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193 results on '"Wigdorovitz, Andrés"'

1. IgY Industries and Markets

Author

Vieira-Pires, Ricardo S., Ahn, Hyeong Chul, Bok, Marina, Caulfield, Catherine D., Chacana, Pablo, Elahi, Fazle, Larsson, Anders O., Leiva, Carlos Leónidas, Moran, Leonard M., Morgan, Patricia M., Parreño, Viviana, Vega, Celina G., Wigdorovitz, Andrés, Zhang, Xiao-Ying, editor, Vieira-Pires, Ricardo S., editor, Morgan, Patricia M., editor, and Schade, Rüdiger, editor

Published
2021
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3. SARS-CoV-2 Specific Nanobodies Neutralize Different Variants of Concern and Reduce Virus Load in the Brain of h-ACE2 Transgenic Mice

Author

Pavan, María Florencia, Bok, Marina, Betanzos San Juan, Rafael, Malito, Juan Pablo, Marcoppido, Gisela Ariana, Franco, Diego Rafael, Militelo, Daniela Ayelen, Schammas, Juan Manuel, Bari, Sara Elizabeth, Stone, William, López, Krisangel, Porier, Danielle LaBrie, Muller, John Anthony, Auguste, Albert Jonathan, Yuan, Lijuan, Wigdorovitz, Andrés, Parreño, Viviana Gladys, Ibañez, Lorena Itat, Pavan, María Florencia, Bok, Marina, Betanzos San Juan, Rafael, Malito, Juan Pablo, Marcoppido, Gisela Ariana, Franco, Diego Rafael, Militelo, Daniela Ayelen, Schammas, Juan Manuel, Bari, Sara Elizabeth, Stone, William, López, Krisangel, Porier, Danielle LaBrie, Muller, John Anthony, Auguste, Albert Jonathan, Yuan, Lijuan, Wigdorovitz, Andrés, Parreño, Viviana Gladys, and Ibañez, Lorena Itat

Abstract

Since the beginning of the COVID-19 pandemic, there has been a significant need to develop antivirals and vaccines to combat the disease. In this work, we developed llama-derived nanobodies (Nbs) directed against the receptor binding domain (RBD) and other domains of the Spike (S) protein of SARS-CoV-2. Most of the Nbs with neutralizing properties were directed to RBD and were able to block S-2P/ACE2 interaction. Three neutralizing Nbs recognized the N-terminal domain (NTD) of the S-2P protein. Intranasal administration of Nbs induced protection ranging from 40% to 80% after challenge with the WA1/2020 strain in k18-hACE2 transgenic mice. Interestingly, protection was associated with a significant reduction in virus replication in nasal turbinates and a reduction in virus load in the brain. Employing pseudovirus neutralization assays, we identified Nbs with neutralizing capacity against the Alpha, Beta, Delta, and Omicron variants, including a Nb capable of neutralizing all variants tested. Furthermore, cocktails of different Nbs performed better than individual Nbs at neutralizing two Omicron variants (B.1.529 and BA.2). Altogether, the data suggest the potential of SARS-CoV-2 specific Nbs for intranasal treatment of COVID-19 encephalitis.

Published
2024

6. SARS-CoV-2 Specific Nanobodies Neutralize Different Variants of Concern and Reduce Virus Load in the Brain of h-ACE2 Transgenic Mice

Author

Pavan, María Florencia, primary, Bok, Marina, additional, Betanzos San Juan, Rafael, additional, Malito, Juan Pablo, additional, Marcoppido, Gisela Ariana, additional, Franco, Diego Rafael, additional, Militelo, Daniela Ayelen, additional, Schammas, Juan Manuel, additional, Bari, Sara Elizabeth, additional, Stone, William, additional, López, Krisangel, additional, Porier, Danielle LaBrie, additional, Muller, John Anthony, additional, Auguste, Albert Jonathan, additional, Yuan, Lijuan, additional, Wigdorovitz, Andrés, additional, Parreño, Viviana Gladys, additional, and Ibañez, Lorena Itat, additional

Published
2024
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7. Anti-hemagglutinin monomeric nanobody provides prophylactic immunity against H1 subtype influenza A viruses.

Author

Barbieri, Elena Susana, Sosa-Holt, Carla, Ibañez, Lorena Itati, Baztarrica, Josefina, Garaicoechea, Lorena, Gay, Claire Lindsey, Caceres, Carlos Joaquin, Aduriz, Matias, Baumeister, Elsa, Escribano, José Angel, Perez, Daniel, Wigdorovitz, Andrés, Parreño, Gladys Viviana, and Puntel, Mariana

Subjects
INFLUENZA viruses, IMMUNITY, C-terminal residues, N-terminal residues, ANTIBODY formation, H7N9 Influenza, SWINE influenza
Abstract

Influenza viruses constitute a major threat to human health globally. The viral surface glycoprotein hemagglutinin (HA) is the immunodominant antigen, contains the site for binding to the cellular receptor (RBS), and it is the major target of neutralizing antibody responses post-infection. We developed llama-derived single chain antibody fragments (VHHs) specific for type A influenza virus. Four VHHs were identified and further characterized. VHH D81 bound residues in the proximity of the C-terminal region of HA1 of H1 and H5 subtypes, and showed weak neutralizing activity, whereas VHH B33 bound residues in the proximity of the N-terminal region of the HA's stem domain (HA2) of H1, H5, and H9 subtypes, and showed no neutralizing activity. Of most relevance, VHHs E13 and G41 recognized highly conserved conformational epitopes on the H1 HA's globular domain (HA1) and showed high virus neutralizing activity (ranging between 0.94 to 0.01μM), when tested against several human H1N1 isolates. Additionally, E13 displayed abrogated virus replication of a panel of H1N1 strains spanning over 80 years of antigenic drift and isolated from human, avian, and swine origin. Interestingly, E13 conferred protection in vivo at a dose as low as 0.05 mg/kg. Mice treated with E13 intranasally resulted in undetectable virus challenge loads in the lungs at day 4 post-challenge. The transfer of sterilizing pan-H1 immunity, by a dose in the range of micrograms given intranasally, is of major significance for a monomeric VHH and supports the further development of E13 as an immunotherapeutic agent for the mitigation of influenza infections. [ABSTRACT FROM AUTHOR]

Published
2024
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8. Heterologous booster with a novel formulation containing glycosylated trimeric S protein is effective against Omicron

Author

Bottero, Daniela, primary, Rudi, Erika, additional, Martin Aispuro, Pablo, additional, Zurita, Eugenia, additional, Gaillard, Emilia, additional, Gonzalez Lopez Ledesma, Maria M., additional, Malito, Juan, additional, Stuible, Matthew, additional, Ambrosis, Nicolas, additional, Durocher, Yves, additional, Gamarnik, Andrea V., additional, Wigdorovitz, Andrés, additional, and Hozbor, Daniela, additional

Published
2023
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11. Nanobodies against SARS-CoV-2 reduced virus load in the brain of challenged mice and neutralized Wuhan, Delta and Omicron Variants

Author

Pavan, María Florencia, primary, Bok, Marina, additional, Betanzos San Juan, Rafael, additional, Malito, Juan Pablo, additional, Marcoppido, Gisela Ariana, additional, Franco, Diego Rafael, additional, Militello, Daniela Ayelen, additional, Schammas, Juan Manuel, additional, Bari, Sara, additional, Stone, William B., additional, López, Krisangel, additional, Porier, Danielle, additional, Muller, John, additional, Auguste, Albert Jonathan, additional, Yuan, Lijuan, additional, Wigdorovitz, Andrés, additional, Parreno, Viviana, additional, and Ibañez, Lorena Itatí, additional

Published
2023
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13. Nanobodies against SARS-CoV-2 reduced virus load in the brain of challenged mice and neutralized Wuhan, Delta and Omicron Variants

Author

Pavan, María Florencia, Bok, Marina, Juan, Rafael Betanzos San, Malito, Juan Pablo, Marcoppido, Gisela Ariana, Franco, Diego Rafael, Militello, Daniela Ayelen, Schammas, Juan Manuel, Bari, Sara, Stone, William B., López, Krisangel, Porier, Danielle L., Muller, John, Auguste, Albert J., Yuan, Lijuan, Wigdorovitz, Andrés, Parreño, Viviana, and Ibañez, Lorena Itatí

Subjects
Article
Abstract

In this work, we developed llama-derived nanobodies (Nbs) directed to the receptor binding domain (RBD) and other domains of the Spike (S) protein of SARS-CoV-2. Nanobodies were selected after the biopanning of two VHH-libraries, one of which was generated after the immunization of a llama ( lama glama ) with the bovine coronavirus (BCoV) Mebus, and another with the full-length pre-fused locked S protein (S-2P) and the RBD from the SARS-CoV-2 Wuhan strain (WT). Most of the neutralizing Nbs selected with either RBD or S-2P from SARS-CoV-2 were directed to RBD and were able to block S- 2P/ACE2 interaction. Three Nbs recognized the N-terminal domain (NTD) of the S-2P protein as measured by competition with biliverdin, while some non-neutralizing Nbs recognize epitopes in the S2 domain. One Nb from the BCoV immune library was directed to RBD but was non-neutralizing. Intranasal administration of Nbs induced protection ranging from 40% to 80% against COVID-19 death in k18-hACE2 mice challenged with the WT strain. Interestingly, protection was not only associated with a significant reduction of virus replication in nasal turbinates and lungs, but also with a reduction of virus load in the brain. Employing pseudovirus neutralization assays, we were able to identify Nbs with neutralizing capacity against the Alpha, Beta, Delta and Omicron variants. Furthermore, cocktails of different Nbs performed better than individual Nbs to neutralize two Omicron variants (B.1.529 and BA.2). Altogether, the data suggest these Nbs can potentially be used as a cocktail for intranasal treatment to prevent or treat COVID-19 encephalitis, or modified for prophylactic administration to fight this disease.

Published
2023

14. Immunological study of COVID-19 vaccine candidate based on recombinant spike trimer protein from different SARS-CoV-2 variants of concern

Author

Rudi, Erika, Martin Aispuro, Pablo, Zurita, Eugenia, Gonzalez Lopez Ledesma, Maria M., Bottero, Daniela, Malito, Juan, Gabrielli, Magali, Gaillard, Emilia, Stuible, Matthew, Durocher, Yves, Gamarnik, Andrea V., Wigdorovitz, Andrés, and Hozbor, Daniela

Subjects
Mice, COVID-19 Vaccines, SARS-CoV-2, Immunoglobulin G, Immunology, Interleukin-17, Spike Glycoprotein, Coronavirus, Immunology and Allergy, Animals, COVID-19, Humans, Antibodies, Viral, Antibodies, Neutralizing
Abstract

The emergency of new SARS-CoV-2 variants that feature increased immune escape marks an urgent demand for better vaccines that will provide broader immunogenicity. Here, we evaluated the immunogenic capacity of vaccine candidates based on the recombinant trimeric spike protein (S) of different SARS-CoV-2 variants of concern (VOC), including the ancestral Wuhan, Beta and Delta viruses. In particular, we assessed formulations containing either single or combined S protein variants. Our study shows that the formulation containing the single S protein from the ancestral Wuhan virus at a concentration of 2µg (SW2-Vac 2µg) displayed in the mouse model the highest IgG antibody levels against all the three (Wuhan, Beta, and Delta) SARS-CoV-2 S protein variants tested. In addition, this formulation induced significantly higher neutralizing antibody titers against the three viral variants when compared with authorized Gam-COVID-Vac-rAd26/rAd5 (Sputnik V) or ChAdOx1 (AstraZeneca) vaccines. SW2-Vac 2µg was also able to induce IFN-gamma and IL-17, memory CD4 populations and follicular T cells. Used as a booster dose for schedules performed with different authorized vaccines, SW2-Vac 2µg vaccine candidate also induced higher levels of total IgG and IgG isotypes against S protein from different SARS-CoV-2 variants in comparison with those observed with homologous 3-dose schedule of Sputnik V or AstraZeneca. Moreover, SW2-Vac 2µg booster induced broadly strong neutralizing antibody levels against the three tested SARS-CoV-2 variants. SW2-Vac 2µg booster also induced CD4+ central memory, CD4+ effector and CD8+ populations. Overall, the results demonstrate that SW2-Vac 2 µg is a promising formulation for the development of a next generation COVID-19 vaccine.

Published
2022

21. Development of Nanobodies against Mal de Río Cuarto virus major viroplasm protein P9-1 for diagnostic sandwich ELISA and immunodetection

Author

Llauger, Gabriela, primary, Monti, Demián, additional, Adúriz, Matías, additional, Romão, Ema, additional, Dumón, Analía Delina, additional, Mattio, María Fernanda, additional, Wigdorovitz, Andrés, additional, Muyldermans, Serge, additional, Vincke, Cécile, additional, Parreño, Viviana, additional, and Vas, Mariana del, additional

Published
2021
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23. Development of a platform process for the production and purification of single‐domain antibodies

Author

Koch Institute for Integrative Cancer Research at MIT, Massachusetts Institute of Technology. Department of Chemical Engineering, Massachusetts Institute of Technology. Department of Biological Engineering, Crowell, Laura E, Goodwine, Chaz, Holt, Carla S, Rocha, Lucia, Vega, Celina, Rodriguez, Sergio A, Dalvie, Neil C, Tracey, Mary K, Puntel, Mariana, Wigdorovitz, Andrés, Parreño, Viviana, Love, Kerry R, Cramer, Steven M, Love, J Christopher, Koch Institute for Integrative Cancer Research at MIT, Massachusetts Institute of Technology. Department of Chemical Engineering, Massachusetts Institute of Technology. Department of Biological Engineering, Crowell, Laura E, Goodwine, Chaz, Holt, Carla S, Rocha, Lucia, Vega, Celina, Rodriguez, Sergio A, Dalvie, Neil C, Tracey, Mary K, Puntel, Mariana, Wigdorovitz, Andrés, Parreño, Viviana, Love, Kerry R, Cramer, Steven M, and Love, J Christopher

Abstract

Single-domain antibodies (sdAbs) offer the affinity and therapeutic value of conventional antibodies, with increased stability and solubility. Unlike conventional antibodies, however, sdAbs do not benefit from a platform manufacturing process. While successful production of a variety of sdAbs has been shown in numerous hosts, purification methods are often molecule specific or require affinity tags, which generally cannot be used in clinical manufacturing due to regulatory concerns. Here, we have developed a broadly applicable production and purification process for sdAbs in Komagataella phaffii (Pichia pastoris) and demonstrated the production of eight different sdAbs at a quality appropriate for nonclinical studies. We developed a two-step, integrated purification process without the use of affinity resins and showed that modification of a single process parameter, pH of the bridging buffer, was required for the successful purification of a variety of sdAbs. Further, we determined that this parameter can be predicted based only on the biophysical characteristics of the target molecule. Using these methods, we produced nonclinical quality sdAbs as few as 5 weeks after identifying the product sequence. Nonclinical studies of three different sdAbs showed that molecules produced using our platform process conferred protection against viral shedding of rotavirus or H1N1 influenza and were equivalent to similar molecules produced in Escherichia coli and purified using affinity tags.

Published
2021

24. Development of a platform process for the production and purification of single‐domain antibodies

Author

Crowell, Laura E., primary, Goodwine, Chaz, additional, Holt, Carla S., additional, Rocha, Lucia, additional, Vega, Celina, additional, Rodriguez, Sergio A., additional, Dalvie, Neil C., additional, Tracey, Mary K., additional, Puntel, Mariana, additional, Wigdorovitz, Andrés, additional, Parreño, Viviana, additional, Love, Kerry R., additional, Cramer, Steven M., additional, and Love, J. Christopher, additional

Published
2021
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26. Foot-and-Mouth Disease: Optimization, Reproducibility, and Scalability of High-Yield Production of Virus-Like Particles for a Next-Generation Vaccine

Author

Mignaqui, Ana Clara, primary, Ferella, Alejandra, additional, Cass, Brian, additional, Mukankurayija, Larissa, additional, L'Abbé, Denis, additional, Bisson, Louis, additional, Sánchez, Cintia, additional, Scian, Romina, additional, Cardillo, Sabrina Beatriz, additional, Durocher, Yves, additional, and Wigdorovitz, Andrés, additional

Published
2020
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28. Erratum to: Safety and efficacy of an E2 glycoprotein subunit vaccine produced in mammalian cells to prevent experimental infection with bovine viral diarrhoea virus in cattle

Author

Pecora, Andrea, Aguirreburualde, María Sol Pérez, Ostachuk, Agustín, Aguirreburualde, Alejandra, Leunda, Maria Rosa, Odeon, Anselmo, Chiavenna, Sebastián, Bochoeyer, Diego, Spitteler, Marcelo, Filippi, Jorge L., Santos, Maria J. Dus, Levy, Susana M., and Wigdorovitz, Andrés

Published
2016
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30. A novel MHC‐II targeted BVDV subunit vaccine induces a neutralizing immunological response in guinea pigs and cattle.

Author

Bellido, Demian, Baztarrica, Josefina, Rocha, Lucía, Pecora, Andrea, Acosta, Mario, Escribano, José M., Parreño, Viviana, and Wigdorovitz, Andrés

Subjects
CULLING of animals, ANIMAL vaccination, CYTOSKELETAL proteins, HISTOCOMPATIBILITY testing, CATTLE, GUINEA pigs
Abstract

Bovine viral diarrhoea virus (BVDV) is a major cause of economic loss in the cattle industry, worldwide. Infection results in reduced productive performance, growth retardation, reduced milk production and increased susceptibility to other diseases leading to early culling of animals. There are two primary methods used to control the spread of BVDV: the elimination of persistently infected (PI) animals and vaccination. Currently, modified live or inactivated vaccines are used in BVDV vaccination programmes, but there are safety risks or insufficient protection, respectively, with these vaccines. Here, we report the development and efficacy of the first targeted subunit vaccine against BVDV. The core of the vaccine is the fusion of the BVDV structural protein, E2, to a single‐chain antibody, APCH, together termed, APCH‐E2. The APCH antibody targets the E2 antigen to the major histocompatibility type II molecule (MHC‐II) present on antigen‐presenting cells. Industrial production of the vaccine is carried out using the baculovirus expression vector system (BEVS) using single‐use manufacturing technologies. This new subunit vaccine induces strong BVDV‐specific neutralizing antibodies in guinea pigs and cattle. Importantly, in cattle with low levels of natural BVDV‐specific neutralizing antibodies, the vaccine induced strong neutralizing antibody levels to above the protective threshold, as determined by a competition ELISA. The APCH‐E2 vaccine induced a rapid and sustained neutralizing antibody response compared with a conventional vaccine in cattle. [ABSTRACT FROM AUTHOR]

Published
2021
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37. A synthetic biology approach for consistent production of plant-made recombinant polyclonal antibodies against snake venom toxins

Author

Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes, Ministerio de Ciencia, Innovación y Universidades, Ministerio de Economía, Industria y Competitividad, Ministerio de Economía y Competitividad, Julve Parreño, Jose Manuel, Huet, Estefania, Fernandez-del-Carmen, Asun, Segura, Alvaro, Venturi, Micol, Gandia, Antoni, Pan, Wei-song, Albaladejo, Irene, Forment Millet, José Javier, Pla, Davinia, Wigdorovitz, Andrés, Calvete, Juan J., Gutierrez, Carlos, Gutiérrez, José María, GRANELL RICHART, ANTONIO, Orzáez Calatayud, Diego Vicente, Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes, Ministerio de Ciencia, Innovación y Universidades, Ministerio de Economía, Industria y Competitividad, Ministerio de Economía y Competitividad, Julve Parreño, Jose Manuel, Huet, Estefania, Fernandez-del-Carmen, Asun, Segura, Alvaro, Venturi, Micol, Gandia, Antoni, Pan, Wei-song, Albaladejo, Irene, Forment Millet, José Javier, Pla, Davinia, Wigdorovitz, Andrés, Calvete, Juan J., Gutierrez, Carlos, Gutiérrez, José María, GRANELL RICHART, ANTONIO, and Orzáez Calatayud, Diego Vicente

Abstract

[EN] Antivenoms developed from the plasma of hyperimmunized animals are the only effective treatment available against snakebite envenomation but shortage of supply contributes to the high morbidity and mortality toll of this tropical disease. We describe a synthetic biology approach to affordable and cost-effective antivenom production based on plant-made recombinant polyclonal antibodies (termed pluribodies). The strategy takes advantage of virus superinfection exclusion to induce the formation of somatic expression mosaics in agroinfiltrated plants, which enables the expression of complex antibody repertoires in a highly reproducible manner. Pluribodies developed using toxin-binding genetic information captured from peripheral blood lymphocytes of hyperimmunized camels recapitulated the overall binding activity of the immune response. Furthermore, an improved plant-made antivenom (plantivenom) was formulated using an invitro selected pluribody against Bothrops asper snake venom toxins and has been shown to neutralize a wide range of toxin activities and provide protection against lethal venom doses in mice.

Published
2018

41. A synthetic biology approach for consistent production of plant-made recombinant polyclonal antibodies against snake venom toxins

Author

Julve Parreño, Jose Manuel, primary, Huet, Estefanía, additional, Fernández-del-Carmen, Asun, additional, Segura, Alvaro, additional, Venturi, Micol, additional, Gandía, Antoni, additional, Pan, Wei-song, additional, Albaladejo, Irene, additional, Forment, Javier, additional, Pla, Davinia, additional, Wigdorovitz, Andrés, additional, Calvete, Juan J., additional, Gutiérrez, Carlos, additional, Gutiérrez, José María, additional, Granell, Antonio, additional, and Orzáez, Diego, additional

Published
2017
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42. Plant-produced viral bovine vaccines: What happened during the last ten years?

Author

Ruiz, Vanesa, Mozgovoj, Marina Valeria, Dus Santos, María José, and Wigdorovitz, Andrés

Subjects
Otras Biotecnología Agropecuaria, CIENCIAS AGRÍCOLAS, VACCINES, VLP, Biotecnología Agropecuaria, BOVINE, VIRUS, purl.org/becyt/ford/4.4 [https], PLANT, MOLECULAR FARMING, purl.org/becyt/ford/4 [https]
Abstract

Vaccination has proved to be an efficient strategy to deal with viral infections in both human and animal species. However, protection of cattle against viral infections is still a major concern in veterinary science. During the last two decades, the development of efficient plant‐based expression strategies for recombinant proteins prompted the application of this methodology for veterinary vaccine purposes. The main goals of viral bovine vaccines are to improve the health and welfare of cattle and increase the production of livestock, in a cost‐effective manner. This review explores some of the more prominent recent advances in plant‐made viral bovine vaccines against foot‐and‐mouth disease virus (FMDV), bovine rotavirus (BRV), bovine viral diarrhoea virus (BVDV), bluetongue virus (BTV) and bovine papillomavirus (BPV), some of which are considered to be the most important viral causative agents of economic loss in cattle production. Fil: Ruiz, Vanesa. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Mozgovoj, Marina Valeria. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Dus Santos, María José. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Wigdorovitz, Andrés. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina

Published
2015
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43. Development of an enhanced bovine viral diarrhea virus subunitvaccine based on E2 glycoprotein fused to a single chain antibodywhich targets to antigen-presenting cells

Author

Pecora, Andrea, Malacari, Darío A., Pérez Aguirreburualde, María Sol, Bellido, Demian, Escribano, José M., Dus Santos, María José, and Wigdorovitz, Andrés

Subjects
Ciencias Biológicas, purl.org/becyt/ford/1 [https], Otras Ciencias Biológicas, Glucoproteína E2, Vacuna a subunidad, Virus de la diarrea viral bovina, Baculovirus, purl.org/becyt/ford/1.6 [https], Anticuerpo de cadena simple, CIENCIAS NATURALES Y EXACTAS
Abstract

El virus de la diarrea viral bovina (BVDV) es causante de importantes pérdidas económicas a nivel mundial. La proteína E2 es la inmunodominante del virus y es la candidata para desarrollar vacunas de subunidad. Para mejorar su inmunogenicidad, una versión truncada de la E2 (tE2) se fusionó a un anticuerpo de cadena simple (APCH), que se dirige a las células presentadoras de antígeno. Se expresaron las proteínas APCH-tE2 y tE2 en el sistema de baculovirus y su inmunogenicidad fue evaluada y comparada en cobayos; la proteína APCH-tE2 fue la que indujo la mejor respuesta humoral. Por dicha razón se la evaluó en bovinos utilizando 1,5 μg de antígeno. Los animales presentaron altos títulos de anticuerpos neutralizantes contra BVDV hasta un año posinmunización. Esta nueva vacuna está en proceso de escalado y se transfirió al sector privado. Actualmente se está evaluando para su registro como la primera vacuna argentina de subunidad para bovinos. Bovine viral diarrhea virus (BVDV) is an important cause of economic losses world-wide. E2 is an immunodominant protein and a promising candidate to develop subunit vaccines.To improve its immunogenicity, a truncated E2 (tE2) was fused to a single chain antibody named APCH, which targets to antigen-presenting cells. APCH-tE2 and tE2 proteins were expressed inthe baculovirus system and their immunogenicity was firstly compared in guinea pigs. APCH-tE2 vaccine was the best one to evoke a humoral response, and for this reason, it was selected fora cattle vaccination experiment. All the bovines immunized with 1.5 µg of APCH-tE2 developedhigh levels of neutralizing antibodies against BVDV up to a year post-immunization, demon-strating its significant potential as a subunit vaccine. This novel vaccine is undergoing scale-upand was transferred to the private sector. Nowadays, it is being evaluated for registration asthe first Argentinean subunit vaccine for cattle. Fil: Pecora, Andrea. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina Fil: Malacari, Darío A.. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina Fil: Pérez Aguirreburualde, María Sol. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Bellido, Demian. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Vetanco; Argentina Fil: Escribano, José M.. Algenex; España Fil: Dus Santos, María José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina Fil: Wigdorovitz, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina

Published
2015

44. The efficacy of ELISA commercial kits for the screening of equineinfectious anemia virus infection

Author

Alvarez, Irene, Cipolini Galarza, Fabiana, Wigdorovitz, Andrés, Trono, Karina Gabriela, and Barrandeguy, María Edith

Subjects
Ciencias Biológicas, purl.org/becyt/ford/1 [https], DIAGNÓSTICO, Otras Ciencias Biológicas, VIRUS DE LA ANEMIA INFECCIOSA EQUINA, ELISA, purl.org/becyt/ford/1.6 [https], CIENCIAS NATURALES Y EXACTAS
Abstract

El mejor indicador de la infección por el virus de la anemia infecciosa equina (Equine infectious anemia virus, EIAV) es la detección de anticuerpos específicos en el suero del caballo. En el presente trabajo se evaluó la capacidad de detección de anticuerpos contra EIAV de dos equipos de ELISA comerciales utilizando 302 muestras de suero equino, así como las ventajas potenciales de su uso como herramientas de screening. Ambos ensayos de ELISA presentaron 100 % de sensibilidad diagnóstica y una especificidad diagnóstica del orden de 92,3 a 94,3 %. Las muestras discordantes fueron analizadas por inmunoblot. Los resultados mostraron que las dos pruebas ELISA son muy eficientes para detectar animales infectados por EIAV, al permitir identificar un mayor número de animales positivos que la prueba de inmunodifusión en gel de agar, oficialmente aprobada en la República Argentina para la certificación de los animales. Las pruebas de ELISA constituyen herramientas muy útiles en los programas de control y de erradicación de la infección por EIAV. The most used and reliable indicator of equine infectious anemia virus (EIAV) infec-tion is the detection of its specific antibodies in horse serum. In the present study, theperformance of two commercial ELISA tests for the detection of EIAV antibodies as well asthe potential advantages of their use as an EIAV infection screening tool were evaluated in 302horse serum samples. Both ELISA assays showed 100% diagnostic sensitivity, and 92.3-94.3%diagnostic specificity. Discordant results were analyzed by immunoblot. The results showedthat both ELISA tests are very efficient at detecting EIAV infected animals, allowing to identifya higher number of positive horse cases. Thus, ELISA assays can be useful tools in EIA controland eradication. Fil: Alvarez, Irene. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina Fil: Cipolini Galarza, Fabiana. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina Fil: Wigdorovitz, Andrés. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina Fil: Trono, Karina Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina Fil: Barrandeguy, María Edith. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Virología; Argentina. Universidad del Salvador. Escuela de Veterinaria; Argentina

Published
2015

46. A synthetic biology approach for consistent production of plant‐made recombinant polyclonal antibodies against snake venom toxins.

Author

Julve Parreño, Jose Manuel, Huet, Estefanía, Fernández‐del‐Carmen, Asun, Segura, Alvaro, Venturi, Micol, Gandía, Antoni, Pan, Wei‐song, Albaladejo, Irene, Forment, Javier, Pla, Davinia, Wigdorovitz, Andrés, Calvete, Juan J., Gutiérrez, Carlos, Gutiérrez, José María, Granell, Antonio, and Orzáez, Diego

Subjects
SYNTHETIC biology, RECOMBINANT antibodies, SNAKE venom, ANTIVENINS, PHYTOTHERAPY
Abstract

Abstract: Antivenoms developed from the plasma of hyperimmunized animals are the only effective treatment available against snakebite envenomation but shortage of supply contributes to the high morbidity and mortality toll of this tropical disease. We describe a synthetic biology approach to affordable and cost‐effective antivenom production based on plant‐made recombinant polyclonal antibodies (termed pluribodies). The strategy takes advantage of virus superinfection exclusion to induce the formation of somatic expression mosaics in agroinfiltrated plants, which enables the expression of complex antibody repertoires in a highly reproducible manner. Pluribodies developed using toxin‐binding genetic information captured from peripheral blood lymphocytes of hyperimmunized camels recapitulated the overall binding activity of the immune response. Furthermore, an improved plant‐made antivenom (plantivenom) was formulated using an in vitro selected pluribody against Bothrops asper snake venom toxins and has been shown to neutralize a wide range of toxin activities and provide protection against lethal venom doses in mice. [ABSTRACT FROM AUTHOR]

Published
2018
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