{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T06:31:57Z","timestamp":1772087517217,"version":"3.50.1"},"reference-count":63,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2026,2,24]],"date-time":"2026-02-24T00:00:00Z","timestamp":1771891200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001677","name":"Institut national de la sant\u00e9 et de la recherche m\u00e9dicale","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100001677","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Institut Pasteur and Centre national de la recherche scientifique"},{"name":"Direction g\u00e9n\u00e9rale de l\u2019armement (DGA)-MRIS"},{"name":"Agence de l\u2019innovation de d\u00e9fense (AID) PhD fellowship"},{"name":"Institut Pasteur"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Botulinum neurotoxins (BoNTs), among the most potent biological toxins, rely on co-produced nontoxic proteins to survive harsh gastrointestinal conditions and achieve efficient systemic dissemination after oral exposure. Recent structural and functional studies have revealed how BoNTs bind to the nontoxic non-hemagglutinin (NTNH) factors to engage in interactions with either OrfXs\/P47 or hemagglutinins (HAs) components for systemic dissemination. This review synthesizes recent findings that elucidate the molecular basis of NTNH-specific anchoring to the HA70 triskelion-like element or to the host protease-activated form of OrfX2, thereby highlighting divergent pathways that enhance oral toxicity. We also discuss current perspectives on the molecular mechanisms through which BoNTs, in cooperation with associated nontoxic proteins, are absorbed from the intestine.<\/jats:p>","DOI":"10.3390\/toxins18030116","type":"journal-article","created":{"date-parts":[[2026,2,24]],"date-time":"2026-02-24T08:54:56Z","timestamp":1771923296000},"page":"116","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["From Gut to Systemic Circulation: Molecular Strategies of Botulinum Neurotoxin Complexes"],"prefix":"10.3390","volume":"18","author":[{"given":"Juliette","family":"Mondy","sequence":"first","affiliation":[{"name":"D\u00e9partement de Microbiologie, Unit\u00e9 des Toxines Bact\u00e9riennes, Institut Pasteur, CNRS UMR6047, INSERM U1306, Universit\u00e9 Paris Cit\u00e9, Paris 75015, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9080-7761","authenticated-orcid":false,"given":"Emmanuel","family":"Lemichez","sequence":"additional","affiliation":[{"name":"D\u00e9partement de Microbiologie, Unit\u00e9 des Toxines Bact\u00e9riennes, Institut Pasteur, CNRS UMR6047, INSERM U1306, Universit\u00e9 Paris Cit\u00e9, Paris 75015, France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2026,2,24]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"e70187","DOI":"10.1111\/jnc.70187","article-title":"Botulinum Neurotoxins: History, Mechanism, and Applications. A Narrative Review","volume":"169","author":"Monash","year":"2025","journal-title":"J. Neurochem."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Rasetti-Escargueil, C., Lemichez, E., and Popoff, M.R. (2020). Human Botulism in France, 1875\u20132016. Toxins, 12.","DOI":"10.3390\/toxins12050338"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"104055","DOI":"10.1016\/j.fm.2022.104055","article-title":"Synergistic interaction between pH and NaCl in the limits of germination and outgrowth of Clostridium sporogenes and Group I Clostridium botulinum vegetative cells and spores after heat treatment","volume":"106","author":"Boix","year":"2022","journal-title":"Food Microbiol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1001\/jama.285.8.1059","article-title":"Botulinum toxin as a biological weapon: Medical and public health management","volume":"285","author":"Arnon","year":"2001","journal-title":"JAMA"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Dilena, R., Pozzato, M., Baselli, L., Chidini, G., Barbieri, S., Scalfaro, C., Finazzi, G., Lonati, D., Locatelli, C.A., and Cappellari, A. (2021). Infant Botulism: Checklist for Timely Clinical Diagnosis and New Possible Risk Factors Originated from a Case Report and Literature Review. Toxins, 13.","DOI":"10.3390\/toxins13120860"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1128\/aem.38.2.216-218.1979","article-title":"Bile Acid Inhibition of Clostridium Botulinum","volume":"38","author":"Huhtanen","year":"1979","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"221","DOI":"10.7326\/0003-4819-129-3-199808010-00011","article-title":"Botulism in the United States: A clinical and epidemiologic review","volume":"129","author":"Shapiro","year":"1998","journal-title":"Ann. Intern. Med."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1093\/oxfordjournals.aje.a121239","article-title":"Botulism in the United States. 1899\u20131969","volume":"93","author":"Gangarosa","year":"1971","journal-title":"Am. J. Epidemiol."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Parrera, G.S., Astacio, H., Tunga, P., Anderson, D.M., Hall, C.L., and Richardson, J.S. (2021). Use of Botulism Antitoxin Heptavalent (A, B, C, D, E, F, G)-(Equine) (BAT\u00ae) in Clinical Study Subjects and Patients: A 15-Year Systematic Safety Review. Toxins, 14.","DOI":"10.3390\/toxins14010019"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1128\/mr.46.1.86-94.1982","article-title":"Bacterial toxins: A table of lethal amounts","volume":"46","author":"Gill","year":"1982","journal-title":"Microbiol. Rev."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1016\/j.toxicon.2009.01.015","article-title":"Development of future indications for BOTOX","volume":"54","author":"Brin","year":"2009","journal-title":"Toxicon"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Smith, T.J., Williamson, C.H.D., Hill, K.K., Johnson, S.L., Xie, G., Anniballi, F., Auricchio, B., Fern\u00e1ndez, R.A., Caballero, P.A., and Keim, P. (2021). The Distinctive Evolution of orfX Clostridium parabotulinum Strains and Their Botulinum Neurotoxin Type A and F Gene Clusters Is Influenced by Environmental Factors and Gene Interactions via Mobile Genetic Elements. Front. Microbiol., 12.","DOI":"10.3389\/fmicb.2021.566908"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Peck, M.W., Smith, T.J., Anniballi, F., Austin, J.W., Bano, L., Bradshaw, M., Cuervo, P., Cheng, L.W., Derman, Y., and Dorner, B.G. (2017). Historical Perspectives and Guidelines for Botulinum Neurotoxin Subtype Nomenclature. Toxins, 9.","DOI":"10.3390\/toxins9010038"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1007\/164_2019_342","article-title":"The Structure and Classification of Botulinum Toxins","volume":"263","author":"Dong","year":"2021","journal-title":"Handb. Exp. Pharmacol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2869","DOI":"10.1038\/s41467-019-10732-w","article-title":"A neurotoxin that specifically targets Anopheles mosquitoes","volume":"10","author":"Contreras","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"e02131-14","DOI":"10.1128\/mBio.02131-14","article-title":"On botulinum neurotoxin variability","volume":"6","author":"Montecucco","year":"2015","journal-title":"mBio"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"e0310623","DOI":"10.1128\/mbio.03106-23","article-title":"Botulinum neurotoxin X lacks potency in mice and in human neurons","volume":"15","author":"Gregg","year":"2024","journal-title":"mBio"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"14130","DOI":"10.1038\/ncomms14130","article-title":"Identification and characterization of a novel botulinum neurotoxin","volume":"8","author":"Zhang","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1038\/s42004-024-01262-8","article-title":"Activity of botulinum neurotoxin X and its structure when shielded by a non-toxic non-hemagglutinin protein","volume":"7","author":"Lee","year":"2024","journal-title":"Commun. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1038\/2338","article-title":"Crystal structure of botulinum neurotoxin type A and implications for toxicity","volume":"5","author":"Lacy","year":"1998","journal-title":"Nat. Struct. Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/j.tibs.2005.05.002","article-title":"SNARE complexes and neuroexocytosis: How many, how close","volume":"30","author":"Montecucco","year":"2005","journal-title":"Trends Biochem. Sci."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"29604","DOI":"10.1074\/jbc.M703619200","article-title":"Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes","volume":"282","author":"Fischer","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"e112095","DOI":"10.15252\/embj.2022112095","article-title":"Presynaptic targeting of botulinum neurotoxin type A requires a tripartite PSG-Syt1-SV2 plasma membrane nanocluster for synaptic vesicle entry","volume":"42","author":"Joensuu","year":"2023","journal-title":"EMBO J."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.toxicon.2020.02.006","article-title":"Neuronal selectivity of botulinum neurotoxins","volume":"178","author":"Poulain","year":"2020","journal-title":"Toxicon"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Nowakowska, M.B., Douillard, F.P., and Lindstr\u00f6m, M. (2019). Looking for the X Factor in Bacterial Pathogenesis: Association of orfX-p47 Gene Clusters with Toxin Genes in Clostridial and Non-Clostridial Bacterial Species. Toxins, 12.","DOI":"10.3390\/toxins12010019"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.chom.2017.12.018","article-title":"Identification of a Botulinum Neurotoxin-like Toxin in a Commensal Strain of Enterococcus faecium","volume":"23","author":"Zhang","year":"2018","journal-title":"Cell Host Microbe"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"eadx6145","DOI":"10.1126\/sciadv.adx6145","article-title":"Identification and characterization of botulinum neurotoxin-like two-component toxins in Paeniclostridium ghonii","volume":"11","author":"Lee","year":"2025","journal-title":"Sci. Adv."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"3773","DOI":"10.1016\/j.jmb.2014.09.009","article-title":"Structural basis of the pH-dependent assembly of a botulinum neurotoxin complex","volume":"426","author":"Matsui","year":"2014","journal-title":"J. Mol. Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"17795","DOI":"10.1038\/srep17795","article-title":"Molecular Assembly of Clostridium botulinum progenitor Mcomplex of type E","volume":"5","author":"Eswaramoorthy","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"eadx5831","DOI":"10.1126\/sciadv.adx5831","article-title":"A nut-and-bolt assembly of the bimodular large progenitor botulinum neurotoxin complex","volume":"11","author":"Lam","year":"2025","journal-title":"Sci. Adv."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"eadx5058","DOI":"10.1126\/sciadv.adx5058","article-title":"Structure of the complete 14-subunit botulinum neurotoxin B complex reveals a unique anchoring through the narrow central pore of HA70","volume":"11","author":"Nowakowska","year":"2025","journal-title":"Sci. Adv."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1126\/science.1253823","article-title":"Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex","volume":"344","author":"Lee","year":"2014","journal-title":"Science"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"864","DOI":"10.1038\/s41594-024-01479-0","article-title":"Botulinum neurotoxins exploit host digestive proteases to boost their oral toxicity via activating OrfXs\/P47","volume":"32","author":"Gao","year":"2025","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"3781","DOI":"10.1002\/1873-3468.12889","article-title":"Crystal structures of OrfX2 and P47 from a Botulinum neurotoxin OrfX-type gene cluster","volume":"591","author":"Gustafsson","year":"2017","journal-title":"FEBS Lett."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.toxicon.2017.10.012","article-title":"The hypothetical protein P47 of Clostridium botulinum E1 strain Beluga has a structural topology similar to bactericidal\/permeability-increasing protein","volume":"147","author":"Lam","year":"2018","journal-title":"Toxicon"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1002\/1873-3468.14576","article-title":"Crystal structures of OrfX1, OrfX2 and the OrfX1-OrfX3 complex from the orfX gene cluster of botulinum neurotoxin E1","volume":"597","author":"Gao","year":"2023","journal-title":"FFEBS Lett."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1016\/j.bbamcr.2017.05.019","article-title":"Tubular lipid binding proteins (TULIPs) growing everywhere","volume":"1864","author":"Wong","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.1126\/science.276.5320.1861","article-title":"Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution","volume":"276","author":"Beamer","year":"1997","journal-title":"Science"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1002\/1873-3468.14542","article-title":"Crystal structure of the OrfX1\u2013OrfX3 complex from the PMP1 neurotoxin gene cluster","volume":"597","author":"Stenmark","year":"2023","journal-title":"FEBS Lett."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Lee, K., Gu, S., Jin, L., Le, T.T., Cheng, L.W., Strotmeier, J., Kruel, A.M., Yao, G., Perry, K., and Rummel, A. (2013). Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003690"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"5630","DOI":"10.1073\/pnas.1222139110","article-title":"Molecular assembly of botulinum neurotoxin progenitor complexes","volume":"110","author":"Benefield","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"24777","DOI":"10.1074\/jbc.M703446200","article-title":"A novel subunit structure of Clostridium botulinum serotype D toxin complex with three extended arms","volume":"282","author":"Hasegawa","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"35617","DOI":"10.1074\/jbc.M113.521179","article-title":"Crystal structure of Clostridium botulinum whole hemagglutinin reveals a huge triskelion-shaped molecular complex","volume":"288","author":"Amatsu","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1099\/mic.0.021246-0","article-title":"Disruption of the epithelial barrier by botulinum haemagglutinin (HA) proteins\u2014Differences in cell tropism the mechanism of action between HA proteins of types A or, B. and HA proteins of type C","volume":"155","author":"Jin","year":"2009","journal-title":"Microbiology"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.toxicon.2017.10.020","article-title":"Translocation and dissemination of botulinum neurotoxin from the intestinal tract","volume":"147","author":"Fujinaga","year":"2018","journal-title":"Toxicon"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1007\/978-1-0716-0430-4_19","article-title":"Botulinum Hemagglutinin: Critical Protein for Adhesion and Absorption of Neurotoxin Complex in Host Intestine","volume":"2132","author":"Amatsu","year":"2020","journal-title":"Methods Mol. Biol."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Morimoto, C., Amatsu, S., Matsumura, T., Zuka, M., and Fujinaga, Y. (2025). Botulinum Toxin Complex Serotype B-Okra Exerts Systemic Toxicity via the Oral Route by Disrupting the Intestinal Epithelial Barrier. Toxins, 17.","DOI":"10.20944\/preprints202507.0898.v1"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"10442","DOI":"10.1038\/s41467-025-65384-w","article-title":"Gut mucin fucosylation dictates the entry of botulinum toxin complexes","volume":"16","author":"Amatsu","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Connan, C., Voillequin, M., Chavez, C.V., Mazuet, C., Leveque, C., Vitry, S., Vandewalle, A., and Popoff, M.R. (2017). Botulinum neurotoxin type B uses a distinct entry pathway mediated by CDC42 into intestinal cells versus neuronal cells. Cell. Microbiol., 19.","DOI":"10.1111\/cmi.12738"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Couesnon, A., Molg\u00f3, J., Connan, C., and Popoff, M.R. (2012). Preferential entry of botulinum neurotoxin A Hc domain through intestinal crypt cells and targeting to cholinergic neurons of the mouse intestine. PLoS Pathog., 8.","DOI":"10.1371\/journal.ppat.1002583"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1128\/iai.43.2.487-490.1984","article-title":"Oral toxicities of Clostridium botulinum type A and B toxins from different strains","volume":"43","author":"Ohishi","year":"1984","journal-title":"Infect. Immun."},{"key":"ref_52","first-page":"45","article-title":"Uptake of botulinum neurotoxin in the intestine","volume":"364","author":"Fujinaga","year":"2013","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1038\/nri3608","article-title":"Intestinal epithelial cells: Regulators of barrier function and immune homeostasis","volume":"14","author":"Peterson","year":"2014","journal-title":"Nat. Rev. Immunol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"10629","DOI":"10.1073\/pnas.92.23.10629","article-title":"Rho protein regulates tight junctions and perijunctional actin organization in polarized epithelia","volume":"92","author":"Nusrat","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1128\/MMBR.68.3.373-402.2004","article-title":"Binary bacterial toxins: Biochemistry, biology, and applications of common clostridium and bacillus proteins","volume":"68","author":"Barth","year":"2004","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"6255","DOI":"10.1038\/ncomms7255","article-title":"Botulinum toxin A complex exploits intestinal M cells to enter the host and exert neurotoxicity","volume":"6","author":"Matsumura","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_57","first-page":"355","article-title":"The HA proteins of botulinum toxin disrupt intestinal epithelial intercellular junctions to increase toxin absorption","volume":"10","author":"Matsumura","year":"2008","journal-title":"Cell. Microbiol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1083\/jcb.200910119","article-title":"Botulinum hemagglutinin disrupts the intercellular epithelial barrier by directly binding E-cadherin","volume":"189","author":"Sugawara","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"3361","DOI":"10.1099\/mic.0.26586-0","article-title":"Structural analysis by X-ray crystallography and calorimetry of a haemagglutinin component (HA1) of the progenitor toxin from Clostridium botulinum","volume":"149","author":"Inoue","year":"2003","journal-title":"Microbiology"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Sugawara, Y., Yutani, M., Amatsu, S., Matsumura, T., and Fujinaga, Y. (2014). Functional dissection of the Clostridium botulinum type B hemagglutinin complex: Identification of the carbohydrate and E-cadherin binding sites. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0111170"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.abb.2011.05.012","article-title":"Molecular diversity of the two sugar-binding sites of the \u03b2-trefoil lectin HA33\/C (HA1) from Clostridium botulinum type C neurotoxin","volume":"512","author":"Nakamura","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"3334","DOI":"10.1111\/febs.13346","article-title":"Clostridium botulinum type C hemagglutinin affects the morphology and viability of cultured mammalian cells via binding to the ganglioside GM3","volume":"282","author":"Sugawara","year":"2015","journal-title":"FEBS J."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/0163-7258(82)90061-4","article-title":"Clostridium botulinum toxins","volume":"19","author":"Sakaguchi","year":"1982","journal-title":"Pharmacol. Ther."}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/18\/3\/116\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T05:18:36Z","timestamp":1772083116000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/18\/3\/116"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,24]]},"references-count":63,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2026,3]]}},"alternative-id":["toxins18030116"],"URL":"https:\/\/doi.org\/10.3390\/toxins18030116","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,2,24]]}}}