<\/p>\n\n\n\n

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Robert Dom\u00e8nech Eres<\/strong>
Bernhard Nocht Institute for Tropical Medicine, Germany<\/figcaption><\/figure>\n\n\n\n

Abstract:<\/strong><\/p>\n\n\n\n

The malaria parasite Plasmodium falciparum relies on the coordinated action of specialized secretory systems to invade and replicate within human erythrocytes. During host cell invasion, organelles of the parasite apex, called rhoptries and micronemes, fuse with the parasite plasma membrane (PPM) to secrete proteins that mediate host cell attachment and entry, allowing the parasite to push itself into a parasitophorous vacuole (PV) that is maintained throughout intraerythrocytic development. Maturation of this intracellular niche depends on the discharge of proteins pre-stored in dense granules (DG), which remodel the newly formed PV and the host environment to support parasite survival and replication. Despite the central role of these highly specialized secretion events in the establishment of erythrocyte infection, the underlying membrane fusion machinery that drives organelle discharge remains unknown.<\/p>\n\n\n\n

Here, we combine conditional reverse genetics with quantitative live-cell imaging and protein interaction studies to functionally characterize a membrane fusion complex consisting of at least three SNARE proteins that localize to the PPM. DiCre-mediated genetic disruption of this complex impairs host cell invasion through defective microneme secretion, leading to retention of cargo proteins such as AMA1 within the micronemes in approximately half of the parasite population, rather than translocating to the parasite surface. Furthermore, inactivation of any of these SNAREs caused DG-resident proteins PV1, EXP2 and RESA \u2013 normally targeted to the PV, PVM or host cell compartment \u2013 to remain trapped within the parasite, indicative of defective DG discharge and resulting in parasite death shortly after invasion. Quantitative fluorescence microscopy combined with co-immunoprecipitation analyses further demonstrate that these three SNARE proteins specifically interact at the PPM, forming a membrane fusion complex with consistent stoichiometric proportions during establishment of erythrocyte infection. Combined, our findings identify a SNARE-based fusion complex at the plasma membrane of P. falciparum that orchestrates the coordinated release of micronemes and DGs required for successful red blood cell colonization.<\/p>\n\n\n\n

View poster<\/a><\/em><\/p>\n\n\n\n

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Defective nuclear uptake impairs Plasmodium transmission in SFA mutants Heidelberg<\/strong><\/h2>\n\n\n\n

Presenter: Yvonne Sokolowski-Adams<\/strong><\/strong><\/strong><\/p>\n\n\n\n

Authors: Yvonne Sokolowski-Adams, Buyuan He, Ilzat Ali, Jeffrey Dvorin, Friedrich Frischknecht<\/p>\n\n\n\n

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Yvonne Sokolowski-Adams<\/strong>
Heidelberg University Hospital, Germany<\/figcaption><\/figure>\n\n\n\n

Abstract:<\/strong><\/p>\n\n\n\n

Plasmodium parasites replicate by schizogony in red blood cells and sporogony in mosquito oocysts, processes that require precise coordination of nuclear division and daughter cell assembly. How nuclei are incorporated into emerging daughter cells remains unclear. We analyzed two striated fiber assemblins, SFA1 and SFA2, in Plasmodium falciparum and Plasmodium berghei to define their role in nuclear segregation and
morphogenesis. Deletion of PbSFA1 or PbSFA2 in P. berghei caused moderately reduced asexual growth, yet nuclear numbers per schizont were unchanged, indicating that nuclear multiplication during schizogony is largely intact. Gametocyte commitment and sex ratios were unaffected. In contrast, male gametocytes showed significantly reduced exflagellation, pointing to impaired efficiency of microgamete formation. Because exflagellation requires rapid DNA replication and coordinated nuclear segregation into flagellated gametes, this phenotype suggests defective coupling between nuclear dynamics and cytoskeletal assembly. 3D electron microscopy reveals new views of the link between axoneme assembly and nuclear separation during gametogenesis and hints at a possible role for SFAs in this process. Fertilization and motile ookinete formation still occurred in the mutants, although conversion efficiency was reduced. The strongest defect emerged during sporogony. Mutant parasites formed fewer oocysts and produced almost no sporozoites. Rare sporozoites displayed normal shape and microtubule staining but lacked detectable nuclear material, indicating a severe defect in nuclear incorporation rather than cytoskeletal assembly. No sporozoites were detected in salivary glands. These findings identify SFA1 and SFA2 as structural factors that couple nuclear segregation to daughter cell formation and are particularly critical during transmission stages requiring synchronized nuclear partitioning.<\/p>\n\n\n\n

View poster<\/a><\/em><\/p>\n\n\n\n

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Hole-y nuclear architecture! ExM expands our knowledge of parasite spatio-temporal transcriptional regulation<\/strong><\/strong><\/strong><\/strong><\/h2>\n\n\n\n

Presenter: Maureen Cabahug<\/strong><\/p>\n\n\n\n

Authors: Maureen Cabahug, Jessica Bryant, Parul Singh, Patty Chen<\/p>\n\n\n\n

\"\"
Maureen Cabahug<\/strong>
Institut Pasteur, France<\/figcaption><\/figure>\n\n\n\n

Abstract:<\/strong><\/p>\n\n\n\n

During its complex life cycle, the human malaria parasite, Plasmodium falciparum, has many morphologically distinct stages, each with a unique transcriptional profile. With a limited molecular toolbox regarding sequence-specific transcription factors and genome-organizing proteins, this parasite offers an interesting model for studying how nuclear architecture influences transcriptional programs that underlie survival and virulence in the human host. While heterochromatinized genes encoding variant surface antigens cluster at= the nuclear periphery, our recent work revealed long-range intra- and inter-chromosomal interactions amongst highly active, stage-specific genes during the intraerythrocytic developmental cycle (IDC). In the late stage of the IDC, these active genes are bound by two ApiAP2 factors, AP2-I and AP2-P, as well as MORC, a putative chromatin remodeler. Knockdown of AP2-P, AP2-I, or both led to down-regulation of these genes, and AP2-P knockdown led to loss of interactions. Thus, we hypothesized that this protein complex brings genes together into what may be transcription hubs for rapid, stage-specific activation. To visualize such a nuclear compartment in the tiny parasite nucleus, we recently adapted ultrastructure expansion microscopy, which revealed a striking nuclear substructure in late stages of the IDC. Each nucleus of the segmented schizont has a large, central region that is depleted of histone H3 and enriched in AP2-P and high mobility group box 1 (HMGB1) protein, which binds to the two active ribosomal DNA loci during the IDC. These data suggest that highly active genes, most likely enriched in histone variant H3.3, localize to a central transcription hub that is enriched in transcriptional machinery. Our ongoing work will provide insight into how the parasite nucleus is divided into peripheral and central compartments for constitutive silencing and stage-specific activation, respectively, of genes.<\/p>\n\n\n\n

Due to the confidentiality of the unpublished data, we cannot show the poster.<\/em><\/p>\n\n\n\n

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Understanding the role of lipid metabolism in mediating artemisinin tolerance in Plasmodium falciparum<\/strong><\/strong><\/strong><\/h2>\n\n\n\n

Presenter: Saptarshi Mridha<\/a><\/strong><\/strong><\/p>\n\n\n\n

Authors: Saptarshi Mridha, Riya Ahmed, Krishanpal Karmodiya<\/p>\n\n\n\n

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Saptarshi Mridha<\/strong>
Indian Institute of Science Education and Research Pune, India<\/figcaption><\/figure>\n\n\n\n

Abstract:<\/strong><\/p>\n\n\n\n

Plasmodium falciparum has developed advanced ways to escape both antimalarial treatments and the immune defences of its host, making it the most lethal strain to cause human malaria. Even with the widespread use of antimalarial drugs, the rise and global spread of resistant strains pose substantial complexities to malaria eradication. Artemisinin is the frontline drug against the disease, and the development of resistance to this drug is a significant concern. Mutations in the parasite\u2019s Kelch13 protein, including C580Y, R539T, and I543T, are often linked to artemisinin resistance, but they do not work in isolation. Recent studies show that broader metabolic changes, particularly in lipid metabolism, help these mutant parasites survive the drug-induced stress through dormancy and metabolic adjustments. In this study, we use Kelch13 mutant and wild-type lines to understand the metabolic and lipidomic changes associated with the artemisinin-resistant parasites using transcriptomics and LC\/MS-based lipidomic analyses. Our findings show clear changes in lipid class distribution and flow in resistant parasites. Additionally, population genomics analysis of about 2,500 field isolates from Africa and Southeast Asia was directed towards a possible \u03b1\/\u03b2 hydrolase with multiple mutations alongside Kelch13 changes. Biochemical tests suggest that it acts as a serine hydrolase with possible lipase activity, linking it to lipid remodelling processes that are key to resistance traits. Overall, this research demonstrates that lipidomic changes are a defining feature of artemisinin-resistant P. falciparum. Such changes are a combination of Kelch13-related and other genome-wide mutations in the background. It highlights the significance of metabolic profiling for monitoring resistance and opens new avenues for targeting metabolic enzymes as future antimalarial strategies.<\/p>\n\n\n\n

Due to the confidentiality of the unpublished data, we cannot show the poster.<\/em><\/p>\n\n\n\n

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Plasmodium falciparum cysteine protease falcipain 3: a potential enzyme for proteolytic processing of histone acetyltransferase PfGCN5<\/strong><\/strong><\/strong><\/strong><\/h2>\n\n\n\n

Presenter: Poonam Nagar<\/a><\/strong><\/strong><\/p>\n\n\n\n

Authors: Poonam Nagar<\/p>\n\n\n\n

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Poonam Nagar<\/strong>
Jawaharlal Nehru University, India<\/figcaption><\/figure>\n\n\n\n

Abstract:<\/strong><\/p>\n\n\n\n

Despite over 150 years of malaria research, the causative parasite, Plasmodium, still perplexes researchers. One of the mechanisms by which the parasite controls its gene expression is epigenetic regulation, the champion of which is PfGCN5, an essential enzyme responsible for catalysing the acetylation of histone proteins. PfGCN5 is an approximately 170 kDa chromatin-remodelling enzyme that harbours the conserved bromodomain and acetyltransferase domain localized at its C-terminus. PfGCN5 undergoes proteolytic processing; however, the specific protease involved in this process still remains elusive. Immunoprecipitation of PfGCN5 followed by LC\u2013MS\/MS analysis identified the presence of food vacuolar proteins, like cysteine protease Falcipain 3 (FP3), apart from the typical members of the PfGCN5 complex. Direct interaction between FP3 and PfGCN5 was confirmed by an in vitro pull-down assay and an immunoprecipitation assay. Subsequently, use of the cysteine protease inhibitor E64d led to the inhibition of processing of PfGCN5, accompanied by concomitant enrichment and co-localization of PfGCN5 and FP3 around the food vacuole as evidenced by confocal microscopy and Electron Microscopy. The proteolytic processing of the nuclear protein PfGCN5 by the food vacuolar protease FP3 represents an unusual and atypical phenomenon in eukaryotic systems. Targeting the proteolytic processing of GCN5 and the associated protease FP3 could provide a novel approach for drug development aimed at addressing the growing resistance of parasites to current antimalarial drugs.<\/p>\n\n\n\n

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View poster<\/a><\/em><\/p>\n\n\n\n

Kindly sponsored by The Neer Tewari Foundation<\/a>.<\/em><\/p>\n\n\n\n

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How we halved transfection times, broke up with WR99210 and developed a novel PKG_T618Q selection cassette<\/h2>\n\n\n\n

Presenters: Stephanie Diane Nofal<\/strong><\/strong>, Hugo Belda<\/strong>, Gwendolin Fuchs<\/strong><\/p>\n\n\n\n

Authors: Stephanie Diane Nofal, Hugo Belda, Gwendolin Fuchs, Heledd Davies, Moritz Treeck<\/p>\n\n\n\n

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Stephanie Diane Nofal<\/strong>, Hugo Belda<\/strong> and<\/strong>
Gwendolin Fuchs<\/strong>
Gulbenkian Institute for Molecular Medicine, Portugal<\/figcaption><\/figure>\n\n\n\n

Abstract:<\/strong><\/p>\n\n\n\n

WR99210 is widely used in the malaria field for the selection of transgenic Plasmodium falciparum parasites and has long served as a cornerstone of parasite genetic manipulation. However, increasing difficulties in sourcing WR99210 and the limited efficacy of commercial alternatives raise concerns regarding its long-term availability. Given that WR99210 acts by inhibition of parasite dihydrofolate reductase (DHFR), we reasoned that alternative DHFR inhibitors such as trimethoprim (TMP) could provide a robust and accessible replacement. <\/p>\n\n\n\n

We found that TMP effectively selects parasites carrying a plasmid harbouring the hDHFR resistance cassette and unexpectedly resulted in significantly faster recovery following transfection as compared to standard WR99210 selection. Transfections reached 5% parasitemia within 2\u20133 weeks with TMP selection, compared to 4\u20136 weeks using conventional WR99210 regimens. Notably, the standard WR99210 concentration used for transgenic selection (5 nM) corresponds to approximately 80 times the IC50, whereas TMP selection is performed at ~8x IC50. Reducing WR99210 to 8x IC50 improved recovery times without compromising integration efficiency, indicating that excessive drug pressure delays post-transfection growth. Another challenge to generating transgenic parasite lines is the limited number of drug selection tools available. To further expand the available selection tools, we developed a novel selection cassette based on a T618Q mutation in the cGMP-dependent protein kinase (PKG), which confers resistance to PKG inhibitors such as compound 2 or ML10. When used for Selection Linked Integration (SLI), this cassette proved highly effective.<\/p>\n\n\n\n

Additionally, we generated a new Cas9 plasmid that incorporates a BSD resistance marker. These novel resources provide additional flexibility for combinatorial genome editing, particularly in the context of generating complex lines harbouring multiple modifications. <\/p>\n\n\n\n

Overall, we have developed drug regimens and a novel selection cassette that significantly shorten transfection timelines and broaden the genetic toolkit for parasite transfections. Importantly, these drugs are cheap and easily available, addressing the potential future shortage of WR99210.<\/p>\n\n\n\n

View poster<\/a><\/em><\/p>\n\n\n\n

Kindly sponsored by The Neer Tewari Foundation.<\/em><\/p>\n\n\n\n

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Single-cell transcriptomic profiling of Plasmodium falciparum basal and environmentally-induced sexual commitment<\/h2>\n\n\n\n

Presenter: Anna Oncins Su\u00f1ol<\/a><\/strong><\/strong><\/p>\n\n\n\n

Authors: Anna Oncins Su\u00f1ol, Alfred Cortes, Elisabet Tint\u00f3, Marta Chiodin<\/p>\n\n\n\n

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Anna Oncins Su\u00f1ol<\/strong>
Barcelona Institute for Global Health, Spain<\/figcaption><\/figure>\n\n\n\n

Abstract:<\/strong><\/p>\n\n\n\n

Human-to-mosquito transmission of malaria requires the generation of sexual forms called gametocytes. Plasmodium falciparum replicates asexually in the human blood, with a subset of parasites committing to sexual differentiation at each round of the replicative cycle. In the following cycle, sexually committed parasites stop replicating and convert into sexual forms. Sexual commitment and conversion are driven by the master regulator AP2-G, which initiates a transcriptional cascade required for gametocyte development. AP2-G activation depends on GDV1, which displaces heterochromatin from the ap2-g locus and is negatively regulated by its antisense lncRNA, gdv1-as. Environmental stressors such as elevated temperature, drug exposure or nutrient depletion can increase the proportion of parasites converting into sexual forms. Yet, the mechanisms by which parasites respond to these environmental cues and commit to sexual development remain poorly understood. Here, we applied single-cell transcriptomics to characterize transcriptional changes across the commitment cycle under basal or inducing conditions (choline depletion). Our data showed with unprecedented high resolution that committed parasites cluster separately from non-committed counterparts from the late trophozoite stage and uncovered new genes specifically enriched in the committed population. In contrast, gdv1 transcripts were detected in a broader population before committed parasites diverged. Notably, late schizonts stopped expressing most canonical commitment markers, except for ap2-g, and no longer clustered separately from non-committed parasites, whereas newly formed rings segregated again into sexual or asexual clusters. Furthermore, the comparison between induced and spontaneous sexually committed parasites revealed differences in the expression of some genes. Ongoing analyses of gdv1\/gdv1-as transcript dynamics and their co-expression with other genes may clarify their contribution to spontaneous versus induced commitment. Future work combining the analysis at the single-cell level of knockout lines for early regulators of sexual conversion and different stress conditions will shed additional light on the molecular basis of basal and induced sexual conversion in P. falciparum.<\/p>\n\n\n\n

Due to the confidentiality of the unpublished data, we cannot show the poster.<\/em><\/em><\/p>\n\n\n\n

Kindly sponsored by The Neer Tewari Foundation.<\/em><\/p>\n\n\n\n

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Investigating how variation in malaria vaccine candidate, PfRh5, impacts immune evasion<\/h2>\n\n\n\n

Presenter: Elon Atlaw<\/a><\/strong><\/strong><\/p>\n\n\n\n

Authors: Cyrianne Keutcha, Amy Bei, Laty Thiam, Elon Atlaw, Kristy McHugh, Aboubacar Ba, Rebecca Li, Mariama Nicole Pouye, Awa Cisse, Simon Draper, Yicheng Guo, Dimitra Pipini, Lawrence Shapiro, Zizhang Sheng, Fatoumata Diallo, Seynaboudiouf Sene, Alassane Thiam, Alassane Mbengue, Ines Vigan-womas, Saurabh Patel<\/p>\n\n\n\n

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Elon Atlaw<\/strong>
Yale School of Public Health, US<\/figcaption><\/figure>\n\n\n\n

Abstract:<\/strong><\/p>\n\n\n\n

Although treated with antimalarial drugs and prevented by insecticide-treated nets (ITNs), drug resistance has recently stalled malaria control efforts. Vaccine development offers another strategy, with sporozoite-stage vaccines showing promise, but their efficacy is challenged by the parasite’s complex life cycle and genetic diversity, highlighting the need for next-generation vaccines targeting other stages, like the blood stage, to control breakthrough infections from first-generation vaccines. The RH5 protein in P.falciparum (PfRh5) is a promising target for a blood-stage vaccine due to its conservation, its essential role in the PCRCR complex that binds human erythrocyte receptor, Basigin (BSG), and its susceptibility to vaccine-induced human monoclonal antibodies. A recent phase 2b trial showed that the RH5.1 vaccine had the highest efficacy of any blood-stage vaccine tested to date, but the impact of genetic variation in RH5 needs to be further investigated. We propose to study the effect of three single-nucleotide polymorphisms (SNPs) in PfRh5, D243N, D249G, and F505Y, found in endemic regions of Senegal, on immune response, invasion, and antibody binding. The D243N and F505Y SNPs are located in a region that interacts with another member of the PCRCR complex, PfCyRPA, while D249G is found in a region that interacts with BSG and occurred in a parasite that was less susceptible to a vaccine-induced RH5 antibody. To this end, I first aim to assess the functional roles of PfRh5 variants on immune neutralization using CRISPR-Cas9 gene editing of P. falciparum parasites. My second aim is to identify genetic polymorphisms in PfRh5 in culture-adapted parasite lines from Thies, Senegal using next-generation sequencing. DNA was extracted from dried blood spots of culture-adapted samples (n=58), and the full-length PfRh5 gene was amplified. PfRh5 amplicons were library-prepped and sequenced using Oxford Nanopore Technologies. SNPs were identified in each sample using Geneious Prime Software and will be tested for immune evasion against antibodies isolated from vaccine trials through growth-inhibition assays (GIAs). Our objective is to investigate the role of PfRh5 genetic variants, found in monogenomic clinical isolates or transfected into an isogenic background, to guide the design of the next-generation vaccine.<\/p>\n\n\n\n

Due to the confidentiality of the unpublished data, we cannot show the poster.<\/em><\/em><\/p>\n\n\n\n

Kindly sponsored by The Neer Tewari Foundation.<\/em><\/p>\n\n\n\n

<\/p>\n\n\n\n

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The EMBL Conference ‘BioMalPar XXII: biology and pathology of the malaria parasite<\/a>‘ took place from 27 \u2013 29 May 2026 at EMBL Heidelberg and virtually.<\/em><\/p>\n\n\n\n

Discover BioMalPar XXII from the perspective of event reporter Joy Kabagenyi<\/a>.<\/p>\n","protected":false},"excerpt":{"rendered":"

In case you missed the EMBL Conference BioMalPar, we are presenting the best poster prize winners. Read on to find out about their research!<\/p>\n","protected":false},"author":105,"featured_media":283507,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[7960],"tags":[7858,7950,7958,7832,7732,8210,7642,8100],"embl_taxonomy":[],"class_list":["post-283487","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-best-poster-awards","tag-emblmalaria","tag-abstract","tag-best-poster","tag-biomalpar","tag-conference","tag-malaria-parasite","tag-poster","tag-poster-prize"],"acf":[],"embl_taxonomy_terms":[],"featured_image_src":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-content\/uploads\/KeyVisual_BioMalPar_2026_RGB_square-scaled.jpg","_links":{"self":[{"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/posts\/283487","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/users\/105"}],"replies":[{"embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/comments?post=283487"}],"version-history":[{"count":14,"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/posts\/283487\/revisions"}],"predecessor-version":[{"id":284031,"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/posts\/283487\/revisions\/284031"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/media\/283507"}],"wp:attachment":[{"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/media?parent=283487"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/categories?post=283487"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/tags?post=283487"},{"taxonomy":"embl_taxonomy","embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/course-and-conference-office\/wp-json\/wp\/v2\/embl_taxonomy?post=283487"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}