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  • 1. Cano, F.
    et al.
    Plotnicky-Gilquin, H.
    Nguyen, T. N.
    Liljeqvist, S.
    Samuelson, Patrik
    KTH, Tidigare Institutioner                               , Bioteknologi.
    Bonnefoy, J. Y.
    Ståhl, Stefan
    KTH, Tidigare Institutioner                               , Bioteknologi.
    Robert, A.
    Partial protection to respiratory syncytial virus (RSV) elicited in mice by intranasal immunization using live staphylococci with surface-displayed RSV-peptides2000Inngår i: Vaccine, ISSN 0264-410X, E-ISSN 1873-2518, Vol. 18, nr 24, s. 2743-2752Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    A live bacterial vaccine-delivery system based on the food-grade bacterium Staphylococcus carnosus was used for delivery of peptides from the G glycoprotein of human respiratory syncytial virus, subtype A (RSV-A). Three peptides, corresponding to the G protein amino acids, 144-159 (denoted G5), 190-203 (G9) and 171-188 (G4 S), the latter with four cysteine residues substituted for serines, were expressed by recombinant means as surface-exposed on three different bacteria, and their surface accessibility on the bacteria was verified by fluorescence-activated cell sorting (FACS). Intranasal immunization of mice with the live recombinant staphylococci elicited significant anti-peptide as well as anti-virus serum IgG responses of balanced IgG1/IgG2a isotype profiles, and upon viral challenge with 10(5) tissue culture infectious doses(50) (TCID50), lung protection was demonstrated for approximately half of the mice in the G9 and G4 S immunization groups. To our knowledge, this is the first study in which protective immunity to a viral pathogen has been evoked using food-grade bacteria as vaccine-delivery vehicles.

  • 2. Goetsch, L.
    et al.
    Plotnicky-Gilquin, H.
    Champion, T.
    Beck, A.
    Corvaia, N.
    Ståhl, Stefan
    KTH, Tidigare Institutioner                               , Bioteknologi.
    Bonnefoy, J. Y.
    Nguyen, T. N.
    Power, U. F.
    Influence of administration dose and route on the immunogenicity and protective efficacy of BBG2Na, a recombinant respiratory syncytial virus subunit vaccine candidate2000Inngår i: Vaccine, ISSN 0264-410X, E-ISSN 1873-2518, Vol. 18, nr 24, s. 2735-2742Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    The immunogenicity and protective efficacy of BBG2Na, a novel recombinant respiratory syncytial virus subunit vaccine candidate, was assessed in BALB/c mice under various conditions of dose, administration route and number of immunisations. A single intra-peritoneal (i.p.) dose of 2 mu g, or two doses of 0.2 mu g, were sufficient to induce elevated RSV-A serum antibodies and sterilising lung protective immunity. Serum antibody titres were significantly boosted following second immunisations, but not a third. Of three routes of immunisation, i.p. induced the highest RSV-A antibody titres, followed in efficacy by the intramuscular (i.m.) and subcutaneous (s.c.) routes. Nonetheless, all three routes induced comparable and sterilising lung protection. In contrast, upper respiratory tract protection was observed only after i.p. vaccination, although significant viral titre reductions were evident following i.m. or s.c. immunisations. Interestingly, Pepscan analyses indicated that antibody epitope usage was highest in i.p. and lowest in i.m. immunised mice, respectively. Nonetheless, all routes resulted in antibody responses to known lung protective epitopes (protectopes). Thus, the prevention of serious lower respiratory tract disease, the principle goal of a RSV vaccine, but not URT infection, is dose dependent but unlikely to be influenced by the route of BBG2Na administration.

  • 3. Pinitkiatisakul, Sunan
    et al.
    Friedman, Mikaela
    Wikman, Maria
    Mattsson, Jens G.
    Lovgren-Bengtsson, Karin
    Ståhl, Stefan
    KTH, Skolan för bioteknologi (BIO), Molekylär Bioteknologi.
    Lunden, Anna
    Immunogenicity and protective effect against murine cerebral neosporosis of recombinant NcSRS2 in different iscom formulations2007Inngår i: Vaccine, ISSN 0264-410X, E-ISSN 1873-2518, Vol. 25, nr 18, s. 3658-3668Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Recombinant NcSRS2, a major immunodominant surface antigen of the intracellular protozoan parasite Neospora caninum, was used as a model antigen to compare the immunogenicity of iscoms prepared according to three different methods. Two NcSRS2 fusion proteins were used, one that was biotinylated upon expression in Escherichia coli and linked to Ni2+-loaded iscom matrix (iscom without any protein) via a hexabistidyl (HiS(6)-tagged streptavidin fusion protein, and another that contained both a HiS(6)-tag and streptavidin (HiS(6)-SA-SRS2') and was coupled to either Ni2+-loaded or biotinylated matrix. While all three iscom preparations induced N. caninum specific antibodies at similar levels, HiS(6)-SA-SRS2' coupled to biotinylated matrix generated the strongest cellular responses measured as in vitro proliferation and production of interferon-gamma and interleukin-4 after antigen stimulation of spleen cells. However, the relationship between the levels of these cytokines as well as between IgG1 and IgG2a titres in serum induced by the three iscom preparations were similar, indicating that the balance between Th1 and Th2 responses did not differ. After challenge infection, mice immunised with His(6)-SA-SRS2' coupled to biotinylated matrix had significantly lower amounts of parasite DNA in their brains compared to the other immunised groups. Possible reasons for the performance of the different iscom formulations are discussed.

  • 4. Qazi, K. R.
    et al.
    Wikman, M.
    Vasconcelos, N. M.
    Berzins, K.
    Ståhl, Stefan
    KTH, Skolan för bioteknologi (BIO), Molekylär Bioteknologi.
    Fernandez, C.
    Enhancement of DNA vaccine potency by linkage of Plasmodium falciparum malarial antigen gene fused with a fragment of HSP70 gene2005Inngår i: Vaccine, ISSN 0264-410X, E-ISSN 1873-2518, Vol. 23, nr 9, s. 1114-1125Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Finding an appropriate adjuvant for human vaccination is crucial. HSPs have been shown to act as adjuvants when coadministered with peptide antigens or given as fusion proteins. However, there is a potential risk of autoimmunity when using the complete molecules because HSPs are evolutionary conserved. To overcome this. we first evaluated the adjuvant effect of a less conserved fragment of Plasmodium falciparum HSP70 (Pf70C) as compared it to that of the whole HSP70 molecule from Trypanosoma cruzi (TcHSP70). We found that Pf70C exhibited similar adjuvant properties as the whole molecule. We then evaluated the adjuvant potential of Pf70C for the malarial antigen EB200 in a chimeric DNA construct. No appreciable levels of EB200 specific antibodies were detected in mice immunized with the DNA constructs only. However, the DNA immunization efficiently primed the immune system, as indicated by the strong Th-1 antibody response elicited by a subsequent boosting with the corresponding recombinant fusion proteins. In contrast, while no such priming effect was observed for ex vivo IFN-gamma production, stimulation with the HSP chimeric fusion protein induced an enhanced secretion of IFN-gamma in vitro as compared to other proteins used. Our results emphasize the potential of HSPs as adjuvants in subunit vaccines.

  • 5.
    Wikman, Maria
    et al.
    KTH, Skolan för bioteknologi (BIO).
    Friedman, Mikaela
    KTH, Skolan för bioteknologi (BIO), Molekylär Bioteknologi.
    Pinitkiatisakul, S.
    Andersson, Christin
    KTH, Skolan för bioteknologi (BIO).
    Hemphill, A.
    Lovgren-Bengtsson, K.
    Lunden, A.
    Ståhl, Stefan
    KTH, Skolan för bioteknologi (BIO), Molekylär Bioteknologi.
    General strategies for efficient adjuvant incorporation of recombinant subunit immunogens2005Inngår i: Vaccine, ISSN 0264-410X, E-ISSN 1873-2518, Vol. 23, nr 17-18, s. 2331-2335Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    We have previously reported strategies for Escherichia coli production of recombinant immunogens fused to hydrophobic peptides or lipid tags to improve their capacity to be incorporated into an adjuvant formulation, e.g., immunostimulating complexes (iscoms). Recently, we also explored the strong interaction between biotin and streptavidin to achieve iscom association of recombinant immunogens. Plasmodium falciparum, Toxoplasma gondii and Neospora caninum antigens have served as model immunogens in the different studies. Generated fusion proteins have been found to be successfully incorporated into iscoms and high-titer antigen-specific antibody responses have been obtained upon immunization of mice. We believe that the different concepts presented, utilizing either hydrophobic peptide or lipid tags, or the recently explored biotin-streptavidin principle, offer convenient methods to achieve efficient adjuvant incorporation of recombinant immunogens.

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