{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T18:16:32Z","timestamp":1790878592701,"version":"4.1.0"},"reference-count":36,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2021,1,12]],"date-time":"2021-01-12T00:00:00Z","timestamp":1610409600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2021,1,12]],"date-time":"2021-01-12T00:00:00Z","timestamp":1610409600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["T32 GM07863"],"award-info":[{"award-number":["T32 GM07863"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["P30 CA046592"],"award-info":[{"award-number":["P30 CA046592"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["1F31AI136615-01"],"award-info":[{"award-number":["1F31AI136615-01"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Michigan Economic Development Corporation and Michigan Technology Tri-Corridor","award":["085P1000817"],"award-info":[{"award-number":["085P1000817"]}]},{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","award":["DE-AC02-06CH11357"],"award-info":[{"award-number":["DE-AC02-06CH11357"]}],"id":[{"id":"10.13039\/100000015","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000774","name":"Defense Threat Reduction Agency","doi-asserted-by":"publisher","award":["HDTRA1-15-1-0067"],"award-info":[{"award-number":["HDTRA1-15-1-0067"]}],"id":[{"id":"10.13039\/100000774","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Michigan Translational Research and Commercialization (MTRAC) Life Sciences"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Lectins, carbohydrate-binding proteins, have been regarded as potential antiviral agents, as some can bind glycans on viral surface glycoproteins and inactivate their functions. However, clinical development of lectins has been stalled by the mitogenicity of many of these proteins, which is the ability to stimulate deleterious proliferation, especially of immune cells. We previously demonstrated that the mitogenic and antiviral activities of a lectin (banana lectin, BanLec) can be separated via a single amino acid mutation, histidine to threonine at position 84 (H84T), within the third Greek key. The resulting lectin, H84T BanLec, is virtually non-mitogenic but retains antiviral activity. Decreased mitogenicity was associated with disruption of pi\u2013pi stacking between two aromatic amino acids. To examine whether we could provide further proof-of-principle of the ability to separate these two distinct lectin functions, we identified another lectin, Malaysian banana lectin (Malay BanLec), with similar structural features as BanLec, including pi\u2013pi stacking, but with only 63% amino acid identity, and showed that it is both mitogenic and potently antiviral. We then engineered an F84T mutation expected to disrupt pi\u2013pi stacking, analogous to H84T. As predicted, F84T Malay BanLec (F84T) was less mitogenic than wild type. However, F84T maintained strong antiviral activity and inhibited replication of HIV, Ebola, and other viruses. The F84T mutation disrupted pi\u2013pi stacking without disrupting the overall lectin structure. These findings show that pi\u2013pi stacking in the third Greek key is a conserved mitogenic motif in these two jacalin-related lectins BanLec and Malay BanLec, and further highlight the potential to rationally engineer antiviral lectins for therapeutic purposes.<\/jats:p>","DOI":"10.1038\/s41598-020-80577-7","type":"journal-article","created":{"date-parts":[[2021,1,12]],"date-time":"2021-01-12T19:24:12Z","timestamp":1610479452000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":24,"title":["Targeted disruption of pi\u2013pi stacking in Malaysian banana lectin reduces mitogenicity while preserving antiviral activity"],"prefix":"10.1038","volume":"11","author":[{"given":"Evelyn M.","family":"Cov\u00e9s-Datson","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven R.","family":"King","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maureen","family":"Legendre","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael D.","family":"Swanson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Auroni","family":"Gupta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sandra","family":"Claes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jennifer L.","family":"Meagher","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arnaud","family":"Boonen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lihong","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Birte","family":"Kalveram","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zoe","family":"Raglow","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander N.","family":"Freiberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark","family":"Prichard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeanne A.","family":"Stuckey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominique","family":"Schols","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David M.","family":"Markovitz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,1,12]]},"reference":[{"key":"80577_CR1","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1002\/med.20216","volume":"32","author":"KO Fran\u00e7ois","year":"2012","unstructured":"Fran\u00e7ois, K. O. & Balzarini, J. Potential of carbohydrate-binding agents as therapeutics against enveloped viruses. Med. Res. Rev. 32, 349\u2013387 (2012).","journal-title":"Med. Res. Rev."},{"key":"80577_CR2","doi-asserted-by":"publisher","DOI":"10.1101\/GLYCOBIOLOGY.3E.031","volume-title":"R-Type Lectins Essentials of Glycobiology","author":"RD Cummings","year":"2015","unstructured":"Cummings, R. D. & Schnaar, L. R-Type Lectins Essentials of Glycobiology (Cold Spring Harbor Laboratory Press, New York, 2015). https:\/\/doi.org\/10.1101\/GLYCOBIOLOGY.3E.031."},{"key":"80577_CR3","doi-asserted-by":"publisher","first-page":"53R","DOI":"10.1093\/glycob\/cwh122","volume":"14","author":"N Sharon","year":"2004","unstructured":"Sharon, N. & Lis, H. History of lectins: from hemagglutinins to biological recognition molecules. Glycobiology 14, 53R-62R (2004).","journal-title":"Glycobiology"},{"key":"80577_CR4","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1038\/nm1541","volume":"13","author":"L de Witte","year":"2007","unstructured":"de Witte, L. et al. Langerin is a natural barrier to HIV-1 transmission by Langerhans cells. Nat. Med. 13, 367\u2013371 (2007).","journal-title":"Nat. Med."},{"key":"80577_CR5","doi-asserted-by":"publisher","first-page":"547","DOI":"10.1146\/annurev.immunol.21.120601.140954","volume":"21","author":"U Holmskov","year":"2003","unstructured":"Holmskov, U., Thiel, S. & Jensenius, J. C. Collections and ficolins: Humoral lectins of the innate immune defense. Annu. Rev. Immunol. 21, 547\u2013578 (2003).","journal-title":"Annu. Rev. Immunol."},{"key":"80577_CR6","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1159\/000228159","volume":"2","author":"DP Eisen","year":"2010","unstructured":"Eisen, D. P. Mannose-binding lectin deficiency and respiratory tract infection. J. Innate Immun. 2, 114\u2013122 (2010).","journal-title":"J. Innate Immun."},{"key":"80577_CR7","doi-asserted-by":"publisher","first-page":"e25005","DOI":"10.1371\/journal.pone.0025005","volume":"6","author":"MLB Hillaire","year":"2011","unstructured":"Hillaire, M. L. B. et al. Assessment of the antiviral properties of recombinant porcine SP-D against various influenza A viruses in vitro. PLoS ONE 6, e25005 (2011).","journal-title":"PLoS ONE"},{"key":"80577_CR8","doi-asserted-by":"publisher","first-page":"311","DOI":"10.1172\/JCI117323","volume":"94","author":"KL Hartshorn","year":"1994","unstructured":"Hartshorn, K. L. et al. Evidence for a protective role of pulmonary surfactant protein D (SP-D) against influenza A viruses. J. Clin. Invest. 94, 311\u2013319 (1994).","journal-title":"J. Clin. Invest."},{"key":"80577_CR9","first-page":"L131","volume":"276","author":"GZ Cai","year":"1999","unstructured":"Cai, G. Z., Griffin, G. L., Senior, R. M., Longmore, W. J. & Moxley, M. A. Recombinant SP-D carbohydrate recognition domain is a chemoattractant for human neutrophils. Am. J. Physiol. 276, L131\u2013L136 (1999).","journal-title":"Am. J. Physiol."},{"key":"80577_CR10","first-page":"462","volume":"20","author":"PC Nowell","year":"1960","unstructured":"Nowell, P. C. Phytohemagglutinin: An initiator of mitosis in cultures of normal human leukocytes. Cancer Res. 20, 462\u2013466 (1960).","journal-title":"Cancer Res."},{"key":"80577_CR11","doi-asserted-by":"publisher","first-page":"329","DOI":"10.3109\/1040841X.2012.733680","volume":"40","author":"RS Singh","year":"2014","unstructured":"Singh, R. S. & Walia, A. K. Microbial lectins and their prospective mitogenic potential. Crit. Rev. Microbiol. 40, 329\u2013347 (2014).","journal-title":"Crit. Rev. Microbiol."},{"key":"80577_CR12","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1016\/j.lfs.2018.06.003","volume":"207","author":"EVMM Carvalho","year":"2018","unstructured":"Carvalho, E. V. M. M., Oliveira, W. F., Coelho, L. C. B. B. & Correia, M. T. S. Lectins as mitosis stimulating factors: Briefly reviewed. Life Sci. 207, 152\u2013157 (2018).","journal-title":"Life Sci."},{"key":"80577_CR13","doi-asserted-by":"publisher","first-page":"2802","DOI":"10.1016\/j.biocel.2008.05.023","volume":"40","author":"D Huskens","year":"2008","unstructured":"Huskens, D., Vermeire, K., Vandemeulebroucke, E., Balzarini, J. & Schols, D. Safety concerns for the potential use of cyanovirin-N as a microbicidal anti-HIV agent. Int. J. Biochem. Cell Biol. 40, 2802\u20132814 (2008).","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"80577_CR14","doi-asserted-by":"publisher","first-page":"8646","DOI":"10.1074\/jbc.M109.034926","volume":"285","author":"MD Swanson","year":"2010","unstructured":"Swanson, M. D., Winter, H. C., Goldstein, I. J. & Markovitz, D. M. A lectin isolated from bananas is a potent inhibitor of HIV replication. J. Biol. Chem. 285, 8646\u20138655 (2010).","journal-title":"J. Biol. Chem."},{"key":"80577_CR15","doi-asserted-by":"publisher","first-page":"746","DOI":"10.1016\/j.cell.2015.09.056","volume":"163","author":"MD Swanson","year":"2015","unstructured":"Swanson, M. D. et al. Engineering a therapeutic lectin by uncoupling mitogenicity from antiviral activity. Cell 163, 746\u2013758 (2015).","journal-title":"Cell"},{"key":"80577_CR16","doi-asserted-by":"publisher","first-page":"2122","DOI":"10.1073\/pnas.1915152117","volume":"117","author":"EM Cov\u00e9s-Datson","year":"2020","unstructured":"Cov\u00e9s-Datson, E. M. et al. A molecularly engineered antiviral banana lectin inhibits fusion and is efficacious against influenza virus infection in vivo. Proc. Natl. Acad. Sci. 117, 2122\u20132132 (2020).","journal-title":"Proc. Natl. Acad. Sci."},{"key":"80577_CR17","doi-asserted-by":"publisher","first-page":"e0007595","DOI":"10.1371\/journal.pntd.0007595","volume":"13","author":"EM Cov\u00e9s-Datson","year":"2019","unstructured":"Cov\u00e9s-Datson, E. M. et al. Inhibition of ebola virus by a molecularly engineered banana lectin. PLoS Negl. Trop. Dis. 13, e0007595 (2019).","journal-title":"PLoS Negl. Trop. Dis."},{"key":"80577_CR18","doi-asserted-by":"publisher","first-page":"929","DOI":"10.1016\/j.biocel.2007.10.033","volume":"40","author":"M Gavrovic-Jankulovic","year":"2008","unstructured":"Gavrovic-Jankulovic, M. et al. A novel recombinantly produced banana lectin isoform is a valuable tool for glycoproteomics and a potent modulator of the proliferation response in CD3+, CD4+, and CD8+ populations of human PBMCs. Int. J. Biochem. Cell Biol. 40, 929\u2013941 (2008).","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"80577_CR19","doi-asserted-by":"publisher","first-page":"1227","DOI":"10.1111\/j.1742-4658.2008.06282.x","volume":"275","author":"S Nakamura-Tsuruta","year":"2008","unstructured":"Nakamura-Tsuruta, S. et al. Analysis of the sugar-binding specificity of mannose-binding-type Jacalin-related lectins by frontal affinity chromatography\u2014An approach to functional classification. FEBS J. 275, 1227\u20131239 (2008).","journal-title":"FEBS J."},{"key":"80577_CR20","doi-asserted-by":"publisher","first-page":"1033","DOI":"10.1093\/glycob\/cwi088","volume":"15","author":"JL Meagher","year":"2005","unstructured":"Meagher, J. L., Winter, H. C., Ezell, P., Goldstein, I. J. & Stuckey, J. A. Crystal structure of banana lectin reveals a novel second sugar binding site. Glycobiology 15, 1033\u20131042 (2005).","journal-title":"Glycobiology"},{"key":"80577_CR21","doi-asserted-by":"publisher","first-page":"721","DOI":"10.1042\/bj2720721","volume":"272","author":"VL Koshte","year":"1990","unstructured":"Koshte, V. L., van Dijk, W., van der Stelt, M. E. & Aalberse, R. C. Isolation and characterization of BanLec-I, a mannoside-binding lectin from Musa paradisiac (banana). Biochem. J. 272, 721\u2013726 (1990).","journal-title":"Biochem. J."},{"key":"80577_CR22","doi-asserted-by":"publisher","first-page":"296","DOI":"10.3390\/v8100296","volume":"8","author":"S Lusvarghi","year":"2016","unstructured":"Lusvarghi, S. & Bewley, C. Griffithsin: An antiviral lectin with outstanding therapeutic potential. Viruses 8, 296 (2016).","journal-title":"Viruses"},{"key":"80577_CR23","doi-asserted-by":"publisher","first-page":"e22635","DOI":"10.1371\/journal.pone.0022635","volume":"6","author":"JC Kouokam","year":"2011","unstructured":"Kouokam, J. C. et al. Investigation of griffithsin\u2019s interactions with human cells confirms its outstanding safety and efficacy profile as a microbicide candidate. PLoS ONE 6, e22635 (2011).","journal-title":"PLoS ONE"},{"key":"80577_CR24","doi-asserted-by":"publisher","first-page":"18817","DOI":"10.3390\/molecules191118817","volume":"19","author":"SS Singh","year":"2014","unstructured":"Singh, S. S., Devi, S. K. & Ng, T. B. Banana lectin: A brief review. Molecules 19, 18817\u201318827 (2014).","journal-title":"Molecules"},{"key":"80577_CR25","doi-asserted-by":"publisher","first-page":"1064","DOI":"10.1093\/glycob\/cwv042","volume":"25","author":"MK Sethi","year":"2015","unstructured":"Sethi, M. K. et al. In-depth N-glycome profiling of paired colorectal cancer and non-tumorigenic tissues reveals cancer-, stage- and EGFR-specific protein N-glycosylation. Glycobiology 25, 1064\u20131078 (2015).","journal-title":"Glycobiology"},{"key":"80577_CR26","doi-asserted-by":"publisher","first-page":"218","DOI":"10.1111\/jcmm.12153","volume":"18","author":"P Huang","year":"2014","unstructured":"Huang, P. et al. The role of EGF-EGFR signalling pathway in hepatocellular carcinoma inflammatory microenvironment. J. Cell. Mol. Med. 18, 218\u2013230 (2014).","journal-title":"J. Cell. Mol. Med."},{"key":"80577_CR27","doi-asserted-by":"publisher","first-page":"780","DOI":"10.1096\/fj.04-1766fje","volume":"19","author":"TG Johns","year":"2005","unstructured":"Johns, T. G. et al. The antitumor monoclonal antibody 806 recognizes a high-mannose form of the EGF receptor that reaches the cell surface when cells over-express the receptor. FASEB J. 19, 780\u2013782 (2005).","journal-title":"FASEB J."},{"key":"80577_CR28","doi-asserted-by":"publisher","first-page":"e1003618","DOI":"10.1371\/journal.ppat.1003618","volume":"9","author":"RW Sanders","year":"2013","unstructured":"Sanders, R. W. et al. A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies. PLoS Pathog. 9, e1003618 (2013).","journal-title":"PLoS Pathog."},{"key":"80577_CR29","doi-asserted-by":"publisher","first-page":"e0176057","DOI":"10.1371\/journal.pone.0176057","volume":"12","author":"A Van Hout","year":"2017","unstructured":"Van Hout, A., Dhuys, T., Oeyen, M., Schols, D. & Van Loy, T. Comparison of cell-based assays for the identification and evaluation of competitive CXCR4 inhibitors. PLoS ONE 12, e0176057 (2017).","journal-title":"PLoS ONE"},{"key":"80577_CR30","doi-asserted-by":"publisher","first-page":"1383","DOI":"10.1084\/jem.186.8.1383","volume":"186","author":"D Schols","year":"1997","unstructured":"Schols, D. et al. Inhibition of T-tropic HIV strains by selective antagonization of the chemokine receptor CXCR4. J. Exp. Med. 186, 1383\u20131388 (1997).","journal-title":"J. Exp. Med."},{"key":"80577_CR31","doi-asserted-by":"publisher","first-page":"3724","DOI":"10.1128\/AAC.49.9.3724-3733.2005","volume":"49","author":"SL Williams-Aziz","year":"2005","unstructured":"Williams-Aziz, S. L. et al. Comparative activities of lipid esters of cidofovir and cyclic cidofovir against replication of herpesviruses in vitro. Antimicrob. Agents Chemother. 49, 3724\u20133733 (2005).","journal-title":"Antimicrob. Agents Chemother."},{"key":"80577_CR32","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","volume":"276","author":"Z Otwinowski","year":"1997","unstructured":"Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307\u2013326 (1997).","journal-title":"Methods Enzymol."},{"key":"80577_CR33","doi-asserted-by":"publisher","first-page":"658","DOI":"10.1107\/S0021889807021206","volume":"40","author":"AJ McCoy","year":"2007","unstructured":"McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658\u2013674 (2007).","journal-title":"J. Appl. Crystallogr."},{"key":"80577_CR34","doi-asserted-by":"publisher","first-page":"1022","DOI":"10.1107\/S0021889897006766","volume":"30","author":"A Vagin","year":"1997","unstructured":"Vagin, A. & Teplyakov, A. MOLREP: An automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022\u20131025 (1997).","journal-title":"J. Appl. Crystallogr."},{"key":"80577_CR35","volume-title":"BUSTER version 1.10.0","author":"G Bricogne","year":"2011","unstructured":"Bricogne, G. et al. BUSTER version 1.10.0 (United Kingdom Glob Phasing Ltd, Cambridge, 2011)."},{"key":"80577_CR36","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"P Emsley","year":"2010","unstructured":"Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of coot. Acta Crystallogr. D. Biol. Crystallogr. 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-020-80577-7.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-020-80577-7","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-020-80577-7.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,12,3]],"date-time":"2022-12-03T01:48:11Z","timestamp":1670032091000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-020-80577-7"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,1,12]]},"references-count":36,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2021,12]]}},"alternative-id":["80577"],"URL":"https:\/\/doi.org\/10.1038\/s41598-020-80577-7","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,1,12]]},"assertion":[{"value":"15 August 2020","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"21 December 2020","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"12 January 2021","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"D.M.M. and M.D.S. are inventors on patents for H84T BanLec. D.M.M. is a founder of Defense Biosciences, a company that aims to commercialize H84T BanLec. The other authors have no competing interests to declare.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"656"}}