+1 Recommend
2 collections
      • Record: found
      • Abstract: found
      • Article: found

      IgA antibody production by intrarectal immunization of mice using recombinant major capsid protein of hamster polyomavirus

      Read this article at

          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.


          Viral proteins are highly antigenic and known as potent stimulators of adaptive immune responses. This mechanism is often used for biotechnological applications in monoclonal antibody production resulting in high-affinity IgG antibodies in most cases. The aim of this study was to increase antigen-specific IgA antibody levels in mice in order to generate monoclonal IgA antibodies by hybridoma technology. For this purpose, hamster polyomavirus (HaPyV) major capsid protein VP1 was used to immunize mice by different routes in order to induce VP1-specific IgA titers. Recombinant HaPyV-VP1 was generated in Escherichia coli and administered intraperitoneally, orally, and intrarectally. VP1-specific antibodies were determined by ELISA in sera and organ culture supernatants. We found a significant increase of HaPyV-VP1-specific IgAs in spleen organ cultures after rectal immunization of mice but not in cultures of mesenteric lymph nodes, colon, or Peyer's patches. In contrast, oral and intraperitoneal immunization did not provide an appropriate specific IgA induction at all. These results show that specific IgA antibodies can be induced by intrarectal immunization in the spleen. The generation of monoclonal IgA antibodies with well-defined properties is a useful tool for the investigation of mucosal immune responses or autoimmune diseases and extends the spectrum of antibodies with specific effector functions.

          Related collections

          Most cited references20

          • Record: found
          • Abstract: found
          • Article: not found

          Virus-like particles: Passport to immune recognition

          Virus-like particles (VLPs) are formed by the self-assembly of envelope and/or capsid proteins from many viruses. In many cases such VLPs have structural characteristics and antigenicity similar to the parental virus, and some have already proven successful as vaccines against the cognate virus infection. The structural components of some VLPs have also proven amenable to the insertion or fusion of foreign antigenic sequences, allowing the production of chimeric VLPs exposing the foreign antigen on their surface. Other VLPs have been used as carriers for foreign antigens, including non-protein antigens, via chemical conjugation. This review outlines some of the advantages, disadvantages, and technical considerations for the use of a wide range of VLP systems in vaccine development.
            • Record: found
            • Abstract: found
            • Article: not found

            IgA and the IgA Fc receptor.

            IgA has traditionally been regarded a non-inflammatory antibody. This might indeed be true for secretory IgA (SIgA), which exerts its function at mucosal surfaces where commensal microorganisms and dietary antigens prevail. Serum IgA, however, potently triggers (pro)-inflammatory activity upon binding to the myeloid IgA receptor, FcalphaRI. Here, new insights in the roles of IgA and FcalphaRI are addressed and a model integrating the various functions of IgA in immunity is discussed.
              • Record: found
              • Abstract: found
              • Article: not found

              Oral immunization with recombinant Norwalk virus-like particles induces a systemic and mucosal immune response in mice.

              Recombinant Norwalk virus-like particles (rNV VLPs) produced in insect cells were evaluated as an oral immunogen in CD1 and BALB/c mice by monitoring rNV-specific serum total and subclass immunoglobulin G (IgG) and intestinal IgA responses. Dose and kinetics of response were evaluated in the presence and absence of the mucosal adjuvant cholera toxin (CT). rNV-specific serum IgG and intestinal IgA were detected in the absence of CT, and the number of responders was not significantly different from that of mice administered VLPs with CT at most doses. The use of CT was associated with induction of higher levels of IgG in serum; this effect was greater at higher doses of VLPs. IgG in serum was detected in the majority of animals by 9 days postimmunization (dpi), and intestinal IgA responses were detected by 24 dpi. In the absence of CT, IgG2b was the dominant IgG subclass response in both mouse strains. Thus, nonreplicating rNV VLPs are immunogenic when administered orally in the absence of any delivery system or mucosal adjuvant. These studies demonstrate that rNV VLPs are an excellent model to study the oral delivery of antigen, and they are a potential mucosal vaccine for NV infections.

                Author and article information

                European Journal of Microbiology and Immunology
                Akadémiai Kiadó, co-published with Springer Science+Business Media B.V., Formerly Kluwer Academic Publishers B.V.
                1 September 2012
                : 2
                : 3
                : 231-238
                [ 1 ] Junior Research Group “Antibody Technologies,” Department of Biotechnology, Institute of Biochemistry and Biology, Potsdam University, Potsdam, Germany
                [ 2 ] Beuth University of Applied Sciences, Berlin, Germany
                [ 3 ] Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute for Novel and Emerging Infectious Diseases, Greifswald — Insel Riems, Germany
                Author notes
                [* ] +49-331-97-75348, +49-331-97-75061, katja.heilmann@ 123456uni-potsdam.de
                Original Articles

                Medicine,Immunology,Health & Social care,Microbiology & Virology,Infectious disease & Microbiology
                hybridoma technology,monoclonal Antibodies,IgA immune responses,polyomavirus capsid proteins,intrarectal immunization


                Comment on this article