Ranveig Braathen

• Hinke, Daniëla Maria; Anderson, Ane Marie; Katta, Kirankumar; Laursen, Marlene Fyrstenberg; Tesfaye, Demo Yemane & Werninghaus, Ina Charlotta [Show all 10 contributors for this article] (2024). Applying valency-based immuno-selection to generate broadly cross-reactive antibodies against influenza hemagglutinins. Nature Communications. ISSN 2041-1723. 15(1). doi: 10.1038/s41467-024-44889-w.
• Westhrin, Marita; Blazevski, Jana; Textor, Ana; Abdollahi, Pegah; Gopalakrishnan, Ramakrishna Prabhu & Ngo, Linda Thuy [Show all 13 contributors for this article] (2023). Id-neoantigen vaccine induces therapeutic CD8⁺ T cells against multiple myeloma: H chain-loss escapees cause FLC MM. Journal for ImmunoTherapy of Cancer (JITC). 11:e006944(8), p. 1–13. doi: 10.1136/jitc-2023-006944. Full text in Research Archive
• Werninghaus, Ina Charlotta; Hinke, Daniëla Maria; Fossum, Even; Bogen, Bjarne & Braathen, Ranveig (2023). Neuraminidase delivered as an APC-targeted DNA vaccine induces protective antibodies against influenza. Molecular Therapy. ISSN 1525-0016. 31(7), p. 2188–2205. doi: 10.1016/j.ymthe.2023.03.012. Full text in Research Archive
• Hinke, Daniëla Maria; Andersen, Tor Kristian; Gopalakrishnan, Ramakrishna Prabhu; Skullerud, Lise Madelen; Werninghaus, Ina Charlotta & Grødeland, Gunnveig [Show all 9 contributors for this article] (2022). Antigen bivalency of antigen-presenting cell-targeted vaccines increases B cell responses. Cell reports. ISSN 2211-1247. 39:110901(9), p. 1–27. doi: 10.1016/j.celrep.2022.110901. Full text in Research Archive
• Tesfaye, Demo Yemane; Bobic, Sonja; Lysén, Anna Karin Christina; Huszthy, Peter Csaba; Gudjonsson, Arnar & Braathen, Ranveig [Show all 8 contributors for this article] (2022). Targeting Xcr1 on dendritic cells rapidly induce Th1-associated immune responses that contribute to protection against influenza infection. Frontiers in Immunology. ISSN 1664-3224. 13:752714, p. 1–13. doi: 10.3389/fimmu.2022.752714. Full text in Research Archive
• Bjerkan, Louise; Visweswaran, Ganesh Ram R.; Gudjonsson, Arnar; Labbé, Genevieve M.; Quinkert, Doris & Pattinson, David J. [Show all 10 contributors for this article] (2021). APC-Targeted DNA Vaccination Against Reticulocyte-Binding Protein Homolog 5 Induces Plasmodium falciparum-Specific Neutralizing Antibodies and T Cell Responses. Frontiers in Immunology. ISSN 1664-3224. 12:720550(18), p. 1–13. doi: 10.3389/fimmu.2021.720550. Full text in Research Archive Show summary

  Targeted delivery of antigen to antigen presenting cells (APCs) is an efficient way to induce robust antigen-specific immune responses. Here, we present a novel DNA vaccine that targets the Plasmodium falciparum reticulocyte-binding protein homolog 5 (PfRH5), a leading blood-stage antigen of the human malaria pathogen, to APCs. The vaccine is designed as bivalent homodimers where each chain is composed of an amino-terminal single chain fragment variable (scFv) targeting unit specific for major histocompatibility complex class II (MHCII) expressed on APCs, and a carboxyl-terminal antigenic unit genetically linked by the dimerization unit. This vaccine format, named “Vaccibody”, has previously been successfully applied for antigens from other infectious diseases including influenza and HIV, as well as for tumor antigens. Recently, the crystal structure and key functional antibody epitopes for the truncated version of PfRH5 (PfRH5ΔNL) were characterized, suggesting PfRH5ΔNL to be a promising candidate for next-generation PfRH5 vaccine design. In this study, we explored the APC-targeting strategy for a PfRH5ΔNL-containing DNA vaccine. BALB/c mice immunized with the targeted vaccine induced higher PfRH5-specific IgG1 antibody responses than those vaccinated with a non-targeted vaccine or antigen alone. The APC-targeted vaccine also efficiently induced rapid IFN-γ and IL-4 T cell responses. Furthermore, the vaccine-induced PfRH5-specific IgG showed inhibition of growth of the P. falciparum 3D7 clone parasite in vitro. Finally, sera obtained after vaccination with this targeted vaccine competed for the same epitopes as PfRH5-specific mAbs from vaccinated humans. Robust humoral responses were also induced by a similar P. vivax Duffy-binding protein (PvDBP)-containing targeted DNA vaccine. Our data highlight a novel targeted vaccine platform for the development of vaccines against blood-stage malaria.

• Fossum, Even; Tesfaye, Demo Yemane; Bobic, Sonja; Gudjonsson, Arnar; Braathen, Ranveig & Lahoud, Mireille H. [Show all 8 contributors for this article] (2020). Targeting Antigens to Different Receptors on Conventional Type 1 Dendritic Cells Impacts the Immune Response . Journal of Immunology. ISSN 0022-1767. 205(3), p. 661–673. doi: 10.4049/jimmunol.1901119.
• Braathen, Ranveig; Spång, Heidi Cecilie Larsen; Hinke, Daniëla Maria; Blazevski, Jana; Bobic, Sonja & Fossum, Even [Show all 7 contributors for this article] (2020). A DNA Vaccine That Encodes an Antigen-Presenting Cell-Specific Heterodimeric Protein Protects against Cancer and Influenza . Molecular therapy. Methods & clinical development. ISSN 2399-6951. 17, p. P378–P392. doi: 10.1016/j.omtm.2020.01.007. Full text in Research Archive
• Mahalunkar, Sneha; Yadav, Amit Singh; Gorain, Mahadeo; Pawar, Vinay; Braathen, Ranveig & Weiss, Siegfried [Show all 9 contributors for this article] (2019). Functional design of pH-responsive folate-targeted polymer-coated gold nanoparticles for drug delivery and in vivo therapy in breast cancer. International Journal of Nanomedicine. ISSN 1176-9114. 14, p. 8285–8302. doi: 10.2147/IJN.S215142. Full text in Research Archive
• Huszthy, Peter Csaba; Gopalakrishnan, Ramakrishna Prabhu; Jacobsen, Johanne Tracey; Haabeth, Ole Audun; Løset, Geir Åge & Braathen, Ranveig [Show all 10 contributors for this article] (2019). B cell receptor ligation induces display of V-region peptides on MHC class II molecules to T cells. Proceedings of the National Academy of Sciences of the United States of America. ISSN 0027-8424. 116(51), p. 25850–25859. doi: 10.1073/pnas.1902836116. Full text in Research Archive Show summary

  The B cell receptors (BCRs) for antigen express variable (V) regions that are enormously diverse, thus serving as markers on individual B cells. V region-derived idiotypic (Id) peptides can be displayed as pId:MHCII complexes on B cells for recognition by CD4+ T cells. It is not known if naive B cells spontaneously display pId:MHCII in vivo or if BCR ligation is required for expression, thereby enabling collaboration between Id+ B cells and Id-specific T cells. Here, using a mouse model, we show that naive B cells do not express readily detectable levels of pId:MHCII. However, BCR ligation by Ag dramatically increases physical display of pId:MHCII, leading to activation of Id-specific CD4+ T cells, extrafollicular T-B cell collaboration and some germinal center formation, and production of Id+ IgG. Besides having implications for immune regulation, the results may explain how persistent activation of self-reactive B cells induces the development of autoimmune diseases and B cell lymphomas.

• Lysén, Anna Karin Christina; Braathen, Ranveig; Gudjonsson, Arnar; Tesfaye, Demo Yemane; Bogen, Bjarne & Fossum, Even (2019). Dendritic cell targeted Ccl3- and Xcl1-fusion DNA vaccines differ in induced immune responses and optimal delivery site. Scientific Reports. ISSN 2045-2322. 9:1820, p. 1–11. doi: 10.1038/s41598-018-38080-7. Full text in Research Archive
• Braathen, Ranveig; Spång, Heidi Cecilie Larsen; Lindeberg, Mona Mari; Fossum, Even; Grødeland, Gunnveig & Fredriksen, Agnete [Show all 7 contributors for this article] (2018). The Magnitude and IgG Subclass of Antibodies Elicited by Targeted DNA Vaccine Are Influenced by Specificity for APC Surface Molecules. ImmunoHorizons. ISSN 2573-7732. 2(1), p. 38–53. doi: 10.4049/immunohorizons.1700038. Full text in Research Archive
• Anderson, Ane Marie; Baranowska-Hustad, Marta Natalia; Braathen, Ranveig; Grødeland, Gunnveig & Bogen, Bjarne (2018). Simultaneous targeting of multiple hemagglutinins to APCs for induction of broad immunity against influenza. Journal of Immunology. ISSN 0022-1767. 200(6), p. 2057–2066. doi: 10.4049/jimmunol.1701088.
• Spång, Heidi Cecilie Larsen; Braathen, Ranveig & Bogen, Bjarne (2012). Heterodimeric Barnase-Barstar Vaccine Molecules: Influence of One versus Two Targeting Units Specific for Antigen Presenting Cells. PLOS ONE. ISSN 1932-6203. 7(9). doi: 10.1371/journal.pone.0045393.
• Ghumra, A; Shi, J; McIntosh, RS; Rasmussen, Ingunn B; Braathen, Ranveig & Johansen, Finn Eirik [Show all 13 contributors for this article] (2009). Structural requirements for the interaction of human IgM and IgA with the human Fc alpha/mu receptor. European Journal of Immunology. ISSN 0014-2980. 39(4), p. 1147–1156. doi: 10.1002/eji.200839184.
• Ghumra, A; Semblat, JP; McIntosh, RS; Raza, A; Rasmussen, Ingunn B & Braathen, Ranveig [Show all 11 contributors for this article] (2008). Identification of residues in the C mu 4 domain of polymeric IgM essential for interaction with Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1). Journal of Immunology. ISSN 0022-1767. 181, p. 1988–2000.
• Johansen, Finn Eirik; Braathen, Ranveig; Munthe, Else; Schjerven, Hilde & Brandtzæg, Per (2007). Regulation of the mucosal IgA system. In Kaetzel, CS (Eds.), Mucosal Immune Defense: Immunoglobulin A. Springer Science+Business Media B.V.. ISSN 978-0-387-72231-3. p. 111–143.
• Braathen, Ranveig; Hohman, VS; Brandtzæg, Per & Johansen, Finn Eirik (2007). Secretory antibody formation: Conserved binding interactions between J chain and polymeric Ig receptor from humans and amphibians. Journal of Immunology. ISSN 0022-1767. 178, p. 1589–1597.
• Braathen, Ranveig; Sandvik, Anders; Berntzen, Gøril; Hammerschmidt, S; Fleckenstein, Burkhard & Sandlie, Inger [Show all 9 contributors for this article] (2006). Identification of a polymeric Ig receptor binding phage-displayed peptide that exploits epithelial transcytosis without dimeric IgA competition. Journal of Biological Chemistry. ISSN 0021-9258. 281, p. 7075–7081. Full text in Research Archive
• Elm, C; Braathen, Ranveig; Bergmann, S; Frank, R; Vaerman, JP & Kaetzel, CS [Show all 9 contributors for this article] (2004). Ectodomains 3 and 4 of human polymeric immunoglobulin receptor (hpIgR) mediate invasion of Streptococcus pneumoniae into the epithelium. Journal of Biological Chemistry. ISSN 0021-9258. 279, p. 6296–6304.
• Braathen, Ranveig; Sørensen, Vigdis; Brandtzæg, Per; Sandlie, Inger & Johansen, Finn Eirik (2002). The carboxyl-terminal domains of IgA and IgM direct isotype-specific polymerization and interaction with the polymeric immunoglobulin receptor. Journal of Biological Chemistry. ISSN 0021-9258. 277(45), p. 42755–42762. Full text in Research Archive Show summary

  Mucosal surfaces are protected by polymeric immunoglobulins that are transported across the epithelium by the polymeric immunoglobulin receptor (pIgR). Only polymeric IgA and IgM containing a small polypeptide called the "joining" (J) chain can bind to the pIgR. J chain-positive IgA consists of dimers, and some larger polymers, whereas only IgM pentamers incorporate the J chain. We made domain-swap chimeras between human IgA1 and IgM and found that the COOH-terminal domains of the heavy chains (Ca3 and Cm4, respectively) dictated the size of the polymers formed and also which polymers incorporated the J chain. We also showed that chimeric IgM molecules engineered to contain Ca3 were able to bind the rabbit pIgR. Since the rabbit pIgR normally does not bind IgM, these results suggest that the COOH-terminal domain of the polymeric immunoglobulins is primarily responsible for interaction with the pIgR. Finally, we made a novel chimeric IgA immunoglobulin, containing the terminal domain from IgM. This recombinant molecule formed J chain-containing pentamers that could, like IgA, efficiently form covalent complexes with the human pIgR ectodomain, known as secretory component.

• Johansen, Finn Eirik; Braathen, Ranveig & Brandtzæg, Per (2001). The J chain is essential for polymeric Ig receptor-mediated epithelial transport of IgA. Journal of Immunology. ISSN 0022-1767. 167, p. 5185–5192. Show summary

  Local production of secretory (S)IgA provides adaptive immunologic protection of mucosal surfaces, but SIgA is also protective when administered passively, such as in breast milk. Therefore, SIgA is a potential candidate for therapeutic administration, but its complex structure with four different polypeptide chains produced by two distinct cell types complicates recombinant production. The J chain is critical in the structure of SIgA because it is required for efficient polymerization of IgA and for the affinity of such polymers to the secretory component (SC)/polymeric (p)IgR. To better understand the role of the J chain in SIgA production, we have generated various mutant forms of the human J chain and analyzed the function of these mutants when coexpressed with IgA. We found that the C terminus of the J chain was not required for the formation of IgA polymers, but was essential for the binding of pIgA to SC. Likewise, we found that two of the intrachain disulfide bridges (Cys13:Cys101 and Cys109:Cys134) were also required for the binding of pIgA to SC but, interestingly, not for IgA polymerization. Conversely, the last intrachain disulfide bridge (Cys72:Cys92) was not essential for either of these two J chain functions. Finally, we demonstrated that the presence of only Cys15 or Cys69 was sufficient to support polymerization of IgA, but that these polymers were mostly noncovalently stabilized. Nevertheless, these polymers bound free SC with nearly the same affinity as pIgA containing wild-type J chain, but were transcytosed by pIgR-expressing polarized epithelial cells at a reduced efficiency.

• Johansen, Finn Eirik; Braathen, Ranveig & Brandtzæg, Per (2000). Role of J chain in secretory immunoglobulin formation. Scandinavian Journal of Immunology. ISSN 0300-9475. 52(3), p. 240–248. Show summary

  The joining (J) chain is a small polypeptide, expressed by mucosal and glandular plasma cells, which regulates polymer formation of IgA and IgM. J-chain incorporation into polymeric IgA (pIgA, mainly dimers) and pentameric IgM endows these antibodies with several salient features: a high valency of antigen-binding sites, which make them suitable for agglutinating bacteria and viruses; little or no complement-activating potential, which allow them operate in a non-inflammatory fashion; and, most importantly, only J-chain-containing polymers show high affinity for the polymeric Ig receptor (pIgR), also known as transmembrane secretory component (SC). This epithelial glycoprotein mediates active external transfer of pIgA and pentameric IgM to exocrine secretions. Thus, secretory IgA (SIgA) and SIgM, as well as free SC, are generated by endoproteolytic cleavage of the pIgR extracellular domain. The secretory antibodies form the "first line" of defense against pathogens and noxious substances that favor the mucosae as their portal of entry. The J chain is involved in creating the binding site for pIgR/SC in the Ig polymers not only by determining the polymeric quaternary structure, but apparently also by interacting directly with the receptor protein. Therefore, both the J chain and the pIgR/SC are key proteins in secretory immunity.

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• Fossum, Even; Andersen, Tor Kristian & Braathen, Ranveig (2022). Når gener blir vaksine. Norsk Farmaceutisk Tidsskrift. ISSN 0029-1935. p. 21–24.
• Braathen, Ranveig (2021). Vaksinering mot COVID-19 i Norge.
• Werninghaus, Ina; Hinke, Daniëla Maria; Bogen, Bjarne & Braathen, Ranveig (2021). Neuraminidase in antigen presenting cell-targeted DNA vaccine induces antibody-mediated protection against influenza. Show summary

  Vaccines provide an effective countermeasure against influenza. However, antigenic drift of the virus and varying vaccine efficacy result in a need for novel and flexible vaccine approaches. Conventional influenza vaccines are standardized based on their hemagglutinin (HA) content, however neuraminidase (NA) has also been established as an independent correlate of protection and has great potential as a vaccine antigen. Our lab designed a flexible and rapidly producible DNA vaccine platform, increasing immunogenicity by targeting dimeric vaccine molecules to antigen-presenting cells (APCs). Here, for the first time, NA was included in the APC-targeted DNA vaccine platform encoding MHC class II-targeted heterodimeric antigen-bivalent vaccine proteins. The vaccine with NA was compared to an otherwise identical HA vaccine, which proved successful in previous studies. A single immunization elicited strong and long-lasting NA-specific humoral responses, which had the ability to inhibit NA enzymatic activity. Vaccine-induced NA immunity protected mice completely from challenge with homologous influenza virus. Immunization with NA was overall more effective than the HA-based vaccine and potent at low vaccine doses. Additionally, NA-reactive CD4+ and CD8+ T cells were induced, however protection was mainly antibody-mediated. Furthermore, similarly strong NA-specific immune responses and protection could be obtained with different targeting units as well as dimerization motifs. Overall, our results show that NA is a potent influenza vaccine antigen and can flexibly be used in the APC-targeted DNA vaccine platform. Strategies to combine NA with other influenza antigens like HA to elicit broadened immunity should be explored in future influenza vaccine design.

• Hinke, Daniëla Maria; Andersen, Tor Kristian; Skullerud, Lise Madelen; Werninghaus, Ina; Grødeland, Gunnveig & Fossum, Even [Show all 8 contributors for this article] (2021). Antigen bivalency in antigen presenting cell-targeted vaccines enhances humoral responses. Show summary

  Pathogen-specific antibodies can provide protective immunity against infectious diseases. Vaccine-elicited antibody levels can be increased by targeting antigens to antigen presenting cells (APCs). We hypothesize that antigen multivalency can play an additional role to further enhance antibody responses against APC-targeted vaccines. Here, we examine the role of antigen valency in APC-targeted vaccines delivered in the form of DNA. We designed MHC class II-targeted heterodimeric vaccine molecules that carried either two identical antigens (bivalent vaccines) or two different antigens (monovalent vaccines). Besides antigen valency, the vaccine molecules were identical. Bivalent and monovalent vaccines were compared in their efficiency to induce humoral responses in mice. We found that antigen bivalent vaccine molecules with two identical influenza hemagglutinins (HA) induced higher amounts of anti-HA antibodies than monovalent versions. Furthermore, only MHC class II-targeted HA-bivalent vaccines protected mice completely from challenge with homologous influenza virus. The potentiating effect of antigen bivalency was also obtained with other antigens and APC targeting in the DNA vaccine format, and when delivering vaccines as recombinant protein instead of DNA. In vitro data showed that MHC class II-targeted vaccine proteins aid the clustering of APCs and antigen-specific B cells, suggesting the formation of APC-B cell synapses. We hypothesize that antigen bivalency contributes to efficient cross-linking of B cell receptors within the synapse, resulting in increased B cell responses. Overall, our results indicate that combining antigen bivalency with APC-targeting is an attractive strategy to enhance the immunogenicity of vaccines.

• Laursen, Marlene Fyrstenberg; Daniela Maria, Hinke; Bogen, Bjarne & Braathen, Ranveig (2021). An MHC class II-targeted H1-mix Influenza Vaccine Induces Cross-protective Antibody Responses in Mice. Show summary

  Influenza infections are a major cause of morbidity and mortality worldwide. The surface glycoprotein hemagglutinin (HA) is the primary target for neutralizing antibodies, protecting against influenza infections. Within the influenza A virus (IAV) family, HA subtypes H1-H18 exist. In humans, circulating IAVs belonging to H1 and H3 subtypes cause seasonal influenza. Applying influenza vaccines can lower the burden of influenza disease. However, minor genetic mutations causing substitutions of single amino acids in the HA sequence lead to antigenic drift and immune escape of the virus. This lowers the efficacy of current vaccines and annual revaccination is needed. To develop novel influenza vaccines which more broadly protect immunized individuals without the need of an annual boost is consequently of high interest. In our studies, we combined HAs from 4 different H1N1 IAVs into an MHC class II-targeting heterodimeric DNA H1-mix vaccine (H1-mix). Vaccinated mice were followed for several weeks and antibody responses analyzed by ELISA. The H1-mix induced antibodies against a variety of H1s as well as against other subtypes not included in the mix. Furthermore, mice vaccinated with the H1-mix showed complete protection against a heterologous viral infection with the H1N1 virus A/Puerto Rico/8/1934 (PR8), which was not included in the mix. Mice vaccinated with the individual H1s used in the mix vaccine, showed no protection against PR8. This strategy enables an easy adaption of the vaccine to better protect against drifted viral strains, probably by inducing cross-reactive antibodies. This is an important step towards generating a universal influenza vaccine.

• Grødeland, Gunnveig; Fossum, Even & Braathen, Ranveig (2021). Vaksinepodden.no: Beskyttende effekt.
• Grødeland, Gunnveig; Fossum, Even & Braathen, Ranveig (2021). Vaksinepodden: Vokterceller og T-celler.
• Grødeland, Gunnveig; Fossum, Even & Braathen, Ranveig (2021). Vaksinepodden: RNA-vaksiner: Før, nå og fremover.
• Lysén, Anna Karin Christina; Braathen, Ranveig; Gudjonsson, Arnar; Tesfaye, Demo Yemane; Bogen, Bjarne & Fossum, Even (2020). Author Correction: Dendritic cell targeted Ccl3- and Xcl1-fusion DNA vaccines differ in induced immune responses and optimal delivery site (Scientific Reports, (2019), 9, 1, (1820), 10.1038/s41598-018-38080-7). Scientific Reports. ISSN 2045-2322. 10(1). doi: 10.1038/s41598-020-62688-3.
• Braathen, Ranveig (2020). Vaksinemyte #7: Vaksiner og kreft.
• Braathen, Ranveig & Fossum, Even (2020). En vaksine mot COVID-19.
• Andersen, Tor Kristian; Braathen, Ranveig & Fossum, Even (2020). Vaksinekappløpet – seks vaksiner på oppløpssiden.
• Bjerkan, Louise; Braathen, Ranveig & Gudjonsson, Arnar (2020). Forkjølelsesvirus som vaksine mot covid-19.
• Grødeland, Gunnveig; Fossum, Even & Braathen, Ranveig (2020). Vaksinepodden.no: Covid-19 vaksiner - fra Oxford til Sputnik V.
• Braathen, Ranveig & Anderson, Ane Marie (2019). Flokkimmunitet – et felles ansvar.
• Braathen, Ranveig (2019). Vaksinemyte #6: Kvikksølv i vaksiner.
• Bjerkan, Louise; Gudjonsson, Arnar & Braathen, Ranveig (2019). En malariavaksine med mål og mening!
• Gudjonsson, Arnar; Bjerkan, Louise; Labbe, Genevieve; Draper, Simon; Braathen, Ranveig & Bogen, Bjarne (2019). Targeting PfRH5 to APCs via MHC class II potentiates viral vector immunization against malaria.
• Bjerkan, Louise; Gudjonsson, Arnar; Visweswaran, Ganesh Ram; Genevieve, Labbe; Quinkert, Doris & Draper, Simon [Show all 8 contributors for this article] (2019). APC-targeted DNA vaccination against RH5 induces Plasmodium falciparum-specific neutralizing antibodies and T cell responses.
• Braathen, Ranveig; Spång, Heidi; Hinke, Daniela Maria; Blazevski, Jana & Bogen, Bjarne (2018). Novel heterodimeric DNA vaccine targeting APC protects against MOPC315 myeloma and influenza in BALB/c mice .
• Bjerkan, Louise; Braathen, Ranveig; Gudjonsson, Arnar; Grødeland, Gunnveig; Visweswaran, Ganesh Ram & Bogen, Bjarne (2018). Targeted DNA vaccination induce protective immune responses against malaria .
• Bjerkan, Louise; Braathen, Ranveig; Gudjonsson, Arnar; Grødeland, Gunnveig; Visweswaran, Ganesh Ram & Bogen, Bjarne (2018). An APC-targeted PfRH5 containing DNA vaccine induce protective immune responses against Plasmodium falciparum .
• Hinke, Daniëla Maria; Spång, Heidi; Fossum, Even; Grødeland, Gunnveig; Bogen, Bjarne & Braathen, Ranveig (2018). MHC class II targeted DNA vaccine is most efficient in the induction of protective antibodies against influenza.
• Bjerkan, Louise; Visweswaran, Ganesh Ram; Braathen, Ranveig & Bogen, Bjarne (2016). Novel malaria vaccines by VaccibodyTM DNA immunization. Show summary

  Novel malaria vaccines by VaccibodyTM DNA immunization L Bjerkan1, GR Visweswaran1, R Braathen1, G Labbe 3, SJ Draper3, B Bogen1,2 1K.G. Jebsen Centre for Research on Influenza Vaccines, Oslo 0450, Norway 2Centre for Immune Regulation Institute of Immunology, University of Oslo and Oslo University Hospital, Oslo 0027, Norway 3 The Jenner Institute, University of Oxford, Oxford, United Kingdom DNA vaccines have a multitude of advantages such as ease of construction, mass production, and safety. In this study, we exploit a new strategy for DNA vaccination where transfected cells secrete bivalent fusion proteins, denoted vaccibodies. These molecules target antigen to antigen presenting cells (APCs) resulting in efficient stimulation of B and T cells. Results from this study show that BALB/c mice immunized with vaccibody homodimers bearing the Plasmodium falciparum blood stage antigen reticulocyte binding homolog RH5, induce high antibody titers and exhibit a targeting effect even after viral boost. This DNA vaccination platform will also be tested in larger animals.

• Visweswaran, Ganesh Ram; Bjerkan, Louise; Braathen, Ranveig & Bogen, Bjarne (2016). DEVELOPMENT OF EFFICACIOUS TARGETED DNA VACCINES AGAINST MALARIA. Show summary

  DEVELOPMENT OF EFFICACIOUS TARGETED DNA VACCINES AGAINST MALARIA Ganesh Ram Visweswaran1, Ranveig Braathen1, Louise Bjerkan1, Genevieve Labbe2, Simon J. Draper2 and Bjarne Bogen1 1Institute of Immunology, University of Oslo, Oslo, Norway, 2University of Oxford, Oxford, United Kingdom Objective: To develop novel malaria vaccines (DNA, Protein, and Viral-vectored) that induces long-lasting immune responses and confers protection against malaria. Introduction: Malaria, one of the leading causes of human death (584,000 in 2013) in developing countries, is caused by the protozoan parasite Plasmodium and transmitted by the female anopheles mosquito. To date there are no efficacious malaria vaccines available that would impart protective immune response. In this study, a novel DNA vaccine technology (Vaccibody®) is being used to develop Malaria vaccine using a putative blood-stage antigen P. falciparum Reticulocyte Binding Protein Homologue 5 (PfRH5). Method: Vaccibody is composed of a targeting, dimerization, and an antigenic unit. The first two units are being involved in targeting the MHC-class II molecules on antigen presenting cells and for homodimerization of the vaccibody molecules, respectively. The antigenic unit contains the potential antigen (PfRH5) of interest. Results: All PfRH5 vaccibody proteins were secreted by HEK293E cells and were shown to bind different PfRH5 monoclonal antibodies by ELISA. In vivo experiments revealed that the MHC-class II PfRH5 vaccibodies are better targeted and induced significant antibody titers when compared to the non-targeted and antigen controls. Conclusion: Binding by different PfRH5 monoclonal antibodies confirmed functional PfRH5 vaccibody proteins. The MHC-class II targeted PfRH5 vaccibodies elicited higher immune response in mice than the non-targeted and antigen controls, indicating the targeting potential.

• Braathen, Ranveig; Fredriksen, Agnete; Spång, Heidi Cecilie Larsen; Lindeberg, Mona Mari; Fossum, Even & Bogen, Bjarne (2011). Targeting DNA Vaccines against Influenza, can the Immune Response be Orchestered? Scandinavian Journal of Immunology. ISSN 0300-9475. 73(4), p. 382–383.
• Braathen, Ranveig (2006). Structural Motifs for the Formation of Secretory IgA and Binding of Non-Ig Ligands by the Polymeric Ig Receptor. Universitetet i Oslo. ISSN 82-8072-675-6.

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