{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T02:56:52Z","timestamp":1787021812872,"version":"build-2736575974"},"reference-count":72,"publisher":"Public Library of Science (PLoS)","issue":"3","license":[{"start":{"date-parts":[[2013,3,7]],"date-time":"2013-03-07T00:00:00Z","timestamp":1362614400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosntds.org"],"crossmark-restriction":false},"short-container-title":["PLoS Negl Trop Dis"],"DOI":"10.1371\/journal.pntd.0002046","type":"journal-article","created":{"date-parts":[[2013,3,7]],"date-time":"2013-03-07T16:56:22Z","timestamp":1362675382000},"page":"e2046","update-policy":"https:\/\/doi.org\/10.1371\/journal.pntd.corrections_policy","source":"Crossref","is-referenced-by-count":54,"title":["Rapid and Scalable Plant-based Production of a Cholera Toxin B Subunit Variant to Aid in Mass Vaccination against Cholera Outbreaks"],"prefix":"10.1371","volume":"7","author":[{"given":"Krystal Teasley","family":"Hamorsky","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. Calvin","family":"Kouokam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lauren J.","family":"Bennett","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keegan J.","family":"Baldauf","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroyuki","family":"Kajiura","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazuhito","family":"Fujiyama","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nobuyuki","family":"Matoba","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2013,3,7]]},"reference":[{"key":"ref1","first-page":"289","article-title":"Cholera, 2011","volume":"87","journal-title":"Wkly Epidemiol Rec"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/S0140-6736(86)91944-6","article-title":"Field trial of oral cholera vaccines in Bangladesh","volume":"2","author":"JD Clemens","year":"1986","journal-title":"Lancet"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1093\/infdis\/158.1.60","article-title":"Field trial of oral cholera vaccines in Bangladesh: results of one year of follow-up","volume":"158","author":"JD Clemens","year":"1988","journal-title":"J Infect Dis"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/0264-410X(95)00122-H","article-title":"Field trial of inactivated oral cholera vaccines in Bangladesh: results from 5 years of follow-up","volume":"14","author":"FP van Loon","year":"1996","journal-title":"Vaccine"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/0264-410X(92)90030-N","article-title":"Safety and immunogenicity of an oral recombinant cholera B subunit-whole cell vaccine in Swedish volunteers","volume":"10","author":"M Jertborn","year":"1992","journal-title":"Vaccine"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"e1743","DOI":"10.1371\/journal.pntd.0001743","article-title":"Safety of the recombinant cholera toxin B subunit, killed whole-cell (rBS-WC) oral cholera vaccine in pregnancy","volume":"6","author":"R Hashim","year":"2012","journal-title":"PLoS Negl Trop Dis"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1006\/jmbi.1995.0455","article-title":"The 2.4 A crystal structure of cholera toxin B subunit pentamer: choleragenoid","volume":"251","author":"RG Zhang","year":"1995","journal-title":"J Mol Biol"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1586\/14760584.7.5.561","article-title":"Vaccination with Dukoral against travelers&apos; diarrhea (ETEC) and cholera","volume":"7","author":"T Jelinek","year":"2008","journal-title":"Expert Rev Vaccines"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1038\/nrgastro.2011.174","article-title":"New-generation vaccines against cholera","volume":"8","author":"J Clemens","year":"2011","journal-title":"Nat Rev Gastroenterol Hepatol"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"e1145","DOI":"10.1371\/journal.pntd.0001145","article-title":"Meeting cholera&apos;s challenge to Haiti and the world: a joint statement on cholera prevention and care","volume":"5","author":"P Farmer","year":"2011","journal-title":"PLoS Negl Trop Dis"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"1760","DOI":"10.1377\/hlthaff.28.6.1760","article-title":"A business plan to help the \u2018global South\u2019 in its fight against neglected diseases","volume":"28","author":"SE Frew","year":"2009","journal-title":"Health Aff"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"e1289","DOI":"10.1371\/journal.pntd.0001289","article-title":"Efficacy of a low-cost, inactivated whole-cell oral cholera vaccine: results from 3 years of follow-up of a randomized, controlled trial","volume":"5","author":"D Sur","year":"2011","journal-title":"PLoS Negl Trop Dis"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1093\/infdis\/158.2.372","article-title":"Cross-protection by B subunit-whole cell cholera vaccine against diarrhea associated with heat-labile toxin-producing enterotoxigenic Escherichia coli: results of a large-scale field trial","volume":"158","author":"JD Clemens","year":"1988","journal-title":"J Infect Dis"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1128\/CVI.00543-12","article-title":"Insights from natural infection-derived immunity to cholera instruct vaccine efforts","volume":"19","author":"MF Pasetti","year":"2012","journal-title":"Clin Vaccine Immunol"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"1343","DOI":"10.1093\/cid\/cir141","article-title":"Oral vaccines against cholera","volume":"52","author":"S Shin","year":"2011","journal-title":"Clin Infect Dis"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"e1006","DOI":"10.1371\/journal.pntd.0001006","article-title":"Use of oral cholera vaccines in an outbreak in Vietnam: a case control study","volume":"5","author":"DD Anh","year":"2011","journal-title":"PLoS Negl Trop Dis"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"e952","DOI":"10.1371\/journal.pntd.0000952","article-title":"The case for reactive mass oral cholera vaccinations","volume":"5","author":"R Reyburn","year":"2011","journal-title":"PLoS Negl Trop Dis"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"1574","DOI":"10.1038\/nbt1293-1574","article-title":"Large-scale production of Vibrio cholerae toxin B subunit for use in oral vaccines","volume":"11","author":"M Lebens","year":"1993","journal-title":"Biotechnology (N Y)"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1006\/prep.1994.1071","article-title":"Recombinant cholera toxin B subunit in Escherichia coli: high-level secretion, purification, and characterization","volume":"5","author":"P Slos","year":"1994","journal-title":"Protein Expr Purif"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1111\/j.1574-695X.1998.tb01141.x","article-title":"Affinity purification of recombinant cholera toxin B subunit oligomer expressed in Bacillus brevis for potential human use as a mucosal adjuvant","volume":"20","author":"Y Yasuda","year":"1998","journal-title":"FEMS Immunol Med Microbiol"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1111\/j.1574-6968.1993.tb06389.x","article-title":"Very efficient extracellular production of cholera toxin B subunit using Bacillus brevis","volume":"111","author":"Y Ichikawa","year":"1993","journal-title":"FEMS Microbiol Lett"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1111\/j.1574-6968.1998.tb13295.x","article-title":"Production of cholera toxin B subunit in Lactobacillus","volume":"169","author":"P Slos","year":"1998","journal-title":"FEMS Microbiol Lett"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1016\/j.vaccine.2011.11.059","article-title":"Merozoite surface protein-1 of Plasmodium yoelii fused via an oligosaccharide moiety of cholera toxin B subunit glycoprotein expressed in yeast induced protective immunity against lethal malaria infection in mice","volume":"30","author":"T Miyata","year":"2012","journal-title":"Vaccine"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"831704","DOI":"10.1155\/2011\/831704","article-title":"Protection against autoimmune diabetes by silkworm-produced GFP-tagged CTB-insulin fusion protein","volume":"2011","author":"Q Meng","year":"2011","journal-title":"Clin Dev Immunol"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"13584","DOI":"10.1073\/pnas.0405297101","article-title":"A mucosally targeted subunit vaccine candidate eliciting HIV-1 transcytosis-blocking Abs","volume":"101","author":"N Matoba","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1038\/nbt0398-292","article-title":"Efficacy of a food plant-based oral cholera toxin B subunit vaccine","volume":"16","author":"T Arakawa","year":"1998","journal-title":"Nat Biotechnol"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1007\/s12033-010-9359-1","article-title":"Expression of a cholera toxin B subunit-neutralizing epitope of the porcine epidemic diarrhea virus fusion gene in transgenic lettuce (Lactuca sativa L.)","volume":"48","author":"NX Huy","year":"2011","journal-title":"Mol Biotechnol"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1007\/s12033-008-9086-z","article-title":"Expression and assembly of cholera toxin B subunit (CTB) in transgenic carrot (Daucus carota L.)","volume":"41","author":"YS Kim","year":"2009","journal-title":"Mol Biotechnol"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"10986","DOI":"10.1073\/pnas.0703766104","article-title":"Rice-based mucosal vaccine as a global strategy for cold-chain- and needle-free vaccination","volume":"104","author":"T Nochi","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1111\/j.1467-7652.2008.00381.x","article-title":"Biochemical and immunological characterization of the plant-derived candidate human immunodeficiency virus type 1 mucosal vaccine CTB-MPR","volume":"7","author":"N Matoba","year":"2009","journal-title":"Plant Biotechnol J"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.bbagen.2005.07.003","article-title":"Controlling N-linked glycan site occupancy","volume":"1726","author":"J Jones","year":"2005","journal-title":"Biochimica et biophysica acta"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1146\/annurev.biochem.73.011303.073752","article-title":"Roles of N-linked glycans in the endoplasmic reticulum","volume":"73","author":"A Helenius","year":"2004","journal-title":"Annu Rev Biochem"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1023\/A:1020336332392","article-title":"Expression of cholera toxin B subunit in transgenic tomato plants","volume":"11","author":"D Jani","year":"2002","journal-title":"Transgenic Res"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.jbiotec.2006.06.002","article-title":"Ubiquitin fusion enhances cholera toxin B subunit expression in transgenic plants and the plant-expressed protein binds GM1 receptors more efficiently","volume":"127","author":"S Mishra","year":"2006","journal-title":"J Biotechnol"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1002\/1097-0290(20010220)72:4<490::AID-BIT1011>3.0.CO;2-0","article-title":"Purified cholera toxin B subunit from transgenic tobacco plants possesses authentic antigenicity","volume":"72","author":"XG Wang","year":"2001","journal-title":"Biotechnol Bioeng"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1586\/erv.10.83","article-title":"Plant glycans: friend or foe in vaccine development?","volume":"9","author":"D Bosch","year":"2010","journal-title":"Expert Rev Vaccines"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"2042","DOI":"10.1016\/j.vaccine.2005.01.006","article-title":"Magnifection\u2013a new platform for expressing recombinant vaccines in plants","volume":"23","author":"Y Gleba","year":"2005","journal-title":"Vaccine"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"6852","DOI":"10.1073\/pnas.0400149101","article-title":"In planta engineering of viral RNA replicons: efficient assembly by recombination of DNA modules delivered by Agrobacterium","volume":"101","author":"S Marillonnet","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"e11143","DOI":"10.1371\/journal.pone.0011143","article-title":"HIV-1 neutralization profile and plant-based recombinant expression of actinohivin, an Env glycan-specific lectin devoid of T-cell mitogenic activity","volume":"5","author":"N Matoba","year":"2010","journal-title":"PLoS One"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"5047","DOI":"10.1016\/j.vaccine.2006.03.045","article-title":"Humoral immune responses by prime-boost heterologous route immunizations with CTB-MPR(649\u2013684), a mucosal subunit HIV\/AIDS vaccine candidate","volume":"24","author":"N Matoba","year":"2006","journal-title":"Vaccine"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"218","DOI":"10.2174\/157016208784324994","article-title":"Transcytosis-blocking abs elicited by an oligomeric immunogen based on the membrane proximal region of HIV-1 gp41 target non-neutralizing epitopes","volume":"6","author":"N Matoba","year":"2008","journal-title":"Curr HIV Res"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1007\/978-1-61737-957-4_11","article-title":"Recombinant protein expression in Nicotiana","volume":"701","author":"N Matoba","year":"2011","journal-title":"Methods Mol Biol"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"e22635","DOI":"10.1371\/journal.pone.0022635","article-title":"Investigation of griffithsin&apos;s interactions with human cells confirms its outstanding safety and efficacy profile as a microbicide candidate","volume":"6","author":"JC Kouokam","year":"2011","journal-title":"PLoS One"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.jbiotec.2009.12.006","article-title":"Heat-stable oral alga-based vaccine protects mice from Staphylococcus aureus infection","volume":"145","author":"IA Dreesen","year":"2010","journal-title":"J Biotechnol"},{"key":"ref45","first-page":"Unit 3 19","article-title":"Isolation of mouse small intestinal intraepithelial lymphocytes, Peyer&apos;s patch, and lamina propria cells","volume":"3","author":"L Lefrancois","year":"2001","journal-title":"Curr Protoc Immunol Chapter"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1128\/JVI.01583-08","article-title":"Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies","volume":"83","author":"NA Doria-Rose","year":"2009","journal-title":"J Virol"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"4272","DOI":"10.1128\/IAI.61.10.4272-4279.1993","article-title":"Optimizing oral vaccines: induction of systemic and mucosal B-cell and antibody responses to tetanus toxoid by use of cholera toxin as an adjuvant","volume":"61","author":"RJ Jackson","year":"1993","journal-title":"Infect Immun"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1128\/IAI.10.2.320-327.1974","article-title":"Cyclic adenosine monophosphate and alteration of Chinese hamster ovary cell morphology: a rapid, sensitive in vitro assay for the enterotoxins of Vibrio cholerae and Escherichia coli","volume":"10","author":"RL Guerrant","year":"1974","journal-title":"Infect Immun"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/0165-1161(80)90188-0","article-title":"Validation of conditions for efficient detection of HPRT and APRT mutations in suspension-cultured Chinese hamster ovary cells","volume":"74","author":"LH Thompson","year":"1980","journal-title":"Mutat Res"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"2418","DOI":"10.1128\/IAI.63.7.2418-2423.1995","article-title":"Purification and characterization of a Chinese hamster ovary cell elongation factor of Vibrio hollisae","volume":"63","author":"MH Kothary","year":"1995","journal-title":"Infect Immun"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1093\/protein\/11.7.577","article-title":"The affinity of cholera toxin for Ni2+ ion","volume":"11","author":"MT Dertzbaugh","year":"1998","journal-title":"Protein Eng"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1111\/j.1467-7652.2008.00330.x","article-title":"Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure","volume":"6","author":"R Strasser","year":"2008","journal-title":"Plant Biotechnol J"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1248\/bpb.32.796","article-title":"The significance of glycosylation analysis in development of biopharmaceuticals","volume":"32","author":"N Kawasaki","year":"2009","journal-title":"Biol Pharm Bull"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1038\/nchembio.148","article-title":"Emerging methods for the production of homogeneous human glycoproteins","volume":"5","author":"JR Rich","year":"2009","journal-title":"Nat Chem Biol"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1111\/j.1467-7652.2009.00495.x","article-title":"Production of pharmaceutical-grade recombinant aprotinin and a monoclonal antibody product using plant-based transient expression systems","volume":"8","author":"GP Pogue","year":"2010","journal-title":"Plant Biotechnol J"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1586\/erv.10.85","article-title":"Transient expression systems for plant-derived biopharmaceuticals","volume":"9","author":"TV Komarova","year":"2010","journal-title":"Expert Rev Vaccines"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"1755","DOI":"10.1111\/j.1365-2958.1991.tb01925.x","article-title":"Analysis of structure and function of the B subunit of cholera toxin by the use of site-directed mutagenesis","volume":"5","author":"MG Jobling","year":"1991","journal-title":"Mol Microbiol"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1006\/jmbi.1998.2076","article-title":"The 1.25 A resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site","volume":"282","author":"EA Merritt","year":"1998","journal-title":"J Mol Biol"},{"key":"ref59","first-page":"389","article-title":"Fluorescence-based thermal shift assays","volume":"13","author":"R Zhang","year":"2010","journal-title":"Curr Opin Drug Discov Devel"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/j.jbiotec.2009.09.015","article-title":"Expression of hemagglutinin-neuraminidase glycoprotein of newcastle disease Virus in agroinfiltrated Nicotiana benthamiana plants","volume":"144","author":"E Gomez","year":"2009","journal-title":"J Biotechnol"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"12002","DOI":"10.1128\/JVI.00940-10","article-title":"Immunization with plant-expressed hemagglutinin protects chickens from lethal highly pathogenic avian influenza virus H5N1 challenge infection","volume":"84","author":"D Kalthoff","year":"2010","journal-title":"J Virol"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"6370","DOI":"10.1128\/AEM.01146-10","article-title":"Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and heterologous signal peptides","volume":"76","author":"C Degering","year":"2010","journal-title":"Appl Environ Microbiol"},{"key":"ref63","unstructured":"GenScript website. Available: <comment><ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/www.genscript.com\/cgi-bin\/tools\/rare_codon_analysis\" xlink:type=\"simple\">http:\/\/www.genscript.com\/cgi-bin\/tools\/rare_codon_analysis<\/ext-link><\/comment>. Accessed 2013 Jan 7."},{"key":"ref64","unstructured":"ExPASy website. Available: <comment><ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/web.expasy.org\/protparam\/\" xlink:type=\"simple\">http:\/\/web.expasy.org\/protparam\/<\/ext-link><\/comment>. Accessed 2013 Jan 7."},{"key":"ref65","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1002\/pro.5560030202","article-title":"Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide","volume":"3","author":"EA Merritt","year":"1994","journal-title":"Protein Sci"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"29953","DOI":"10.1074\/jbc.270.50.29953","article-title":"Kinetics of acid-mediated disassembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. Molecular basis of pH stability","volume":"270","author":"LW Ruddock","year":"1995","journal-title":"J Biol Chem"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1038\/nri3251","article-title":"Recent progress in mucosal vaccine development: potential and limitations","volume":"12","author":"N Lycke","year":"2012","journal-title":"Nat Rev Immunol"},{"key":"ref68","doi-asserted-by":"crossref","first-page":"1235","DOI":"10.1093\/infdis\/163.6.1235","article-title":"Field trial of oral cholera vaccines in Bangladesh: serum vibriocidal and antitoxic antibodies as markers of the risk of cholera","volume":"163","author":"JD Clemens","year":"1991","journal-title":"J Infect Dis"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1038\/306551a0","article-title":"Cholera toxin genes: nucleotide sequence, deletion analysis and vaccine development","volume":"306","author":"JJ Mekalanos","year":"1983","journal-title":"Nature"},{"key":"ref70","doi-asserted-by":"crossref","first-page":"8794","DOI":"10.1073\/pnas.0914121107","article-title":"Secretory IgA-mediated protection against V. cholerae and heat-labile enterotoxin-producing enterotoxigenic Escherichia coli by rice-based vaccine","volume":"107","author":"D Tokuhara","year":"2010","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref71","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1128\/IAI.24.3.774-779.1979","article-title":"Antigenic specificity of neutralizing antibody to cholera toxin","volume":"24","author":"JW Peterson","year":"1979","journal-title":"Infect Immun"},{"key":"ref72","doi-asserted-by":"crossref","first-page":"349","DOI":"10.4161\/hv.7.3.14266","article-title":"Emerging antibody products and Nicotiana manufacturing","volume":"7","author":"KJ Whaley","year":"2011","journal-title":"Hum Vaccin"}],"container-title":["PLoS Neglected Tropical Diseases"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pntd.0002046","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,7,23]],"date-time":"2020-07-23T07:00:45Z","timestamp":1595487645000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pntd.0002046"}},"subtitle":[],"editor":[{"given":"Mauricio Martins","family":"Rodrigues","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2013,3,7]]},"references-count":72,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2013,3,7]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pntd.0002046","relation":{},"ISSN":["1935-2735"],"issn-type":[{"value":"1935-2735","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,3,7]]}}}