Polyclonal antibodies

At Inmunova we have wide experience in the research of biological therapies based on polyclonal antibodies.

Polyclonal antibodies (PAbs) are a heterogeneous mixture of antibodies usually produced by different B cells clones in the body. They can recognize and bind to many different epitopes of a single antigen. PAbs act by quickly recognizing and neutralizing the virus or toxin, thus avoiding the disease’s progression.

These antibodies are produced by immunizing an animal with a target antigen to stimulate an inmune response. The new generation of equine polyclonal antibodies (EpAbs) includes their processing, purification and the obtaining of F(ab')2 fragments with high purity and adequate safety profile.
EpAbs technology is used to develop medicines, treat medical emergencies such as snakebite and scorpion sting envenomation, severe poisoning (tetanus toxin, digoxin, and more recently, botulinum toxin) and severe infectious diseases like avian influenza.
Unlike monoclonal antibodies that attack the infectious agent by targeting a limited region, polyclonal antibodies recognize and attack different regions of the virus, which allows them to remain effective against possible mutations. The anti-SARS-CoV-2 hyperimmune serum based on EpAbs and developed by Inmunova demonstrated this, since in vitro viral seroneutralization assays showed its neutralizing capacity against Omicron, Delta, Gamma and Alpha variants.
Furthermore, EpAbs can be produced rapidly on a large scale.

Scientific publications

The science is in our DNA and is the base of everything we do.

We cultivate a culture of scientific excellence and innovation and we communicate our findings in specialized journals with peer reviews.

“Development of a anti-Shiga toxin product for prevention of the hemolytic uremic syndrome”. Hiriart Y, Pardo R, Bukata L, Lauché C, Muñoz L, Colonna M, Goldbaum F, Sanguineti S, Zylberman V. Medicina, 2018;78(2):107-112.

“Development of camelid single chain antibodies against Shiga toxin type 2 (Stx2) with therapeutic potential against Hemolytic Uremic Syndrome (HUS)”. Mejias M, Hiriart Y, Lauché C, Fernandez-Brando RJ, Pardo R, Bruballa A, Ramos MV, Goldbaum FA, Palermo M and Zylberman V. Scientific Reports, 6: 24913. 2016.

“Protection of mice against Stx2-associated damage by maternal immunization with a Brucella Lumazine Synthase-Stx2 B Subunit Chimera”. Mejias MP, Cabrera G, Fernández-Brando RJ, Baschkier A, Ghersi G, Abrey-Recalde MJ, Miliwebsky E, Meiss R, Goldbaum FA, Zylberman V, Rivas M, Palermo MS. Infection and Immunity, (82-4, 1491-1499) 2014.

“Immunization with a Chimera Consisting of the B Subunit of Shiga Toxin Type 2 and Brucella Lumazine Synthase Confers Total Protection against Shiga Toxins in Mice”. Mejias MP, Ghersi G, Craig PO, Panek CA, Bentancor LV, Baschkier A, Goldbaum FA, Zylberman V and Palermo MS. The Journal of Immunology, 191(5):2403-2411, 2013.

“Polymeric Display of Proteins through High Affinity Leucine Zipper Peptide Adaptors”. Craig PO, Alzogaray V and Goldbaum FA. Biomacromolecules, 13(4):1112-1121, 2012.

“Multiple display of a protein domain on a bacterial polymeric scaffold”. Craig, P. O., Berguer, P. M., Ainciart, N., Zylberman, V., Thomas, M. G , Martinez Tosar, L. J., Bulloj, A., Boccaccio, G.L. and Goldbaum, F. A. Proteins, Structure, Function and Bioinformatics, 1;61(4):1089-1100, 2005.

“Brucella spp. lumazine synthase: a novel antigen delivery system” Sciutto, E., Toledo, A., Cruza, C., Rosas, G., Meneses, G., Laplagne, D., Ainciart, N., Cervantes, J., Fragoso, G. and Goldbaum, F. A. Vaccine, 23(21):2784-90, 2005.

“Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides”. Laplagne, D. A., Zylberman, V., Ainciart, N., Steward M. W., Sciutto, E., Fossati, C. A. and Goldbaum, F. A. Proteins, Structure, Function and Bioinformatics, 57(4):820-828, 2004.

“High order quaternary arrangement confers increased stability to Brucella spp. lumazine synthase”. Zylberman, V., Craig, P., Klinke S., Braden, B.C., Cauerhff, A. and Goldbaum F. A. Journal of Biological Chemistry, 279(9):8093-8101, 2004.


“Safety and effectiveness of RBD-specific polyclonal equine F(ab´)2 fragments for the treatment of hospitalized patients with severe Covid-19 disease: A retrospective cohort study”. Farizano Salazar DH, Achinelli F, Colonna M, Pérez L, Giménez AA, et al. (2022). PLOS ONE 17(9): e0274796.
“Non-clinical safety assessment and in vivo biodistribution of CoviFab, an RBD-specific F(ab’)2 fragment derived from equine polyclonal antibodies”. F. Salinas et al. Toxicology and Applied Pharmacology, Volume 434 (2022) 115796.
“RBD-specific polyclonal F(ab´)2 fragments of equine antibodies in patients with moderate to severe COVID-19 disease: A randomized, multicenter, double-blind, placebo-controlled, adaptive phase 2/3 clinical trial”. G. Lopardo et al. EClinicalMedicine, 34 (2021) 100843.

“Development of a Hyperimmune Equine Serum Therapy for COVID-19 in Argentina”. Zylberman, V., Sanguineti, S., Pontoriero, A. V., Higa, S. V., Cerutti, M. L., Morrone Seijo, S. M., et al. Medicina (Buenos Aires) 2020; Vol. 80 (Supl. III): 1-6.


“Isolated chimeric proteins of modified lumazine synthase”. PCT WO 2005/121330, Diciembre 2005. Fernando Alberto Goldbaum, Diego Andres Laplagne, Vanesa Zylberman, Patricio Craig, Paula Mercedes Berguer, Natalia Ainciart, Carlos Alberto Fossati, Carlos Alejandro Velikovsky, Juliana Cassataro, Guillermo Giambartolomei.

“Chimeras of Brucella lumazine synthase and beta subunit of AB5 toxins”, filed on May 26, 2014, under No. PCT/IB2014/061731, Goldbaum, Fernando; Zylberman, Vanesa; Craig, Patricio; Ghersi, Giselle; Palermo, Marina; Mejías, Pilar; Bentancor. Titulares Inmunova S.A. / Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET).