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      A novel recombinant vaccine protecting mice against abrin intoxication

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          Abstract

          Abrin toxin (AT) consisting of an A chain and a B chain is a potential agent for bioterrorism and an effective vaccine against AT poisoning is urgently required. In this study, AT B chain (ATB) was successfully expressed in the Escherichia coli ( E. coli) and assessed the protection capacity against AT intoxication. The recombinant ATB (rATB) subunit induces a good immune response after 4 immunizations. All BALB/c mice immunized intraperitoneally (i.p.) with the purified rATB protein survived after challenged with 5 × LD 50 of AT. Transfusion of sera from immunized mice provided passive protection in naive mice. Furthermore, histological findings showed that immunization with rATB decreased the severity of toxin-related tissue damage. This work indicates that the rATB protein may be a promising vaccine candidate against human exposure to AT.

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          Characterization of a novel high-affinity monoclonal immunoglobulin G antibody against the ricin B subunit.

          Nicholas J. Mantis, Niamh McGuinness (2006)
          There is an urgent need for the development of a passive immunotherapy against the category B select agent ricin, a lethal ribosome-inactivating toxin composed of an enzymatic A subunit (RTA) and a single binding B subunit (RTB). To date, only one monoclonal antibody (MAb), a mouse immunoglobulin G (IgG1) against RTA called R70, has been deemed sufficiently potent in animal models to warrant further testing in humans. In this study, we have identified and characterized MAb 24B11, a murine IgG1 directed against RTB. In a Vero cell cytotoxicity assay, 24B11 was approximately two times more effective at neutralizing ricin than was R70. The equilibrium dissociation constants of 24B11 (KD = 4.2 x 10(-9) M) and R70 (KD = 3.2 x 10(-9) M) were virtually identical, suggesting that the difference in neutralization activity between the two MAbs was not due to differing affinities for the toxin. 24B11 blocked ricin attachment to galactoside receptors on primary mouse splenocytes and on the apical surfaces of human mucosal epithelial cell monolayers. Surprisingly, R70 also effectively interfered with ricin attachment to receptors on cell surfaces. Using a phage-displayed peptide library, we determined that 24B11 binds an epitope on RTB adjacent to, but not within, one of the two galactose binding domains. Finally, we demonstrate that R70 and 24B11, when combined, function synergistically to neutralize ricin in vitro, raising the possibility that these two MAbs could serve as a novel immunotherapeutic in vivo.
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            Vaccines against the category B toxins: Staphylococcal enterotoxin B, epsilon toxin and ricin.

            Nicholas J. Mantis (2005)
            The threat of bioterrorism worldwide has accelerated the demand for the development of therapies and vaccines against the Category B toxins: staphylococcal enterotoxin B (SEB), epsilon toxin (ETX) produced by Clostridium perfringens types B and D, and ricin, a natural product of the castor bean. The diverse and unique nature of these toxins poses a challenge to vaccinologists. While formalin-inactivated toxins can successfully induce antibody-mediated protection in animals, their usefulness in humans is limited because of potential safety concerns. For this reason, research is now aimed at developing recombinant, attenuated vaccines based on a detailed understanding of the molecular mechanisms by which these toxins function. Vaccine development is further complicated by the fact that as bioterrorism agents, SEB, ETX and ricin would most likely be disseminated as aerosols or in food/water supplies. Our understanding of the mechanisms by which these toxins cross mucosal surfaces, and importance of mucosal immunity in preventing toxin uptake is only rudimentary.
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              Immunoglobulin A antibodies against ricin A and B subunits protect epithelial cells from ricin intoxication.

              Niamh McGuinness, S Farrant, Simon Edwards … (2006)
              Epithelial cells of the respiratory and gastrointestinal tracts are extremely vulnerable to the cytotoxic effects of ricin, a Shiga-like toxin with ribosome-inactivating properties. While mucosal immunity to ricin correlates with secretory immunoglobulin A (IgA) antibody levels in vivo, the potential of IgA to protect epithelial cells from ricin in vitro has not been examined due to the unavailability of well-defined antitoxin IgA antibodies. Here we report the characterization of four monoclonal IgA antibodies (IgA MAbs) produced from the Peyer's patches and mesenteric lymph nodes of BALB/c mice immunized intragastrically with ricin toxoid. Two IgA MAbs (33G2 and 35H6) were active against ricin's lectin subunit (RTB), and two (23D7 and 25A4) reacted with the toxin's enzymatic subunit (RTA). All four IgA MAbs neutralized ricin in a Vero cell cytotoxicity assay, blocked toxin-induced interleukin-8 release by the human monocyte/macrophage cell line 28SC, and protected polarized epithelial cell monolayers from ricin-mediated protein synthesis inhibition. 33G2 and 35H6 reduced ricin binding to the luminal surfaces of human intestinal epithelial cells to undetectable levels in tissue section overlay assays, whereas 23D7 had no effect on toxin attachment. 23D7 and 25A4 did, however, reduce ricin transcytosis across MDCK II cell monolayers, possibly by interfering with intracellular toxin transport. We conclude that IgA antibodies against RTA and RTB can protect mucosal epithelial cells from ricin intoxication.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Hum Vaccin Immunother
                Journal ID (iso-abbrev): Hum Vaccin Immunother
                Journal ID (pmc): KHVI
                Title: Human Vaccines & Immunotherapeutics
                Publisher: Taylor & Francis
                ISSN (Print): 2164-5515
                ISSN (Electronic): 2164-554X
                Publication date (Electronic): 18 June 2015
                Publication date Collection: June 2015
                Volume: 11
                Issue: 6
                Pages: 1361-1367
                Affiliations
                [1 ]State Key Laboratory of Pathogen and Biosecurity; Beijing Institute of Microbiology and Epidemiology ; Beijing, PR China
                [2 ]Tianjin Key Laboratory for Biomarkers Occupational and Environmental Hazard; Logistics University of Chinese People's Armed Police Force ; Tianjin, PR China
                [3 ]Institute of Military Veterinary; Academy of Military Medical Sciences ; Changchun,, PR China
                Author notes
                [* ]Correspondence to: Wensen Liu; Email: liuws85952@ 123456163.com ; Jinglin Wang; Email: wjl0801@ 123456vip.163.com
                Article
                Publisher ID: 1008879
                DOI: 10.1080/21645515.2015.1008879
                PMC ID: 4514378
                PubMed ID: 26086588
                SO-VID: 2bdfd41e-ff91-4d23-9e62-bba817e7b22d
                Copyright © © 2015 The Author(s). Published with license by Taylor & Francis Group, LLC© Junhong Wang, Shan Gao, Wenwen Xin, Lin Kang, Na Xu, Tao Zhang, Wensen Liu, and Jinglin Wang
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License ( http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

                History
                Date received : 10 October 2014
                Date revision received : 1 December 2014
                Date accepted : 11 December 2014
                Page count
                Figures: 5, Tables: 1, References: 26, Pages: 7
                Categories
                Subject: Research Paper

                ScienceOpen disciplines: Molecular medicine
                Keywords: abrin toxin,b chain,bioterrorism,immunogen,vaccine candidate
                Data availability:
                ScienceOpen disciplines: Molecular medicine
                Keywords: abrin toxin, b chain, bioterrorism, immunogen, vaccine candidate

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