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[PMID]:27605982
[Au] Autor:Oluwayelu DO; Adebiyi AI
[Ad] Endereço:Department of Veterinary Microbiology & Parasitology, University of Ibadan, Ibadan, Nigeria.
[Ti] Título:Plantibodies in human and animal health: a review.
[So] Source:Afr Health Sci;16(2):640-5, 2016 Jun.
[Is] ISSN:1729-0503
[Cp] País de publicação:Uganda
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Antibodies are essential part of vertebrates' adaptive immune system; they can now be produced by transforming plants with antibody-coding genes from mammals/humans. Although plants do not naturally make antibodies, the plant-derived antibodies (plantibodies) have been shown to function in the same way as mammalian antibodies. METHODS: PubMed and Google search engines were used to download relevant publications on plantibodies in medical and veterinary fields; the papers were reviewed and findings qualitatively described. RESULTS: The process of bioproduction of plantibodies offers several advantages over the conventional method of antibody production in mammalian cells with the cost of antibody production in plants being substantially lesser. Contrary to what is possible with animal-derived antibodies, the process of making plantibodies almost exclusively precludes transfer of pathogens to the end product. Additionally, plants not only produce a relatively high yield of antibodies in a comparatively faster time, they also serve as cost-effective bioreactors to produce antibodies of diverse specificities. CONCLUSION: Plantibodies are safe, cost-effective and offer more advantages over animal-derived antibodies. Methods of producing them are described with a view to inspiring African scientists on the need to embrace and harness this rapidly evolving biotechnology in solving human and animal health challenges on the continent where the climate supports growth of diverse plants.
[Mh] Termos MeSH primário: Formação de Anticorpos/imunologia
Imunomodulação
Planticorpos/administração & dosagem
Planticorpos/imunologia
[Mh] Termos MeSH secundário: Animais
Formação de Anticorpos/fisiologia
Nível de Saúde
Seres Humanos
Nigéria
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Plantibodies)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170414
[Lr] Data última revisão:
170414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160909
[St] Status:MEDLINE
[do] DOI:10.4314/ahs.v16i2.35


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[PMID]:27605983
[Au] Autor:Tumwine JK
[Ad] Endereço:College of Health Sciences, Makerere University and Editor in Chief African Health Sciences.
[Ti] Título:From MNHC, NCDs to prevention of infectious diseases and plantibodies: meeting challenges of our times.
[So] Source:Afr Health Sci;16(2):i-iii, 2016 Jun.
[Is] ISSN:1729-0503
[Cp] País de publicação:Uganda
[La] Idioma:eng
[Mh] Termos MeSH primário: Controle de Doenças Transmissíveis/organização & administração
Promoção da Saúde
Planticorpos
[Mh] Termos MeSH secundário: Serviços de Saúde da Criança/organização & administração
Doenças Transmissíveis/epidemiologia
Doenças Transmissíveis/terapia
Países em Desenvolvimento
Feminino
Seres Humanos
Recém-Nascido
Masculino
Serviços de Saúde Materna/organização & administração
Sociedades Médicas
África do Sul
[Pt] Tipo de publicação:EDITORIAL
[Nm] Nome de substância:
0 (Plantibodies)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170414
[Lr] Data última revisão:
170414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160909
[St] Status:MEDLINE
[do] DOI:10.4314/ahs.v16i2.1


  3 / 73 MEDLINE  
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[PMID]:26865596
[Au] Autor:Choi YS; Moon JH; Kim TG; Lee JY
[Ad] Endereço:Department of Maxillofacial Biomedical Engineering, School of Dentistry, and Institute of Oral Biology, Kyung Hee University, Seoul, Republic of Korea Department of Dental Hygiene, Shinsung University, Chungnam, Republic of Korea.
[Ti] Título:Potent In Vitro and In Vivo Activity of Plantibody Specific for Porphyromonas gingivalis FimA.
[So] Source:Clin Vaccine Immunol;23(4):346-52, 2016 Apr.
[Is] ISSN:1556-679X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fimbrial protein fimbrillin (FimA), a major structural subunit of Porphyromonas gingivalis, has been suggested as a vaccine candidate to control P. gingivalis-induced periodontal disease. Previously, cDNAs encoding IgG monoclonal antibodies (MAbs) against purified FimA from P. gingivalis 2561 have been cloned, and the MAbs have been produced in rice cell suspension. Here we examined the biological activities of the plant-produced MAb specific for FimA (anti-FimA plantibody) of P. gingivalis in vitro and in vivo. The anti-FimA plantibody recognized oligomeric/polymeric forms of native FimA in immunoblot analysis and showed high affinity for native FimA (KD = 0.11 nM). Binding of P. gingivalis (10(8) cells) to 2 mg of saliva-coated hydroxyapatite beads was reduced by 53.8% in the presence of 1 µg/ml plantibody. Anti-FimA plantibody (10 µg/ml) reduced invasion of periodontal ligament cells by P. gingivalis (multiplicity of infection, 100) by 68.3%. Intracellular killing of P. gingivalis opsonized with the anti-FimA plantibody by mouse macrophages was significantly increased (77.1%) compared to killing of bacterial cells with irrelevant IgG (36.7%). In a mouse subcutaneous chamber model, the number of recoverable P. gingivalis cells from the chamber fluid was significantly reduced when the numbers of bacterial cells opsonized with anti-FimA plantibody were compared with the numbers of bacterial cells with irrelevant IgG, 66.7% and 37.1%, respectively. These in vitro and in vivo effects of anti-FimA plantibody were comparable to those of the parental MAb. Further studies with P. gingivalis strains with different types of fimbriae are needed to investigate the usefulness of anti-FimA plantibody for passive immunization to control P. gingivalis-induced periodontal disease.
[Mh] Termos MeSH primário: Proteínas de Fímbrias/imunologia
Planticorpos/imunologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Animais
Aderência Bacteriana/efeitos dos fármacos
Carga Bacteriana
Infecções por Bacteroidaceae/microbiologia
Infecções por Bacteroidaceae/prevenção & controle
Células Cultivadas
Modelos Animais de Doenças
Endocitose/efeitos dos fármacos
Feminino
Seres Humanos
Macrófagos/imunologia
Masculino
Camundongos Endogâmicos C57BL
Viabilidade Microbiana/efeitos dos fármacos
Oryza
Fagocitose
Porphyromonas gingivalis/imunologia
Porphyromonas gingivalis/fisiologia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Plantibodies); 0 (fimbrillin); 147680-16-8 (Fimbriae Proteins)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160212
[St] Status:MEDLINE
[do] DOI:10.1128/CVI.00620-15


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[PMID]:25879373
[Au] Autor:Marusic C; Novelli F; Salzano AM; Scaloni A; Benvenuto E; Pioli C; Donini M
[Ad] Endereço:Laboratory of Biotechnology, ENEA Research Center Casaccia, Rome, Italy.
[Ti] Título:Production of an active anti-CD20-hIL-2 immunocytokine in Nicotiana benthamiana.
[So] Source:Plant Biotechnol J;14(1):240-51, 2016 Jan.
[Is] ISSN:1467-7652
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Anti-CD20 murine or chimeric antibodies (Abs) have been used to treat non-Hodgkin lymphomas (NHLs) and other diseases characterized by overactive or dysfunctional B cells. Anti-CD20 Abs demonstrated to be effective in inducing regression of B-cell lymphomas, although in many cases patients relapse following treatment. A promising approach to improve the outcome of mAb therapy is the use of anti-CD20 antibodies to deliver cytokines to the tumour microenvironment. In particular, IL-2-based immunocytokines have shown enhanced antitumour activity in several preclinical studies. Here, we report on the engineering of an anti-CD20-human interleukin-2 (hIL-2) immunocytokine (2B8-Fc-hIL2) based on the C2B8 mAb (Rituximab) and the resulting ectopic expression in Nicotiana benthamiana. The scFv-Fc-engineered immunocytokine is fully assembled in plants with minor degradation products as assessed by SDS-PAGE and gel filtration. Purification yields using protein-A affinity chromatography were in the range of 15-20 mg/kg of fresh leaf weight (FW). Glycopeptide analysis confirmed the presence of a highly homogeneous plant-type glycosylation. 2B8-Fc-hIL2 and the cognate 2B8-Fc antibody, devoid of hIL-2, were assayed by flow cytometry on Daudi cells revealing a CD20 binding activity comparable to that of Rituximab and were effective in eliciting antibody-dependent cell-mediated cytotoxicity of human PBMC versus Daudi cells, demonstrating their functional integrity. In 2B8-Fc-hIL2, IL-2 accessibility and biological activity were verified by flow cytometry and cell proliferation assay. To our knowledge, this is the first example of a recombinant immunocytokine based on the therapeutic Rituximab antibody scaffold, whose expression in plants may be a valuable tool for NHLs treatment.
[Mh] Termos MeSH primário: Antígenos CD20/imunologia
Interleucina-2/biossíntese
Tabaco/genética
[Mh] Termos MeSH secundário: Agrobacterium/metabolismo
Sequência de Aminoácidos
Citotoxicidade Celular Dependente de Anticorpos
Western Blotting
Seres Humanos
Extratos Vegetais/metabolismo
Folhas de Planta/metabolismo
Planticorpos/química
Planticorpos/isolamento & purificação
Plantas Geneticamente Modificadas
Ligação Proteica
Engenharia de Proteínas
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD20); 0 (Interleukin-2); 0 (Plant Extracts); 0 (Plantibodies)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150417
[St] Status:MEDLINE
[do] DOI:10.1111/pbi.12378


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[PMID]:26709700
[Au] Autor:Wang B; Swaminathan S; Bhattacharyya MK
[Ad] Endereço:Department of Agronomy, Iowa State University, Ames, 50011-1010, United States of America.
[Ti] Título:Identification of Fusarium virguliforme FvTox1-Interacting Synthetic Peptides for Enhancing Foliar Sudden Death Syndrome Resistance in Soybean.
[So] Source:PLoS One;10(12):e0145156, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Soybean is one of the most important crops grown across the globe. In the United States, approximately 15% of the soybean yield is suppressed due to various pathogen and pests attack. Sudden death syndrome (SDS) is an emerging fungal disease caused by Fusarium virguliforme. Although growing SDS resistant soybean cultivars has been the main method of controlling this disease, SDS resistance is partial and controlled by a large number of quantitative trait loci (QTL). A proteinacious toxin, FvTox1, produced by the pathogen, causes foliar SDS. Earlier, we demonstrated that expression of an anti-FvTox1 single chain variable fragment antibody resulted in reduced foliar SDS development in transgenic soybean plants. Here, we investigated if synthetic FvTox1-interacting peptides, displayed on M13 phage particles, can be identified for enhancing foliar SDS resistance in soybean. We screened three phage-display peptide libraries and discovered four classes of M13 phage clones displaying FvTox1-interacting peptides. In vitro pull-down assays and in vivo interaction assays in yeast were conducted to confirm the interaction of FvTox1 with these four synthetic peptides and their fusion-combinations. One of these peptides was able to partially neutralize the toxic effect of FvTox1 in vitro. Possible application of the synthetic peptides in engineering SDS resistance soybean cultivars is discussed.
[Mh] Termos MeSH primário: Resistência à Doença/genética
Fusarium/patogenicidade
Micotoxinas/imunologia
Doenças das Plantas/imunologia
Planticorpos/genética
Feijão de Soja/microbiologia
[Mh] Termos MeSH secundário: Bacteriófagos/genética
Resistência à Doença/fisiologia
Micotoxinas/metabolismo
Biblioteca de Peptídeos
Peptídeos/genética
Peptídeos/imunologia
Doenças das Plantas/microbiologia
Folhas de Planta/microbiologia
Raízes de Plantas/microbiologia
Planticorpos/imunologia
Plantas Geneticamente Modificadas/genética
Locos de Características Quantitativas/genética
Feijão de Soja/genética
Feijão de Soja/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Mycotoxins); 0 (Peptide Library); 0 (Peptides); 0 (Plantibodies)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151229
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0145156


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[PMID]:26109093
[Au] Autor:Hernández-Velázquez A; López-Quesada A; Ceballo-Cámara Y; Cabrera-Herrera G; Tiel-González K; Mirabal-Ortega L; Pérez-Martínez M; Pérez-Castillo R; Rosabal-Ayán Y; Ramos-González O; Enríquez-Obregón G; Depicker A; Pujol-Ferrer M
[Ad] Endereço:Plant Biotechnology Department, Center for Genetic Engineering and Biotechnology (CIGB), PO Box 6162, 10600, Havana, Havana, Cuba. abel.hernandez@cigb.edu.cu.
[Ti] Título:Tobacco seeds as efficient production platform for a biologically active anti-HBsAg monoclonal antibody.
[So] Source:Transgenic Res;24(5):897-909, 2015 Oct.
[Is] ISSN:1573-9368
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The use of plants as heterologous hosts is one of the most promising technologies for manufacturing valuable recombinant proteins. Plant seeds, in particular, constitute ideal production platforms for long-term applications requiring a steady supply of starting material, as they combine the general advantages of plants as bioreactors with the possibility of biomass storage for long periods in a relatively small volume, thus allowing manufacturers to decouple upstream and downstream processing. In the present work we have used transgenic tobacco seeds to produce large amounts of a functionally active mouse monoclonal antibody against the Hepatitis B Virus surface antigen, fused to a KDEL endoplasmic reticulum retrieval motif, under control of regulatory sequences from common bean (Phaseolus vulgaris) seed storage proteins. The antibody accumulated to levels of 6.5 mg/g of seed in the T3 generation, and was purified by Protein A affinity chromatography combined with SEC-HPLC. N-glycan analysis indicated that, despite the KDEL signal, the seed-derived plantibody bore both high-mannose and complex-type sugars that indicate partial passage through the Golgi compartment, although its performance in the immunoaffinity purification of HBsAg was unaffected. An analysis discussing the industrial feasibility of replacing the currently used tobacco leaf-derived plantibody with this seed-derived variant is also presented.
[Mh] Termos MeSH primário: Antígenos de Superfície da Hepatite B/imunologia
Planticorpos/imunologia
Sementes/imunologia
Tabaco/embriologia
[Mh] Termos MeSH secundário: Cromatografia Líquida de Alta Pressão
Cromatografia Líquida/métodos
Eletroforese em Gel de Poliacrilamida
Antígenos de Superfície da Hepatite B/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hepatitis B Surface Antigens); 0 (Plantibodies)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150626
[St] Status:MEDLINE
[do] DOI:10.1007/s11248-015-9890-8


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[PMID]:25779638
[Au] Autor:Rubio-Infante N; Govea-Alonso DO; Romero-Maldonado A; García-Hernández AL; Ilhuicatzi-Alvarado D; Salazar-González JA; Korban SS; Rosales-Mendoza S; Moreno-Fierros L
[Ad] Endereço:Inmunidad en Mucosas, UBIMED, FES-Iztacala, Universidad Nacional Autónoma de México, Avenida de los Barrios 1, 54090, Tlalnepantla, Mexico.
[Ti] Título:A Plant-Derived Multi-HIV Antigen Induces Broad Immune Responses in Orally Immunized Mice.
[So] Source:Mol Biotechnol;57(7):662-74, 2015 Jul.
[Is] ISSN:1559-0305
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Multi-HIV, a multiepitopic protein derived from both gp120 and gp41 envelope proteins of the human immunodeficiency virus (HIV), has been proposed as a vaccine prototype capable of inducing broad immune responses, as it carries various B and T cell epitopes from several HIV strains. In this study, the immunogenic properties of a Multi-HIV expressed in tobacco chloroplasts are evaluated in test mice. BALB/c mice orally immunized with tobacco-derived Multi-HIV have elicited antibody responses, including both the V3 loop of gp120 and the ELDKWA epitope of gp41. Based on splenocyte proliferation assays, stimulation with epitopes of the C4, V3 domain of gp120, and the ELDKWA domain of gp41 elicits positive cellular responses. Furthermore, specific interferon gamma production is observed in both CD4+ and CD8+ T cells stimulated with HIV peptides. These results demonstrate that plant-derived Multi-HIV induces T helper-specific responses. Altogether, these findings illustrate the immunogenic potential of plant-derived Multi-HIV in an oral immunization scheme. The potential of this low-cost immunization approach and its implications on HIV/AIDS vaccine development are discussed.
[Mh] Termos MeSH primário: Proteína gp120 do Envelope de HIV/biossíntese
Proteína gp41 do Envelope de HIV/biossíntese
Infecções por HIV/imunologia
Planticorpos/imunologia
[Mh] Termos MeSH secundário: Animais
Cloroplastos/imunologia
Epitopos de Linfócito T/imunologia
Proteína gp120 do Envelope de HIV/administração & dosagem
Proteína gp120 do Envelope de HIV/imunologia
Proteína gp41 do Envelope de HIV/administração & dosagem
Proteína gp41 do Envelope de HIV/imunologia
Infecções por HIV/prevenção & controle
Infecções por HIV/virologia
HIV-1/imunologia
HIV-1/patogenicidade
Seres Humanos
Imunização
Camundongos
Tabaco/citologia
Tabaco/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Epitopes, T-Lymphocyte); 0 (HIV Envelope Protein gp120); 0 (HIV Envelope Protein gp41); 0 (Plantibodies); 0 (gp120 protein, Human immunodeficiency virus 1)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150318
[St] Status:MEDLINE
[do] DOI:10.1007/s12033-015-9856-3


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[PMID]:25500833
[Au] Autor:Lozano-Torres JL; Wilbers RH; Warmerdam S; Finkers-Tomczak A; Diaz-Granados A; van Schaik CC; Helder J; Bakker J; Goverse A; Schots A; Smant G
[Ad] Endereço:Laboratory of Nematology, Wageningen University, Wageningen, The Netherlands.
[Ti] Título:Apoplastic venom allergen-like proteins of cyst nematodes modulate the activation of basal plant innate immunity by cell surface receptors.
[So] Source:PLoS Pathog;10(12):e1004569, 2014 Dec.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Despite causing considerable damage to host tissue during the onset of parasitism, nematodes establish remarkably persistent infections in both animals and plants. It is thought that an elaborate repertoire of effector proteins in nematode secretions suppresses damage-triggered immune responses of the host. However, the nature and mode of action of most immunomodulatory compounds in nematode secretions are not well understood. Here, we show that venom allergen-like proteins of plant-parasitic nematodes selectively suppress host immunity mediated by surface-localized immune receptors. Venom allergen-like proteins are uniquely conserved in secretions of all animal- and plant-parasitic nematodes studied to date, but their role during the onset of parasitism has thus far remained elusive. Knocking-down the expression of the venom allergen-like protein Gr-VAP1 severely hampered the infectivity of the potato cyst nematode Globodera rostochiensis. By contrast, heterologous expression of Gr-VAP1 and two other venom allergen-like proteins from the beet cyst nematode Heterodera schachtii in plants resulted in the loss of basal immunity to multiple unrelated pathogens. The modulation of basal immunity by ectopic venom allergen-like proteins in Arabidopsis thaliana involved extracellular protease-based host defenses and non-photochemical quenching in chloroplasts. Non-photochemical quenching regulates the initiation of the defense-related programmed cell death, the onset of which was commonly suppressed by venom allergen-like proteins from G. rostochiensis, H. schachtii, and the root-knot nematode Meloidogyne incognita. Surprisingly, these venom allergen-like proteins only affected the programmed cell death mediated by surface-localized immune receptors. Furthermore, the delivery of venom allergen-like proteins into host tissue coincides with the enzymatic breakdown of plant cell walls by migratory nematodes. We, therefore, conclude that parasitic nematodes most likely utilize venom allergen-like proteins to suppress the activation of defenses by immunogenic breakdown products in damaged host tissue.
[Mh] Termos MeSH primário: Proteínas de Helminto/imunologia
Nematoides/imunologia
Infecções por Nematoides/imunologia
Doenças das Plantas/parasitologia
Imunidade Vegetal/imunologia
Receptores de Superfície Celular/imunologia
Peçonhas/imunologia
[Mh] Termos MeSH secundário: Animais
Antígenos de Helmintos/imunologia
Apoptose/imunologia
Arabidopsis
Imunidade Inata/imunologia
Doenças das Plantas/imunologia
Planticorpos/imunologia
Tylenchoidea
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, Helminth); 0 (Helminth Proteins); 0 (Plantibodies); 0 (Receptors, Cell Surface); 0 (Venoms)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1004569


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[PMID]:25218825
[Au] Autor:Zhang Y; Li D; Jin X; Huang Z
[Ad] Endereço:Vaccine Research Center, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, 200031, China.
[Ti] Título:Fighting Ebola with ZMapp: spotlight on plant-made antibody.
[So] Source:Sci China Life Sci;57(10):987-8, 2014 Oct.
[Is] ISSN:1869-1889
[Cp] País de publicação:China
[La] Idioma:eng
[Mh] Termos MeSH primário: Anticorpos Monoclonais/uso terapêutico
Antivirais/uso terapêutico
Doença pelo Vírus Ebola/tratamento farmacológico
Planticorpos/uso terapêutico
[Mh] Termos MeSH secundário: Animais
Células CHO
Cricetinae
Cricetulus
Seres Humanos
Infectologia/tendências
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antiviral Agents); 0 (Plantibodies); 0 (ZMapp)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:141017
[Lr] Data última revisão:
141017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140915
[St] Status:MEDLINE
[do] DOI:10.1007/s11427-014-4746-7


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[PMID]:24975464
[Au] Autor:Lai H; He J; Hurtado J; Stahnke J; Fuchs A; Mehlhop E; Gorlatov S; Loos A; Diamond MS; Chen Q
[Ad] Endereço:The Biodesign Institute, Arizona State University, Tempe, AZ, USA.
[Ti] Título:Structural and functional characterization of an anti-West Nile virus monoclonal antibody and its single-chain variant produced in glycoengineered plants.
[So] Source:Plant Biotechnol J;12(8):1098-107, 2014 Oct.
[Is] ISSN:1467-7652
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Previously, our group engineered a plant-derived monoclonal antibody (MAb pE16) that efficiently treated West Nile virus (WNV) infection in mice. In this study, we developed a pE16 variant consisting of a single-chain variable fragment (scFv) fused to the heavy chain constant domains (CH) of human IgG (pE16scFv-CH). pE16 and pE16scFv-CH were expressed and assembled efficiently in Nicotiana benthamiana ∆XF plants, a glycosylation mutant lacking plant-specific N-glycan residues. Glycan analysis revealed that ∆XF plant-derived pE16scFv-CH (∆XFpE16scFv-CH) and pE16 (∆XFpE16) both displayed a mammalian glycosylation profile. ∆XFpE16 and ∆XFpE16scFv-CH demonstrated equivalent antigen-binding affinity and kinetics, and slightly enhanced neutralization of WNV in vitro compared with the parent mammalian cell-produced E16 (mE16). A single dose of ∆XFpE16 or ∆XFpE16scFv-CH protected mice against WNV-induced mortality even 4 days after infection at equivalent rates as mE16. This study provides a detailed tandem comparison of the expression, structure and function of a therapeutic MAb and its single-chain variant produced in glycoengineered plants. Moreover, it demonstrates the development of anti-WNV MAb therapeutic variants that are equivalent in efficacy to pE16, simpler to produce, and likely safer to use as therapeutics due to their mammalian N-glycosylation. This platform may lead to a more robust and cost-effective production of antibody-based therapeutics against WNV infection and other infectious, inflammatory or neoplastic diseases.
[Mh] Termos MeSH primário: Anticorpos Antivirais/imunologia
Antígenos Virais/imunologia
Anticorpos de Cadeia Única/imunologia
Tabaco/metabolismo
Febre do Nilo Ocidental/prevenção & controle
Vírus do Nilo Ocidental/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/imunologia
Expressão Gênica
Glicosilação
Seres Humanos
Imunoglobulina G/imunologia
Camundongos
Camundongos Endogâmicos C57BL
Testes de Neutralização
Planticorpos/imunologia
Ressonância de Plasmônio de Superfície
Proteínas do Envelope Viral/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antibodies, Viral); 0 (Antigens, Viral); 0 (Immunoglobulin G); 0 (Plantibodies); 0 (Single-Chain Antibodies); 0 (Viral Envelope Proteins)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140701
[St] Status:MEDLINE
[do] DOI:10.1111/pbi.12217



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