{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,26]],"date-time":"2026-05-26T07:02:11Z","timestamp":1779778931572,"version":"3.53.1"},"reference-count":58,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,5,26]],"date-time":"2026-05-26T00:00:00Z","timestamp":1779753600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Microbiol."],"abstract":"<jats:p>\n                    Anticoagulants are the primary drugs for the prevention and treatment of thromboembolism. However, most currently available anticoagulants have certain limitations, and there is an urgent need for novel anticoagulants. Marine microorganisms represent a valuable reservoir for the discovery of novel drugs. A marine microorganism capable of producing an anticoagulant protein was isolated from the mangrove mudflat sediment in Beihai City, China. The strain was classified and identified based on 16S rRNA gene sequencing and sequence alignment, combined with phenotypic characteristics. The anticoagulant protein was isolated and purified by ammonium sulfate precipitation, DEAE Sepharose Fast Flow anion exchange chromatography, and Sepharose CL-6B gel filtration chromatography. Its molecular weight was determined by SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis) and COSMOSIL 5Diol-120-II gel filtration chromatography. Physicochemical properties, hemolytic safety, and the effect on erythrocyte aggregation were also examined. To evaluate its anticoagulant effect,\n                    <jats:italic>in vitro<\/jats:italic>\n                    experiments including inhibition of fibrin formation and fibrinogen degradation were performed. The results showed that the strain was identified as\n                    <jats:italic>Bacillus velezensis<\/jats:italic>\n                    and designated as B01. The purified anticoagulant protein had a molecular weight of 27.2\u202fkDa. Its optimal reaction temperature was 50\u202f\u00b0C, and it exhibited good temperature stability in the range of 25\u201337\u202f\u00b0C. The optimal pH was 9.0, and it remained stable under alkaline conditions, particularly at pH 9.0\u201310.0. Cu\n                    <jats:sup>2+<\/jats:sup>\n                    and Fe\n                    <jats:sup>3+<\/jats:sup>\n                    significantly inhibited the protein\u2019s activity, whereas Zn\n                    <jats:sup>2+<\/jats:sup>\n                    , Ca\n                    <jats:sup>2+<\/jats:sup>\n                    , and Mn\n                    <jats:sup>2+<\/jats:sup>\n                    promoted its anticoagulant activity. The protein showed no hemolytic activity and did not induce erythrocyte aggregation. It degraded fibrinogen with a chain degradation order of \u03b3\u202f&amp;gt;\u202fB\u03b2\u202f&amp;gt;\u202fA\u03b1, a pattern that is relatively rare. This anticoagulant protein has the potential to become a novel anticoagulant agent.\n                  <\/jats:p>","DOI":"10.3389\/fmicb.2026.1857346","type":"journal-article","created":{"date-parts":[[2026,5,26]],"date-time":"2026-05-26T06:03:06Z","timestamp":1779775386000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["Purification, characterization, and anticoagulant mechanism of an anticoagulant protein from marine Bacillus velezensis B01"],"prefix":"10.3389","volume":"17","author":[{"given":"Jingran","family":"Yu","sequence":"first","affiliation":[{"name":"College of Agriculture and Forestry, Linyi University","place":["Linyi, Shandong, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mingdi","family":"Yang","sequence":"additional","affiliation":[{"name":"College of Agriculture and Forestry, Linyi University","place":["Linyi, Shandong, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haoyi","family":"Xu","sequence":"additional","affiliation":[{"name":"College of Agriculture and Forestry, Linyi University","place":["Linyi, Shandong, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yankai","family":"Qin","sequence":"additional","affiliation":[{"name":"Agricultural and Financial Service Center of Zaoyuan Town","place":["Linyi, Shandong, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xuezheng","family":"Zhang","sequence":"additional","affiliation":[{"name":"College of Medicine, Linyi University","place":["Linyi, Shandong, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xuguang","family":"Ruan","sequence":"additional","affiliation":[{"name":"College of Agriculture and Forestry, Linyi University","place":["Linyi, Shandong, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fuyao","family":"Tong","sequence":"additional","affiliation":[{"name":"College of Agriculture and Forestry, Linyi University","place":["Linyi, Shandong, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaoyan","family":"Cao","sequence":"additional","affiliation":[{"name":"College of Medicine, Linyi University","place":["Linyi, Shandong, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,5,26]]},"reference":[{"key":"ref1","article-title":"ANSI\/AAMI\/ISO 10993-4:2017; biological evaluation of medical devices\u2014part 4: selection of tests for interactions with blood","year":"2017"},{"key":"ref2","volume-title":"Technical Guidelines for Drug Research 2005","author":"Administration","year":"2006"},{"key":"ref3","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1016\/j.ijbiomac.2020.11.188","article-title":"Instability of therapeutic proteins \u2014 an overview of stresses, stabilization mechanisms and analytical techniques involved in lyophilized proteins","volume":"167","author":"Arun Butreddy","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"ref4","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1007\/s42452-025-07102-1","article-title":"Insights on the therapeutic potential of fibrinolytic enzymes, emphasis on Nattokinase and its enhanced production using advanced technologies: a critical review","volume":"7","author":"Ashokan","year":"2025","journal-title":"Discover Appl. Sci."},{"key":"ref5","doi-asserted-by":"publisher","first-page":"237","DOI":"10.7324\/jabb.2024.175220","article-title":"Purification and evaluating in vitro activity of a fibrinolytic protease produced by a mangrove isolate Bacillus subtilis AIBL_AMSB2_M7E32","volume":"12","author":"Bhavana","year":"2024","journal-title":"J. Appl. Biol. Biotech."},{"key":"ref6","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"ref7","doi-asserted-by":"publisher","first-page":"104994","DOI":"10.1016\/j.ultsonch.2020.104994","article-title":"Investigations in ultrasound-assisted anticoagulant production by marine Bacillus subtilis ZHX","volume":"64","author":"Cao","year":"2020","journal-title":"Ultrason. Sonochem."},{"key":"ref8","doi-asserted-by":"publisher","first-page":"2575","DOI":"10.3390\/pharmaceutics14122575","article-title":"Alternative excipients for protein stabilization in protein therapeutics: overcoming the limitations of Polysorbates","volume":"14","author":"Casta\u00f1eda Ruiz","year":"2022","journal-title":"Pharmaceutics"},{"key":"ref9","doi-asserted-by":"publisher","first-page":"6121","DOI":"10.1021\/bi00416a044","article-title":"Fibrin(ogen) peptide B beta 15-42 inhibits platelet aggregation and fibrinogen binding to activated platelets","volume":"27","author":"Chen","year":"1988","journal-title":"Biochemistry"},{"key":"ref10","doi-asserted-by":"publisher","first-page":"1177271918785130","DOI":"10.1177\/1177271918785130","article-title":"Nattokinase: a promising alternative in prevention and treatment of cardiovascular diseases","volume":"13","author":"Chen","year":"2018","journal-title":"Biomark. Insights"},{"key":"ref11","doi-asserted-by":"publisher","first-page":"335","DOI":"10.11931\/guihaia.gxzw201909018","article-title":"Diversity and anti-thrombotic activity of endophytic and rhizospheric bacteria isolated from Aegiceras corniculatum","volume":"40","author":"Fei","year":"2020","journal-title":"Guihaia"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/B978-0-12-821406-0.00012-6","article-title":"Current status and future directions in producing microbial fibrinolytic enzymes for biomedical applications","volume-title":"Recent Developments in Applied Microbiology and Biochemistry","author":"Gowthami","year":"2021"},{"key":"ref13","doi-asserted-by":"publisher","first-page":"238","DOI":"10.3321\/j.issn:0476-0301.2003.02.019","article-title":"Determination of inhibitory activity to thrombin of inhibitor from Yanyuan leech","volume":"39","author":"Guangyu","year":"2003","journal-title":"J. Beijing Norm. Univ. (Nat. Sci.)"},{"key":"ref14","doi-asserted-by":"publisher","first-page":"36","DOI":"10.15407\/ubj96.06.036","article-title":"Purification and physico-chemical properties of Bacillus atrophaeus protease with elastolytic and fibrinogenolytic activity","volume":"96","author":"Gudzenko","year":"2024","journal-title":"Ukrainian Biochem. J."},{"key":"ref15","doi-asserted-by":"publisher","first-page":"2516","DOI":"10.1099\/mic.0.038588-0","article-title":"Binding and degradation of fibrinogen by Bacteroides fragilis and characterization of a 54 kDa fibrinogen-binding protein","volume":"156","author":"Houston","year":"2010","journal-title":"Microbiology (Reading)"},{"key":"ref16","doi-asserted-by":"publisher","first-page":"111527","DOI":"10.1016\/j.biopha.2021.111527","article-title":"Antithrombotic and anticoagulant effects of a novel protein isolated from the venom of the Deinagkistrodon acutus snake","volume":"138","author":"Huang","year":"2021","journal-title":"Biomed. Pharmacother."},{"key":"ref17","doi-asserted-by":"publisher","first-page":"267","DOI":"10.1385\/0-89603-268-x:267","article-title":"Molecular-weight estimation for native proteins using size-exclusion high-performance liquid chromatography","volume":"32","author":"Irvine","year":"1994","journal-title":"Methods Mol. Biol."},{"key":"ref18","doi-asserted-by":"publisher","first-page":"106371","DOI":"10.1016\/j.pep.2023.106371","article-title":"Insight into the thrombolytic ability of an extracellular fibrinolytic enzyme from Bacillus amyloliquefaciens GXU-1 isolated from Sipunculus nudus","volume":"213","author":"Jiang","year":"2024","journal-title":"Protein Expr. Purif."},{"key":"ref19","volume-title":"Study of Anticoagulation Active Protein from Termitomyces Albuminosus TA-SD Master' Thesis","author":"Jiejing","year":"2008"},{"key":"ref20","doi-asserted-by":"publisher","first-page":"1213","DOI":"10.1166\/jbn.2015.2071","article-title":"Downstream processing, formulation development and antithrombotic evaluation of microbial Nattokinase","volume":"11","author":"Kapoor","year":"2015","journal-title":"J. Biomed. Nanotechnol."},{"key":"ref21","doi-asserted-by":"publisher","first-page":"e13","DOI":"10.1161\/atvbaha.117.308564","article-title":"Fibrinogen and fibrin in hemostasis and thrombosis","volume":"37","author":"Kattula","year":"2017","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref22","doi-asserted-by":"publisher","first-page":"1647","DOI":"10.3390\/jcm14051647","article-title":"Anticoagulation management: current landscape and future trends","volume":"14","author":"Kholmukhamedov","year":"2025","journal-title":"J. Clin. Med."},{"key":"ref23","doi-asserted-by":"publisher","first-page":"1013","DOI":"10.1021\/bm025545v","article-title":"Formation of fibrin gel in fibrinogen-thrombin system: static and dynamic light scattering study","volume":"3","author":"Kita","year":"2002","journal-title":"Biomacromolecules"},{"key":"ref24","doi-asserted-by":"publisher","first-page":"1017","DOI":"10.1093\/jb\/mvj112","article-title":"Engineering of the pH-dependence of Thermolysin activity as examined by site-directed mutagenesis of Asn112 located at the active site of Thermolysin","volume":"139","author":"Kusano","year":"2006","journal-title":"J. Biochem."},{"key":"ref25","doi-asserted-by":"publisher","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"ref26","doi-asserted-by":"publisher","first-page":"72","DOI":"10.15625\/0866-7160\/v27n3.5274","article-title":"Study on alkalophilic and halophilic microorganisms in the sea waters of northern Vietnam gulf","volume":"27","author":"Le Gia","year":"2014","journal-title":"Acad. J. Biol."},{"key":"ref27","doi-asserted-by":"publisher","first-page":"601","DOI":"10.1016\/j.ijbiomac.2021.02.167","article-title":"Purification, characterization, and chemical modification of Bacillus velezensis SN-14 fibrinolytic enzyme","volume":"177","author":"Lu","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"ref28","doi-asserted-by":"publisher","first-page":"267","DOI":"10.3390\/md22060267","article-title":"Purification and characterization of a novel fibrinolytic enzyme from marine bacterium Bacillus sp. S-3685 isolated from the South China Sea","volume":"22","author":"Ma","year":"2024","journal-title":"Mar. Drugs"},{"key":"ref29","doi-asserted-by":"publisher","first-page":"914","DOI":"10.1038\/nature06797","article-title":"Triggers, targets and treatments for thrombosis","volume":"451","author":"Mackman","year":"2008","journal-title":"Nature"},{"key":"ref30","doi-asserted-by":"publisher","first-page":"477","DOI":"10.1016\/j.ijbiomac.2015.04.075","article-title":"Antiplatelet and antithrombotic activity of a fibrin(ogen)olytic protease from Bacillus cereus strain FF01","volume":"79","author":"Majumdar","year":"2015","journal-title":"Int. J. Biol. Macromol."},{"key":"ref31","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1016\/j.bioeng.2006.07.001","article-title":"Protein engineering of class-a non-specific acid phosphatase (PhoN) of Salmonella typhimurium: modulation of the pH-activity profile","volume":"23","author":"Makde","year":"2006","journal-title":"Biomol. Eng."},{"key":"ref32","doi-asserted-by":"publisher","first-page":"1301","DOI":"10.1007\/s11095-024-03726-x","article-title":"Stability of protein pharmaceuticals: recent advances","volume":"41","author":"Manning","year":"2024","journal-title":"Pharm. Res."},{"key":"ref33","doi-asserted-by":"publisher","first-page":"998","DOI":"10.1007\/s12257-010-0116-x","article-title":"Isolation, purification, and characterization of haloalkaline xylanase from a marine Bacillus pumilus strain, GESF-1","volume":"15","author":"Menon","year":"2010","journal-title":"Biotechnol. Bioprocess Eng."},{"key":"ref34","doi-asserted-by":"publisher","first-page":"2466","DOI":"10.1182\/blood-2003-01-0204","article-title":"Recombinant BbetaArg14His fibrinogen implies participation of N-terminus of Bbeta chain in desA fibrin polymerization","volume":"102","author":"Moen","year":"2003","journal-title":"Blood"},{"key":"ref35","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1097\/00001721-199707000-00001","article-title":"Fibrinogen and fibrin polymerization: appraisal of the binding events that accompany fibrin generation and fibrin clot assembly","volume":"8","author":"Mosesson","year":"1997","journal-title":"Blood Coagul. Fibrinolysis"},{"key":"ref36","doi-asserted-by":"publisher","first-page":"490","DOI":"10.3390\/jpm15100490","article-title":"Next-generation anticoagulants: precision strategies for patient-centered Thromboprophylaxis","volume":"15","author":"Nasiri","year":"2025","journal-title":"J. Pers. Med."},{"key":"ref37","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1186\/s43556-024-00214-x","article-title":"Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation","volume":"5","author":"Nencini","year":"2024","journal-title":"Mol. Biomed."},{"key":"ref38","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1007\/bf02121748","article-title":"Characterization of three Aeromonas and nine pseudomonas species by extracellular enzymes and haemolysins","volume":"161","author":"Nord","year":"1975","journal-title":"Med. Microbiol. Immunol."},{"key":"ref39","doi-asserted-by":"publisher","first-page":"102","DOI":"10.1053\/j.seminhematol.2014.02.002","article-title":"Direct oral anticoagulants and bleeding risk (in comparison to vitamin K antagonists and heparins), and the treatment of bleeding","volume":"51","author":"Palareti","year":"2014","journal-title":"Semin. Hematol."},{"key":"ref40","doi-asserted-by":"publisher","first-page":"287","DOI":"10.16429\/j.1009-7848.2019.04.034","article-title":"Effect of metal ions on protease activity of microorganisms and its mechanism","volume":"19","author":"Qian","year":"2019","journal-title":"J. Chin. Inst. Food Sci. Technol."},{"key":"ref41","doi-asserted-by":"publisher","first-page":"724","DOI":"10.1055\/s-0034-1390325","article-title":"Thrombosis: a major contributor to global disease burden","volume":"40","author":"Raskob","year":"2014","journal-title":"Semin. Thromb. Hemost."},{"key":"ref42","doi-asserted-by":"publisher","first-page":"719","DOI":"10.1016\/j.toxicon.2012.05.008","article-title":"Anticoagulant activity of moon jellyfish (Aurelia aurita) tentacle extract","volume":"60","author":"Rastogi","year":"2012","journal-title":"Toxicon"},{"key":"ref43","doi-asserted-by":"publisher","first-page":"e70360","DOI":"10.1002\/pro.70360","article-title":"Structure-guided engineering of protein stability through core hydrophobicity","volume":"34","author":"Ravichandran","year":"2025","journal-title":"Protein Sci."},{"key":"ref44","doi-asserted-by":"publisher","first-page":"1880","DOI":"10.3390\/pharmaceutics13111880","article-title":"Microbial fibrinolytic enzymes as anti-thrombotics: production, characterisation and prodigious biopharmaceutical applications","volume":"13","author":"Sharma","year":"2021","journal-title":"Pharmaceutics"},{"key":"ref45","doi-asserted-by":"publisher","first-page":"2196","DOI":"10.3390\/life13112196","article-title":"Fibrin and fibrinolytic enzyme Cascade in thrombosis: unravelling the role","volume":"13","author":"Singh","year":"2023","journal-title":"Life (Basel)"},{"key":"ref46","doi-asserted-by":"publisher","first-page":"182-190","DOI":"10.7324\/JABB.2024.161429","article-title":"A novel fibrinolytic enzyme producer from mangrove soil sediments: screening, isolation, strain improvement, and fermentation","volume":"12","author":"Sompalli","year":"2024","journal-title":"J. Appl. Biol. Biotechnol."},{"key":"ref47","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1007\/s12010-007-9024-8","article-title":"Biochemical and enzymatic properties of a novel marine fibrinolytic enzyme from Urechis unicinctus","volume":"136","author":"Wang","year":"2007","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref48","doi-asserted-by":"publisher","first-page":"50","DOI":"10.1186\/s42483-023-00204-x","article-title":"Biocontrol and molecular characterization of Bacillus velezensis D against tobacco bacterial wilt","volume":"5","author":"Wang","year":"2023","journal-title":"Phytopathol. Res."},{"key":"ref49","doi-asserted-by":"publisher","first-page":"105311","DOI":"10.1016\/j.biocontrol.2023.105311","article-title":"Isolation and characterization of Bacillus velezensis strain B19 for biocontrol of Panax notoginseng root rot","volume":"185","author":"Wang","year":"2023","journal-title":"Biol. Control"},{"key":"ref50","doi-asserted-by":"publisher","first-page":"3957","DOI":"10.1021\/jf1049535","article-title":"Production of fibrinolytic enzyme from Bacillus amyloliquefaciens by fermentation of chickpeas, with the evaluation of the anticoagulant and antioxidant properties of chickpeas","volume":"59","author":"Wei","year":"2011","journal-title":"J. Agric. Food Chem."},{"key":"ref51","doi-asserted-by":"publisher","first-page":"e120S","DOI":"10.1378\/chest.11-2294","article-title":"New antithrombotic drugs: antithrombotic therapy and prevention of thrombosis, 9th ed: American College of Chest Physicians Evidence-Based Clinical Practice Guidelines","volume":"141","author":"Weitz","year":"2012","journal-title":"Chest"},{"key":"ref52","doi-asserted-by":"publisher","first-page":"1007","DOI":"10.1161\/atvbaha.124.320151","article-title":"Global Health burden of venous thromboembolism","volume":"44","author":"Wendelboe","year":"2024","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref53","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1016\/s0969-2126(97)00171-8","article-title":"Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen","volume":"5","author":"Yee","year":"1997","journal-title":"Structure"},{"key":"ref54","doi-asserted-by":"publisher","first-page":"322","DOI":"10.1016\/j.fsi.2018.04.055","article-title":"Probiotic potential of Bacillus velezensis JW: antimicrobial activity against fish pathogenic bacteria and immune enhancement effects on Carassius auratus","volume":"78","author":"Yi","year":"2018","journal-title":"Fish Shellfish Immunol."},{"key":"ref55","doi-asserted-by":"publisher","first-page":"356","DOI":"10.3390\/md20060356","article-title":"A novel bi-functional fibrinolytic enzyme with anticoagulant and thrombolytic activities from a marine-derived fungus aspergillus versicolor ZLH-1","volume":"20","author":"Zhao","year":"2022","journal-title":"Mar. Drugs"},{"key":"ref56","doi-asserted-by":"publisher","first-page":"1513438","DOI":"10.3389\/fpls.2024.1513438","article-title":"Isolation and identification of a novel Bacillus velezensis strain JIN4 and its potential for biocontrol of kiwifruit bacterial canker caused by Pseudomonas syringae pv. Actinidiae","volume":"15","author":"Zhao","year":"2024","journal-title":"Front. Plant Sci."},{"key":"ref57","first-page":"259","article-title":"Expression of hemolytic phospholipase C from Pseudomonas aeruginosa in Escherichia coli","volume":"53","author":"Zhao","year":"2013","journal-title":"Acta Microbiol Sin."},{"key":"ref58","doi-asserted-by":"publisher","first-page":"843","DOI":"10.3390\/microorganisms10050843","article-title":"Purification and characterization of a fibrinolytic enzyme from marine Bacillus velezensis Z01 and assessment of its therapeutic efficacy in vivo","volume":"10","author":"Zhou","year":"2022","journal-title":"Microorganisms"}],"container-title":["Frontiers in Microbiology"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmicb.2026.1857346\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,26]],"date-time":"2026-05-26T06:03:11Z","timestamp":1779775391000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmicb.2026.1857346\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,5,26]]},"references-count":58,"alternative-id":["10.3389\/fmicb.2026.1857346"],"URL":"https:\/\/doi.org\/10.3389\/fmicb.2026.1857346","relation":{},"ISSN":["1664-302X"],"issn-type":[{"value":"1664-302X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,5,26]]},"article-number":"1857346"}}