{"id":39456,"date":"2021-06-25T20:00:00","date_gmt":"2021-06-25T18:00:00","guid":{"rendered":"https:\/\/www.embl.org\/news\/?p=39456"},"modified":"2024-03-22T11:17:50","modified_gmt":"2024-03-22T10:17:50","slug":"structural-biology-reveals-new-opportunities-to-combat-tuberculosis","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/","title":{"rendered":"Structural biology reveals new opportunities to combat tuberculosis"},"content":{"rendered":"\n

Tuberculosis is one of the top ten causes of death worldwide, infecting about one-quarter of the world\u2019s population. Although it is treatable, the rise of multidrug-resistant tuberculosis poses a major threat to global health security, and has been declared by the World Health Organization as a global health emergency<\/a>. Reduced access to diagnosis and treatment during the COVID-19 pandemic is expected to dramatically increase the number of tuberculosis infections. This will set global efforts to tackle the disease back several years.<\/p>\n\n\n\n

Tuberculosis is caused by infection with Mycobacterium tuberculosis<\/em>: a bacterium that infects human lungs and other organs by using complex molecular machineries. These include protein complexes known as type VII secretion systems, which enable M. tuberculosis<\/em> to release molecules into its host, which disarm and ultimately kill the infected human cell. Five such secretion systems, labelled ESX-1 to ESX-5, are found among M. tuberculosis<\/em> and other closely related mycobacteria, many of which are pathogenic. Without them, the bacteria are unable to infect human cells.<\/p>\n\n\n\n

The Wilmanns group at EMBL Hamburg has been using high-resolution structural biology to study mycobacterial proteins for the last two decades. The molecular understanding of the bacterial machinery used to infect cells resulted in collaborations with industry to develop new drugs against tuberculosis. In their most recent study, they determined the molecular structure of the secretion system ESX-5 to a high level of detail. They saw that the core of ESX-5 is built of 30 protein units, which form a dynamic membrane pore to allow secretion of proteins that enable the bacterium to survive and multiply inside human cells. Knowledge of the ESX-5 structure at high-resolution is essential to target specific sites with small-molecule drugs.<\/p>\n\n\n\n

\u201cOur new structure of the ESX-5 secretion complex provides deep insight into a major sluice gate that separates the inner of these bacteria from the outer host environment. Opening this gate allow the pathogen to spit out its deadly weapons to infect humans to develop tuberculosis. We can use this structure as a toolbox with literally thousands of potential drug targets. This will open an entirely new field of studies on tuberculosis,\u201d says Matthias Wilmanns, who leads the study. Kate Beckham, who developed an innovative way to isolate ESX-5, adds: \u201cThe central pore we saw in ESX-5 could serve as a new drug target. Blocking it could prevent infection with pathogenic mycobacteria.\u201d<\/p>\n\n\n\n

The study could also help scientists to develop new vaccines for tuberculosis. The widely used Bacillus Calmette\u2013Gu\u00e9rin (BCG) vaccine, which has its 100th anniversary<\/a> this year, is based on a strain of mycobacterium that has lost its ability to cause disease because of a defect in the ESX-1 system. However, as BCG vaccination offers insufficient protection and is most effective in young infants only, alternative vaccines are urgently needed. Due to its close structural and functional relation with ESX-1, targeting the ESX-5 secretion system might spur the development of new vaccines that could complement or replace those currently used.<\/p>\n\n\n\n

Determining the molecular structure of ESX-5 was particularly challenging because of its large size and complexity. No single structural biology method can provide the full picture. In this case, the key to success was using integrative structural biology, in which data obtained using different methods \u2013 cryo-electron microscopy, X-ray crystallography, mass spectrometry and computational methods \u2013 were used jointly to create a coherent model.<\/p>\n\n\n\n

\u201cEighteen months ago, solving this structure looked like mission: impossible,\u201d says Matthias Wilmanns. \u201cWe managed to put the puzzle pieces together because each team member contributed unique expertise. To solve the complete structure, we collaborated with Jan Kosinski\u2019s group at EMBL Hamburg and the Centre for Structural Systems Biology<\/a>, which provided necessary expertise in integrative structural biology. We also received great help from our colleagues at EMBL Heidelberg, who performed cryo-electron microscopy experiments.\u201d<\/p>\n\n\n\n

This study illustrates some of EMBL\u2019s approaches to life science research in its forthcoming scientific programme, Molecules to Ecosystems 2022\u20132026<\/em>. As part of this programme, EMBL will take an interdisciplinary approach to understanding the molecular basis of life in the context of environmental changes. This will provide translational potential to support advances in human and planetary health.<\/p>\n\n\n\n

EMBL\u2019s approach, including this study, is aligned with the collaborative efforts of other research groups and institutions from Northern Germany working together at the Centre for Structural Systems Biology<\/a>.<\/p>\n\n\n\n

\n\n\n\n

Tuberkulosebek\u00e4mpfung: Neue Erkenntnisse aus der Strukturbiologie<\/strong><\/h1>\n\n\n\n

Die Gruppen Wilmanns und Kosinski vom EMBL Hamburg haben die detaillierte Struktur eines bakteriellen Proteinkomplexes bestimmt, der f\u00fcr die Tuberkulose-Infektion entscheidend ist<\/h2>\n\n\n\n
\"Eine
Molekulare Struktur des mykobakteriellen ESX-5-Sekretionssystems. Das mykobakterielle ESX-5-Sekretionssystem befindet sich in der bakteriellen Innenmembran und besteht aus sechs Einheiten, die sich zu einer symmetrischen Struktur mit einer Pore in der Mitte zusammensetzen. Credit: Isabel Romero Calvo\/EMBL<\/figcaption><\/figure>\n\n\n\n

Obwohl sie in den meisten F\u00e4llen gut behandelbar ist, ist Tuberkulose<\/a> eine der zehn h\u00e4ufigsten Todesursachen weltweit. Ein Viertel der Weltbev\u00f6lkerung ist mit Tuberkulose infiziert. Die Verbreitung der multiresistenten Tuberkulose stellt eine gro\u00dfe Bedrohung f\u00fcr die globale Gesundheitssicherheit dar und wurde von der Weltgesundheitsorganisation zum globalen Gesundheitsnotstand<\/a> erkl\u00e4rt. Der zus\u00e4tzlich eingeschr\u00e4nkte Zugang zu Diagnose und Behandlung w\u00e4hrend der COVID-19-Pandemie erh\u00f6ht die Zahl der Tuberkulose-Infektionen voraussichtlich dramatisch<\/a> und wird damit globale Bem\u00fchungen zur Bek\u00e4mpfung der Krankheit um mehrere Jahre zur\u00fcckwerfen.<\/p>\n\n\n\n

Tuberkulose wird durch eine Infektion mit dem Mycobacterium tuberculosis verursacht: einem Bakterium, das die menschliche Lunge und andere Organe mit Hilfe komplexer molekularer Mechanismen infiziert. Dazu geh\u00f6ren Proteinkomplexe, die als Typ-VII-Sekretionssysteme bekannt sind und die es M. tuberculosis erm\u00f6glichen, Molek\u00fcle in seinem Wirt freizusetzen, die die infizierte menschliche Zelle entwaffnen und schlie\u00dflich abt\u00f6ten. F\u00fcnf solcher Sekretionssysteme, bezeichnet als ESX-1 bis ESX-5, finden sich bei M. tuberculosis und anderen eng verwandten, meist pathogenen Mykobakterien. Ohne die Sekretionssysteme sind die Bakterien nicht in der Lage, menschliche Zellen zu infizieren.<\/p>\n\n\n\n

Die Wilmanns Gruppe am EMBL Hamburg<\/a> hat in den vergangenen zwei Jahrzehnten mit Hilfe der hochaufl\u00f6senden Methoden der Strukturbiologie mykobakterielle Proteine untersucht. In ihrer j\u00fcngsten Studie bestimmte sie die molekulare Struktur des Sekretionssystems ESX-5 im kleinstm\u00f6glichen Detail. Die ForscherInnen fanden dabei heraus, dass der Kern von ESX-5 aus 30 Proteineinheiten aufgebaut ist, <\/a>die eine dynamische Membranpore bilden um die Sekretion von Proteinen zu erm\u00f6glichen, die dem Bakterium das \u00dcberleben und die Vermehrung in menschlichen Zellen erm\u00f6glichen. Die Kenntnis der ESX-5-Struktur in hoher Aufl\u00f6sung ist unerl\u00e4sslich, um spezifische Stellen mit niedermolekularen Wirkstoffen anzusprechen. Das molekulare Verst\u00e4ndnis der bakteriellen Mechanismen, mit der Zellen infiziert werden, f\u00fchrte bereits zu Kooperationen mit der Industrieforschung, um neue Medikamente gegen Tuberkulose zu entwickeln.<\/p>\n\n\n\n

“Unsere neue Struktur des ESX-5-Sekretionskomplexes gibt einen tiefen Einblick in ein wichtiges Schleusentor, das das Innere dieser Bakterien von der \u00e4u\u00dferen Wirtsumgebung trennt. Wird dieses Tor ge\u00f6ffnet, kann der Erreger seine t\u00f6dlichen Waffen ausspucken, um den Menschen zu infizieren und Tuberkulose zu entwickeln. Wir k\u00f6nnen diese Struktur als Werkzeugkasten mit buchst\u00e4blich Tausenden von potenziellen Wirkstoffzielen nutzen. Damit er\u00f6ffnet sich ein v\u00f6llig neues Feld f\u00fcr Studien zur Tuberkulose”, sagt Matthias Wilmanns, der die Studie leitet. Kate Beckham, die einen innovativen Weg zur Isolierung von ESX-5 entwickelt hat, erg\u00e4nzt: “Die zentrale Pore, die wir in ESX-5 gesehen haben, k\u00f6nnte als neues Ziel f\u00fcr Medikamente dienen. Sie zu blockieren k\u00f6nnte eine Infektion mit pathogenen Mykobakterien verhindern.”<\/p>\n\n\n\n

Die Studie k\u00f6nnte Wissenschaftlern auch dabei helfen, neue Impfstoffe gegen Tuberkulose zu entwickeln. Der weit verbreitete Bacillus Calmette-Gu\u00e9rin (BCG)-Impfstoff, der in diesem Jahr sein 100-j\u00e4hriges Jubil\u00e4um<\/a> feiert, basiert auf einem Mykobakterienstamm, der durch einen Defekt im ESX-1-System seine F\u00e4higkeit verloren hat, Krankheiten zu verursachen. Da die BCG-Impfung mittlerweile also nur einen unzureichenden Schutz bietet und lediglich bei S\u00e4uglingen am wirksamsten ist, werden dringend alternative Impfstoffe ben\u00f6tigt. Aufgrund seiner engen strukturellen und funktionellen Verwandtschaft mit ESX-1 k\u00f6nnte die gezielte Beeinflussung des ESX-5-Sekretionssystems die Entwicklung neuer Impfstoffe vorantreiben, die die derzeit verwendeten Impfstoffe erg\u00e4nzen oder ersetzen k\u00f6nnten.<\/p>\n\n\n\n

Die Bestimmung der molekularen Struktur von ESX-5 war aufgrund seiner gro\u00dfen Gr\u00f6\u00dfe und Komplexit\u00e4t eine besondere Herausforderung. Keine einzelne strukturbiologische Methode kann das vollst\u00e4ndige Bild liefern. In diesem Fall lag der Schl\u00fcssel zum Erfolg in der integrativen Strukturbiologie, bei der Daten, die mit verschiedenen Methoden gewonnen wurden \u2013 Kryo-Elektronenmikroskopie, R\u00f6ntgenkristallographie, Massenspektrometrie und Berechnungsmethoden \u2013 \u00fcbereinander gelegt wurden, um ein koh\u00e4rentes Modell zu erstellen. Der in der vorliegenden Studie angewandte Arbeitsansatz ist auf die Zusammenarbeit mit verschiedenen Forschungsgruppen und Institutionen abgestimmt, die im Hamburger Zentrum f\u00fcr Strukturelle Systembiologie (CSSB) zusammenarbeiten.<\/p>\n\n\n\n

“Vor achtzehn Monaten sah die L\u00f6sung dieser Struktur wie eine \u201aMission: impossible\u2018 aus”, sagt Matthias Wilmanns. “Wir haben es geschafft, die Puzzlest\u00fccke zusammenzusetzen, weil jedes Teammitglied einzigartige Expertise beisteuerte. Um die komplette Struktur zu l\u00f6sen, arbeiteten wir mit Jan Kosinskis Gruppe am EMBL Hamburg und dem Zentrum f\u00fcr Strukturelle Systembiologie<\/a> zusammen, die die notwendige Expertise in integrativer Strukturbiologie beisteuerten. Gro\u00dfe Hilfe erhielten wir auch von unseren Kollegen am EMBL Heidelberg, die kryo-elektronenmikroskopische Experimente durchf\u00fchrten.”<\/p>\n\n\n\n

Diese Studie veranschaulicht einige der Ans\u00e4tze, die das EMBL im Rahmen seines kommenden wissenschaftlichen Programms “Molecules to Ecosystems 2022-2026” in der lebenswissenschaftlichen Forschung verfolgt. Im Rahmen dieses Programms wird das EMBL einen interdisziplin\u00e4ren Ansatz verfolgen, um die molekularen Grundlagen des Lebens im Kontext von Umweltver\u00e4nderungen zu verstehen. Dies wird das translationales Potenzial bieten, Fortschritte in der globalen Gesundheits- und Umweltforschung zu unterst\u00fctzen.<\/p>\n","protected":false},"excerpt":{"rendered":"

EMBL Hamburg\u2019s Wilmanns and Kosinski groups have determined the detailed structure of a bacterial protein complex critical for tuberculosis infection.<\/p>\n","protected":false},"author":96,"featured_media":39706,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[718,775,1704,53,3684,928,876,540,35,764,306],"embl_taxonomy":[9596,19307,19403],"class_list":["post-39456","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-cryo-em","tag-cssb","tag-embl-programme","tag-hamburg","tag-infection-biology","tag-infectious-disease","tag-integrative-modelling","tag-kosinski","tag-structural-biology","tag-tuberculosis","tag-wilmanns","embl_taxonomy-embl-hamburg","embl_taxonomy-kosinski-group","embl_taxonomy-wilmanns-group"],"acf":{"featured":true,"show_featured_image":false,"article_intro":"

EMBL Hamburg\u2019s Wilmanns and Kosinski groups have determined the detailed structure of a bacterial protein complex critical for tuberculosis infection<\/p>\n","related_links":[{"link_description":"Wilmanns Group","link_url":"https:\/\/www.embl.org\/groups\/wilmanns\/"},{"link_description":"Kosi\u0144ski Group","link_url":"https:\/\/www.embl.org\/groups\/kosinski\/"},{"link_description":"Structure of key system for TB infection ","link_url":"https:\/\/www.embl.org\/news\/science\/1704-structure-key-system-tb-infection-revealed\/"}],"source_article":[{"publication_title":"Structure of the mycobacterial ESX-5 type VII secretion system pore complex","publication_link":{"title":"","url":"https:\/\/www.science.org\/doi\/10.1126\/sciadv.abg9923","target":"_blank"},"publication_authors":"Beckham K. S. H., et al.","publication_source":"Science advances","publication_date":"25 June 2021","publication_doi":"10.1126\/sciadv.abg9923"}],"in_this_article":false,"press_contact":"EMBL Generic","vf_locked":false,"field_target_display":""},"embl_taxonomy_terms":[{"uuid":"a:3:{i:0;s:36:\"b14d3f13-5670-44fb-8970-e54dfd9c921a\";i:1;s:36:\"89e00fee-87f4-482e-a801-4c3548bb6a58\";i:2;s:36:\"613c4de5-1775-447f-af71-4b07085318e9\";}","parents":[],"name":["EMBL Hamburg"],"slug":"embl-hamburg","description":"Where > All EMBL sites > EMBL Hamburg"},{"uuid":"a:3:{i:0;s:36:\"302cfdf7-365b-462a-be65-82c7b783ebf7\";i:1;s:36:\"2dc39890-6c01-47bf-ac78-d42abdb10079\";i:2;s:36:\"5cf17219-ae78-437e-85e4-aad17a7c5e0f\";}","parents":[],"name":["Kosinski Group"],"slug":"kosinski-group","description":"What > Structural Biology (EMBL Hamburg) > Kosinski Group"},{"uuid":"a:3:{i:0;s:36:\"302cfdf7-365b-462a-be65-82c7b783ebf7\";i:1;s:36:\"2dc39890-6c01-47bf-ac78-d42abdb10079\";i:2;s:36:\"b7081976-e7c1-4678-ab00-3e02d20e9e87\";}","parents":[],"name":["Wilmanns Group"],"slug":"wilmanns-group","description":"What > Structural Biology (EMBL Hamburg) > Wilmanns Group"}],"yoast_head":"\nStructural biology reveals new opportunities to combat tuberculosis | EMBL<\/title>\n<meta name=\"description\" content=\"EMBL Hamburg\u2019s Wilmanns group has determined the detailed structure of a bacterial protein secretion complex critical for tuberculosis infection\" \/>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Structural biology reveals new opportunities to combat tuberculosis | EMBL\" \/>\n<meta property=\"og:description\" content=\"EMBL Hamburg\u2019s Wilmanns group has determined the detailed structure of a bacterial protein secretion complex critical for tuberculosis infection\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/\" \/>\n<meta property=\"og:site_name\" content=\"EMBL\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/embl.org\/\" \/>\n<meta property=\"article:published_time\" content=\"2021-06-25T18:00:00+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2024-03-22T10:17:50+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg\" \/>\n\t<meta property=\"og:image:width\" content=\"1000\" \/>\n\t<meta property=\"og:image:height\" content=\"600\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/jpeg\" \/>\n<meta name=\"author\" content=\"Dorota Badowska\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:creator\" content=\"@d_badowska\" \/>\n<meta name=\"twitter:site\" content=\"@embl\" \/>\n<meta name=\"twitter:label1\" content=\"Written by\" \/>\n\t<meta name=\"twitter:data1\" content=\"Dorota Badowska\" \/>\n\t<meta name=\"twitter:label2\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data2\" content=\"7 minutes\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\/\/schema.org\",\"@graph\":[{\"@type\":\"NewsArticle\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/\"},\"author\":{\"name\":\"Dorota Badowska\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/b8ae50efcd7533f0ab2ec368736b1d04\"},\"headline\":\"Structural biology reveals new opportunities to combat tuberculosis\",\"datePublished\":\"2021-06-25T18:00:00+00:00\",\"dateModified\":\"2024-03-22T10:17:50+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/\"},\"wordCount\":1580,\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg\",\"keywords\":[\"cryo-em\",\"cssb\",\"embl programme\",\"hamburg\",\"infection biology\",\"infectious disease\",\"integrative modelling\",\"kosinski\",\"structural biology\",\"tuberculosis\",\"wilmanns\"],\"articleSection\":[\"Science\",\"Science & Technology\"],\"inLanguage\":\"en-US\"},{\"@type\":\"WebPage\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/\",\"url\":\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/\",\"name\":\"Structural biology reveals new opportunities to combat tuberculosis | EMBL\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/#website\"},\"primaryImageOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/#primaryimage\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg\",\"datePublished\":\"2021-06-25T18:00:00+00:00\",\"dateModified\":\"2024-03-22T10:17:50+00:00\",\"description\":\"EMBL Hamburg\u2019s Wilmanns group has determined the detailed structure of a bacterial protein secretion complex critical for tuberculosis infection\",\"inLanguage\":\"en-US\",\"potentialAction\":[{\"@type\":\"ReadAction\",\"target\":[\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/\"]}]},{\"@type\":\"ImageObject\",\"inLanguage\":\"en-US\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/#primaryimage\",\"url\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg\",\"contentUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg\",\"width\":1000,\"height\":600,\"caption\":\"The mycobacterial ESX-5 secretion system is located in the bacterial inner membrane and consists of six units, which assemble into a symmetrical structure with a pore at the centre. Credit: Isabel Romero Calvo\/EMBL\"},{\"@type\":\"WebSite\",\"@id\":\"https:\/\/www.embl.org\/news\/#website\",\"url\":\"https:\/\/www.embl.org\/news\/\",\"name\":\"European Molecular Biology Laboratory News\",\"description\":\"News from the European Molecular Biology Laboratory\",\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"alternateName\":\"EMBL News\",\"potentialAction\":[{\"@type\":\"SearchAction\",\"target\":{\"@type\":\"EntryPoint\",\"urlTemplate\":\"https:\/\/www.embl.org\/news\/?s={search_term_string}\"},\"query-input\":{\"@type\":\"PropertyValueSpecification\",\"valueRequired\":true,\"valueName\":\"search_term_string\"}}],\"inLanguage\":\"en-US\"},{\"@type\":\"Organization\",\"@id\":\"https:\/\/www.embl.org\/news\/#organization\",\"name\":\"European Molecular Biology Laboratory\",\"alternateName\":\"EMBL\",\"url\":\"https:\/\/www.embl.org\/news\/\",\"logo\":{\"@type\":\"ImageObject\",\"inLanguage\":\"en-US\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/logo\/image\/\",\"url\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2025\/09\/EMBL_logo_colour-1-300x144-1.png\",\"contentUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2025\/09\/EMBL_logo_colour-1-300x144-1.png\",\"width\":300,\"height\":144,\"caption\":\"European Molecular Biology Laboratory\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/logo\/image\/\"},\"sameAs\":[\"https:\/\/www.facebook.com\/embl.org\/\",\"https:\/\/x.com\/embl\",\"https:\/\/www.instagram.com\/embl_org\/\",\"https:\/\/www.linkedin.com\/company\/15813\/\",\"https:\/\/www.youtube.com\/user\/emblmedia\/\"]},{\"@type\":\"Person\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/b8ae50efcd7533f0ab2ec368736b1d04\",\"name\":\"Dorota Badowska\",\"image\":{\"@type\":\"ImageObject\",\"inLanguage\":\"en-US\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/image\/\",\"url\":\"https:\/\/secure.gravatar.com\/avatar\/71b761203da9931cfcd018d7d980d858eaf63f8ff17a65ddf17171da6835e105?s=96&d=mm&r=g\",\"contentUrl\":\"https:\/\/secure.gravatar.com\/avatar\/71b761203da9931cfcd018d7d980d858eaf63f8ff17a65ddf17171da6835e105?s=96&d=mm&r=g\",\"caption\":\"Dorota Badowska\"},\"description\":\"Endlessly curious science communicator. Neuroscientist in past life.\",\"sameAs\":[\"linkedin.com\/in\/dorotabadowska\",\"https:\/\/x.com\/d_badowska\"],\"url\":\"https:\/\/www.embl.org\/news\/author\/dorota-badowskaembl-hamburg-de\/\"}]}<\/script>\n<!-- \/ Yoast SEO plugin. -->","yoast_head_json":{"title":"Structural biology reveals new opportunities to combat tuberculosis | EMBL","description":"EMBL Hamburg\u2019s Wilmanns group has determined the detailed structure of a bacterial protein secretion complex critical for tuberculosis infection","robots":{"index":"index","follow":"follow","max-snippet":"max-snippet:-1","max-image-preview":"max-image-preview:large","max-video-preview":"max-video-preview:-1"},"canonical":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/","og_locale":"en_US","og_type":"article","og_title":"Structural biology reveals new opportunities to combat tuberculosis | EMBL","og_description":"EMBL Hamburg\u2019s Wilmanns group has determined the detailed structure of a bacterial protein secretion complex critical for tuberculosis infection","og_url":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/","og_site_name":"EMBL","article_publisher":"https:\/\/www.facebook.com\/embl.org\/","article_published_time":"2021-06-25T18:00:00+00:00","article_modified_time":"2024-03-22T10:17:50+00:00","og_image":[{"width":1000,"height":600,"url":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg","type":"image\/jpeg"}],"author":"Dorota Badowska","twitter_card":"summary_large_image","twitter_creator":"@d_badowska","twitter_site":"@embl","twitter_misc":{"Written by":"Dorota Badowska","Est. reading time":"7 minutes"},"schema":{"@context":"https:\/\/schema.org","@graph":[{"@type":"NewsArticle","@id":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/#article","isPartOf":{"@id":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/"},"author":{"name":"Dorota Badowska","@id":"https:\/\/www.embl.org\/news\/#\/schema\/person\/b8ae50efcd7533f0ab2ec368736b1d04"},"headline":"Structural biology reveals new opportunities to combat tuberculosis","datePublished":"2021-06-25T18:00:00+00:00","dateModified":"2024-03-22T10:17:50+00:00","mainEntityOfPage":{"@id":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/"},"wordCount":1580,"publisher":{"@id":"https:\/\/www.embl.org\/news\/#organization"},"image":{"@id":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/#primaryimage"},"thumbnailUrl":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg","keywords":["cryo-em","cssb","embl programme","hamburg","infection biology","infectious disease","integrative modelling","kosinski","structural biology","tuberculosis","wilmanns"],"articleSection":["Science","Science & Technology"],"inLanguage":"en-US"},{"@type":"WebPage","@id":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/","url":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/","name":"Structural biology reveals new opportunities to combat tuberculosis | EMBL","isPartOf":{"@id":"https:\/\/www.embl.org\/news\/#website"},"primaryImageOfPage":{"@id":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/#primaryimage"},"image":{"@id":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/#primaryimage"},"thumbnailUrl":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg","datePublished":"2021-06-25T18:00:00+00:00","dateModified":"2024-03-22T10:17:50+00:00","description":"EMBL Hamburg\u2019s Wilmanns group has determined the detailed structure of a bacterial protein secretion complex critical for tuberculosis infection","inLanguage":"en-US","potentialAction":[{"@type":"ReadAction","target":["https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/"]}]},{"@type":"ImageObject","inLanguage":"en-US","@id":"https:\/\/www.embl.org\/news\/science\/structural-biology-reveals-new-opportunities-to-combat-tuberculosis\/#primaryimage","url":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg","contentUrl":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg","width":1000,"height":600,"caption":"The mycobacterial ESX-5 secretion system is located in the bacterial inner membrane and consists of six units, which assemble into a symmetrical structure with a pore at the centre. Credit: Isabel Romero Calvo\/EMBL"},{"@type":"WebSite","@id":"https:\/\/www.embl.org\/news\/#website","url":"https:\/\/www.embl.org\/news\/","name":"European Molecular Biology Laboratory News","description":"News from the European Molecular Biology Laboratory","publisher":{"@id":"https:\/\/www.embl.org\/news\/#organization"},"alternateName":"EMBL News","potentialAction":[{"@type":"SearchAction","target":{"@type":"EntryPoint","urlTemplate":"https:\/\/www.embl.org\/news\/?s={search_term_string}"},"query-input":{"@type":"PropertyValueSpecification","valueRequired":true,"valueName":"search_term_string"}}],"inLanguage":"en-US"},{"@type":"Organization","@id":"https:\/\/www.embl.org\/news\/#organization","name":"European Molecular Biology Laboratory","alternateName":"EMBL","url":"https:\/\/www.embl.org\/news\/","logo":{"@type":"ImageObject","inLanguage":"en-US","@id":"https:\/\/www.embl.org\/news\/#\/schema\/logo\/image\/","url":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2025\/09\/EMBL_logo_colour-1-300x144-1.png","contentUrl":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2025\/09\/EMBL_logo_colour-1-300x144-1.png","width":300,"height":144,"caption":"European Molecular Biology Laboratory"},"image":{"@id":"https:\/\/www.embl.org\/news\/#\/schema\/logo\/image\/"},"sameAs":["https:\/\/www.facebook.com\/embl.org\/","https:\/\/x.com\/embl","https:\/\/www.instagram.com\/embl_org\/","https:\/\/www.linkedin.com\/company\/15813\/","https:\/\/www.youtube.com\/user\/emblmedia\/"]},{"@type":"Person","@id":"https:\/\/www.embl.org\/news\/#\/schema\/person\/b8ae50efcd7533f0ab2ec368736b1d04","name":"Dorota Badowska","image":{"@type":"ImageObject","inLanguage":"en-US","@id":"https:\/\/www.embl.org\/news\/#\/schema\/person\/image\/","url":"https:\/\/secure.gravatar.com\/avatar\/71b761203da9931cfcd018d7d980d858eaf63f8ff17a65ddf17171da6835e105?s=96&d=mm&r=g","contentUrl":"https:\/\/secure.gravatar.com\/avatar\/71b761203da9931cfcd018d7d980d858eaf63f8ff17a65ddf17171da6835e105?s=96&d=mm&r=g","caption":"Dorota Badowska"},"description":"Endlessly curious science communicator. Neuroscientist in past life.","sameAs":["linkedin.com\/in\/dorotabadowska","https:\/\/x.com\/d_badowska"],"url":"https:\/\/www.embl.org\/news\/author\/dorota-badowskaembl-hamburg-de\/"}]}},"field_target_display":"","field_article_language":{"value":"english","label":"English"},"fimg_url":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg","featured_image_src":"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2021\/06\/20210622_ESX5-illustration_v3_IRC.jpg","_links":{"self":[{"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/posts\/39456","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/users\/96"}],"replies":[{"embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/comments?post=39456"}],"version-history":[{"count":33,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/posts\/39456\/revisions"}],"predecessor-version":[{"id":67219,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/posts\/39456\/revisions\/67219"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/media\/39706"}],"wp:attachment":[{"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/media?parent=39456"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/categories?post=39456"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/tags?post=39456"},{"taxonomy":"embl_taxonomy","embeddable":true,"href":"https:\/\/www.embl.org\/news\/wp-json\/wp\/v2\/embl_taxonomy?post=39456"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}