{"id":70921,"date":"2024-10-15T11:47:00","date_gmt":"2024-10-15T09:47:00","guid":{"rendered":"https:\/\/www.embl.org\/news\/?p=70921"},"modified":"2025-03-15T23:02:15","modified_gmt":"2025-03-15T22:02:15","slug":"vitamin-b1s-journey-in-your-body-and-why-it-matters","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science-technology\/vitamin-b1s-journey-in-your-body-and-why-it-matters\/","title":{"rendered":"Vitamin B1\u2019s journey in your body, and why it matters"},"content":{"rendered":"\n<article class=\"vf-card vf-card--brand vf-card--bordered vf-u-margin__bottom--800\" default>\n  <div class=\"vf-card__content | vf-stack vf-stack--400\">\n      <h3 class=\"vf-card__heading\">\n      Summary    <\/h3>\n                <p class=\"vf-card__text\"><ul>\r\n \t<li>Vitamin B<sub>1<\/sub> deficiencies can have devastating health consequences.<\/li>\r\n \t<li>EMBL Hamburg\u2019s L\u00f6w Group provided detailed molecular insights into how specialised transporter proteins enable vitamin B<sub>1<\/sub> to cross membranes in our body to reach vital tissues and organs.<\/li>\r\n \t<li>They identified several common drugs that disrupt vitamin B<sub>1 <\/sub>transport, potentially causing deficiency of this nutrient in the brain despite normal blood levels. The finding could help prevent this side effect in the future.<\/li>\r\n \t<li>The study offers also new insights into rare diseases of the nervous system caused by impaired B<sub>1<\/sub> transport.<\/li>\r\n<\/ul><\/p>\n      <\/div>\n<\/article>\n\n\n\n\n<p>Vitamin B<sub>1<\/sub>, also known as thiamine, is essential for the survival of our cells. The human body can\u2019t produce it, but we can maintain healthy levels of this vitamin by eating foods like salmon, legumes, and brown rice. Doing this is crucial, because B<sub>1<\/sub> deficiency can cause serious dysfunctions of the cardiovascular and central nervous systems, disability, and even death.<\/p>\n\n\n\n<p>However, sometimes, B<sub>1 <\/sub>deficiency may develop in the brain and other vital organs as a side effect of some drugs. This can happen despite normal B<sub>1<\/sub> levels in the blood, which often makes such deficiencies go undetected before it\u2019s too late.<\/p>\n\n\n\n<p>To understand what\u2019s behind such hidden deficiencies, the L\u00f6w Group at EMBL Hamburg and <a href=\"https:\/\/www.cssb-hamburg.de\/\" target=\"_blank\" rel=\"noreferrer noopener\">CSSB<\/a> and collaborators at <a href=\"https:\/\/csb.sites.vib.be\/en\" target=\"_blank\" rel=\"noreferrer noopener\">VIB-VUB Center for Structural Biology<\/a> used structural biology and biophysical techniques to investigate how vitamin B<sub>1<\/sub> travels in our body to reach different tissues, and what factors can hinder its progress.<\/p>\n\n\n\n<h2 class=\"wp-block-heading\" id=\"a1\"><strong>Vitamin B<sub>1<\/sub>\u2019s hurdle run<\/strong><\/h2>\n\n\n\n<p>On its journey from the gut to the body\u2019s cells, vitamin B<sub>1<\/sub> must pass through several membranes, which act as barriers \u2013 starting with the gut wall, then blood vessels, organs, and finally, the membranes of individual cells. The most stringent of these is the blood-brain barrier, which seals the brain off from toxins that might enter from the bloodstream. However, the barrier also makes it difficult for essential nutrients, including vitamins, to cross.<\/p>\n\n\n\n<p>To allow vitamins and other nutrients to reach cells throughout the body, these membranes are equipped with specialised transporter molecules that let them pass. In vitamin B<sub>1<\/sub>\u2019s case, this job is done mostly by two transporters: SLC19A2 and SLC19A3. While we know these transporters are important for human health, it has been unclear how exactly they work on the molecular level.<\/p>\n\n\n\n<p>To uncover this, the L\u00f6w Group investigated SLC19A3, the transporter essential for getting B<sub>1<\/sub> across the gut wall and the blood-brain barrier \u2013 two crucial steps in the vitamin&#8217;s journey.<\/p>\n\n\n\n<p>To observe the transporter in action, they created a \u2018molecular movie\u2019 by putting together a series of snapshots obtained with cryo-electron microscopy (cryo-EM).<\/p>\n\n\n\n<p>\u201cWith this, we could capture the dynamics of the transport process and visualise molecular details of how the transporter recognises and pushes the B<sub>1<\/sub> molecule across the cell membrane,\u201d said Christian L\u00f6w, Group Leader and corresponding author of the study.<\/p>\n\n\n\n<div class=\"vf-embed vf-embed--16x9 | vf-u-margin__bottom--400\">\n<iframe src=\"https:\/\/www.youtube.com\/embed\/JebMa72e1Ms?si=QOaUyRmIHlKc2bds\" frameborder=\"0\" controls allowfullscreen><\/iframe><\/div>\n\n  \n<figcaption class=\"vf-figure__caption vf-u-margin__top--200\">Transport cycle of the human vitamin B<sub>1<\/sub> transporter protein SLC19A3. The two domains of the protein, shown in light purple and light blue, create a moving barrier around the substrate thiamine (vitamin B<sub>1<\/sub>), shown in orange. Operating like a molecular sluice, SLC19A3 manages the efficient and specific transport of vitamin B<sub>1<\/sub> throughout the body. Credit: Florian Gabriel, Dorota Badowska\/EMBL.<\/figcaption>\n\n\n\n\n\n<h2 class=\"wp-block-heading\" id=\"a2\"><strong>Insights into rare diseases<\/strong><\/h2>\n\n\n\n<p>The molecular snapshots enabled the scientists to determine which parts of the SLC19A3 transporter are the most critical for it to work correctly. If these parts malfunction, the transporter won\u2019t work.<\/p>\n\n\n\n<p>This explains why mutations in these critical parts impair B<sub>1<\/sub> transport to the brain and lead to severe neurological symptoms. These <a href=\"https:\/\/www.orpha.net\/en\/disease\/list\/gene\/SLC19A3?orpha=118766&amp;name=SLC19A3&amp;mode=gene\" target=\"_blank\" rel=\"noreferrer noopener\">rare conditions<\/a>, which start manifesting symptoms in infancy, are treated with high doses of B<sub>1<\/sub> and other compounds. Despite this, one in 20 patients die and nearly one-third still suffer from symptoms.<\/p>\n\n\n\n<p>To investigate this, the scientists created a version of the SLC19A3 transporter carrying a mutation that causes a severe brain disease called <a href=\"https:\/\/www.orpha.net\/en\/disease\/detail\/65284?name=SLC19A3&amp;mode=gene\" target=\"_blank\" rel=\"noreferrer noopener\">BTBGD<\/a>. This let them observe exactly how the mutation affects the transporter\u2019s molecular structure and makes it unreceptive to B<sub>1<\/sub>. Understanding this disease-causing mechanism might help to design more effective treatments for BTBGD in the future.<\/p>\n\n\n\n<h2 class=\"wp-block-heading\" id=\"a3\"><strong>Drugs that can cause hidden B<sub>1<\/sub> deficiencies<\/strong><\/h2>\n\n\n\n<p>Severe B<sub>1<\/sub> deficiency symptoms can be caused not only by rare mutations, but also by some medications. Several commonly prescribed drugs, including some antidepressants, antibiotics, and oncological medications, impair SLC19A3. This can potentially lead to dangerous B<sub>1<\/sub> deficiencies throughout the body or in specific organs or tissues.<\/p>\n\n\n\n<p>Brain-specific deficiencies are especially dangerous because they can occur even when our blood levels of B<sub>1<\/sub> are normal, making them undetectable by standard blood tests. This hidden deficiency can quietly lead to serious, potentially fatal brain dysfunction.<\/p>\n\n\n\n<p>\u201cWhile medicine already knows a few drugs that have the potential to cause hidden B<sub>1<\/sub> deficiencies, there may be many more that we\u2019re unaware of,\u201d said Florian Gabriel, PhD student at EMBL Hamburg and the first author of the study. \u201cIdentifying them isn\u2019t straightforward, so our research aimed to make it easier. We\u2019ve uncovered the molecular basis of how drug molecules block the SLC19A3 transporter and we are currently using that knowledge to screen all <a href=\"https:\/\/www.fda.gov\/\" target=\"_blank\" rel=\"noreferrer noopener\">FDA<\/a>&#8211; and <a href=\"https:\/\/www.ema.europa.eu\/en\/homepage\" target=\"_blank\" rel=\"noreferrer noopener\">EMA<\/a>-approved drugs for similar effects.\u201d<\/p>\n\n\n\n<p>The L\u00f6w Group also identified the structural features that make a drug likely to impair B<sub>1<\/sub> transport. To do this, they used cryo-EM and biophysical techniques to analyse how known blockers interact with SLC19A3.<\/p>\n\n\n\n<p>Using this knowledge, they have identified seven new drugs that block the B<sub>1<\/sub> transporter <em>in vitro<\/em> and are likely to do it in the human body as well. These include several antidepressants, the antiparasitic hydroxychloroquine, and three cancer drugs.<\/p>\n\n\n\n<p>While these findings still need to be confirmed in humans, they are a first step to protect patients from potentially dangerous drug-induced B<sub>1<\/sub> deficiencies in the future.<\/p>\n\n\n\n<p>\u201cThese results will not only help to better monitor the health of patients taking those drugs, but might also help to design new drugs in the future that won\u2019t have this side effect,\u201d said L\u00f6w. \u201cWe believe our work could also create a basis for studying how medicines interact with similar transporters in the human body. In the long term, it might also guide the design of future drugs that could use those transporters to reach target organs more efficiently.\u201d<\/p>\n\n\n\n<p>For solving the structures of the SLC19A3 transporter, the L\u00f6w Group used the state-of-the-art cryo-EM facilities at the <a href=\"https:\/\/www.cssb-hamburg.de\/facilities\/cryo_em\/index_eng.html\" target=\"_blank\" rel=\"noreferrer noopener\">CSSB<\/a> in Hamburg and the <a href=\"https:\/\/www.embl.org\/about\/info\/imaging-centre\/\">EMBL Imaging Centre<\/a> in Heidelberg. Critical biophysical experiments were performed at EMBL Hamburg\u2019s <a href=\"https:\/\/www.embl.org\/groups\/sample-preparation-characterisation\/\">Sample Preparation and Characterisation Facility<\/a>.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>EMBL Hamburg scientists have gained molecular insights into how we absorb vitamin B1 \u2013 a mechanism with implications for disease and drug development.<\/p>\n","protected":false},"author":96,"featured_media":70925,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[17591],"tags":[65,17279,775,53,793,461,5686,5744,35],"embl_taxonomy":[18857,9596,19325],"class_list":["post-70921","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science-technology","tag-biophysics","tag-cryo-electron-microscopy","tag-cssb","tag-hamburg","tag-imaging-centre","tag-low","tag-rare-disease","tag-sample-preparation-and-characterisation-facility","tag-structural-biology","embl_taxonomy-christian-loew","embl_taxonomy-embl-hamburg","embl_taxonomy-low-group-visiting"],"acf":{"featured":true,"show_featured_image":false,"field_target_display":"embl","field_article_language":{"value":"english","label":"English"},"article_intro":"<p>EMBL Hamburg and CSSB scientists have uncovered the molecular details of how we absorb vitamin B<sub>1<\/sub>, paving the way to preventing dangerous hidden B<sub>1<\/sub> deficiencies in patients<\/p>\n","related_links":[{"link_description":"L\u00f6w Group","link_url":"https:\/\/www.embl.org\/groups\/loew\/"},{"link_description":"The secret of molecular promiscuity","link_url":"https:\/\/www.embl.org\/news\/embletc\/issue-101\/the-secret-of-molecular-promiscuity\/"},{"link_description":"Structure of a promiscuous protein will help scientists design better drugs","link_url":"https:\/\/www.embl.org\/news\/science\/structure-of-promiscuous-protein-will-help-scientists-design-better-drugs\/"}],"source_article":[{"publication_title":"Structural basis of thiamine transport and drug recognition by SLC19A3.","publication_link":{"title":"","url":"https:\/\/www.nature.com\/articles\/s41467-024-52872-8","target":"_blank"},"publication_authors":"Gabriel F., Spriestersbach L., Fuhrmann A. et al.","publication_source":"Nature Communications","publication_date":"2 October 2024","publication_doi":"10.1038\/s41467-024-52872-8"}],"in_this_article":[{"heading_description":"Vitamin B1\u2019s hurdle run","anchor":"#a1"},{"heading_description":"Insights into rare diseases","anchor":"#a2"},{"heading_description":"Drugs that can cause hidden B1 deficiencies","anchor":"#a3"}],"press_contact":"EMBL Generic","article_translations":false,"languages":"","vf_locked":false,"vfwp-news_embl_taxonomy":[9596,18857,19325]},"embl_taxonomy_terms":[{"uuid":"a:2:{i:0;s:36:\"4428d1fd-441a-4d6d-a1c5-5dcf5665f213\";i:1;s:36:\"5dc558bb-6e73-4760-8a1b-597f6dab7d01\";}","parents":[],"name":["Christian Loew"],"slug":"christian-loew","description":"Who &gt; 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On its way from the gut to the cells throughout the body, vitamin B1 must cross several cell membranes. One of the most critical hurdles for B1 is the blood-brain barrier. EMBL Hamburg\u2019s L\u00f6w Group has provided detailed molecular insights into how vitamin B1 overcomes these obstacles. 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