Publikationer från Malmö universitet
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  • 1.
    Izadi, Arman
    et al.
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Karami, Yasaman
    Univ Lorraine, CNRS, Inria, LORIA, F-54000 Nancy, France.;Univ Paris Cite, Inst Pasteur, Dept Struct Biol & Chem, Struct Bioinformat Unit,CNRS UMR3528, F-75015 Paris, France..
    Bratanis, Eleni
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Wrighton, Sebastian
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Khakzad, Hamed
    Univ Lorraine, CNRS, Inria, LORIA, F-54000 Nancy, France..
    Nyblom, Maria
    Lund Univ, Dept Biol, Lund, Sweden.;Lund Univ, Lund Prot Prod Platform LP3, Lund, Sweden..
    Olofsson, Berit
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Happonen, Lotta
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Tang, Di
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Sundwall, Martin
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Godzwon, Magdalena
    Lund Univ, Dept Immunotechnol, Lund, Sweden.;Lund Univ, SciLifeLab Drug Discovery & Dev Platform, Lund, Sweden..
    Chao, Yashuan
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Toledo, Alejandro Gomez
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Schmidt, Tobias
    Lund Univ, Fac Med, Dept Clin Sci Lund, Div Pediat, Lund, Sweden..
    Ohlin, Mats
    Lund Univ, Dept Immunotechnol, Lund, Sweden.;Lund Univ, SciLifeLab Drug Discovery & Dev Platform, Lund, Sweden..
    Nilges, Michael
    Univ Paris Cite, Inst Pasteur, Dept Struct Biol & Chem, Struct Bioinformat Unit,CNRS UMR3528, F-75015 Paris, France..
    Malmstrom, Johan
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Bahnan, Wael
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Shannon, Oonagh
    Malmö universitet, Odontologiska fakulteten (OD). Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Malmstrom, Lars
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden..
    Nordenfelt, Pontus
    Lund Univ, Fac Med, Dept Clin Sci Lund, Infect Med, Lund, Sweden.;Lund Univ, Skane Univ Hosp Lund, Dept Lab Med, Clin Microbiol, Lund, Sweden..
    The hinge-engineered IgG1-IgG3 hybrid subclass IgGh47 potently enhances Fc-mediated function of anti-streptococcal and SARS-CoV-2 antibodies2024Ingår i: Nature Communications, E-ISSN 2041-1723, Vol. 15, nr 1, artikel-id 3600Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Streptococcus pyogenes can cause invasive disease with high mortality despite adequate antibiotic treatments. To address this unmet need, we have previously generated an opsonic IgG1 monoclonal antibody, Ab25, targeting the bacterial M protein. Here, we engineer the IgG2-4 subclasses of Ab25. Despite having reduced binding, the IgG3 version promotes stronger phagocytosis of bacteria. Using atomic simulations, we show that IgG3's Fc tail has extensive movement in 3D space due to its extended hinge region, possibly facilitating interactions with immune cells. We replaced the hinge of IgG1 with four different IgG3-hinge segment subclasses, IgGh(xx). Hinge-engineering does not diminish binding as with IgG3 but enhances opsonic function, where a 47 amino acid hinge is comparable to IgG3 in function. IgGh(47) shows improved protection against S. pyogenes in a systemic infection mouse model, suggesting that IgGh(47) has promise as a preclinical therapeutic candidate. Importantly, the enhanced opsonic function of IgGh(47) is generalizable to diverse S. pyogenes strains from clinical isolates. We generated IgGh(47) versions of anti-SARS-CoV-2 mAbs to broaden the biological applicability, and these also exhibit strongly enhanced opsonic function compared to the IgG1 subclass. The improved function of the IgGh(47) subclass in two distant biological systems provides new insights into antibody function.

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  • 2.
    Palm, Frida
    et al.
    Lund Univ, Dept Clin Sci, Div Infect Med, Lund, Sweden..
    Broman, Axel
    Lund Univ, Dept Biomed Engn, Lund, Sweden..
    Marcoux, Genevieve
    Lund Univ, Dept Lab Med, Div Hematol & Transfus Med, Lund, Sweden..
    Semple, John W.
    Lund Univ, Dept Lab Med, Div Hematol & Transfus Med, Lund, Sweden.;Off Med Serv, Clin Immunol & Transfus Med, Lund, Sweden.;Univ Toronto, Dept Pharmacol & Toxicol, Toronto, ON, Canada..
    Laurell, Thomas L.
    Lund Univ, Dept Biomed Engn, Lund, Sweden..
    Malmstrom, Johan
    Lund Univ, Dept Clin Sci, Div Infect Med, Lund, Sweden..
    Shannon, Oonagh
    Lund Univ, Dept Clin Sci, Div Infect Med, Lund, Sweden..
    Phenotypic characterization of acoustically enriched extracellular vesicles from pathogen-activated platelets2023Ingår i: Journal of Innate Immunity, ISSN 1662-811X, E-ISSN 1662-8128, Vol. 15, nr 1, s. 599-613Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Extracellular vesicles (EVs) are derived from the membrane of platelets and released in the circulation upon activation or injury. Analogous to the parent cell, platelet derived EVs play an important role in hemostasis and immune responses by transfer of bioactive cargo from the parent cells. Platelet activation and release of EVs increases in several pathological inflammatory diseases, such as sepsis. We have previously reported that the M1 protein released from the bacterial pathogen Streptococcus pyogenes directly mediates platelet activation. In this study, EVs were isolated from these pathogen-activated platelets using acoustic trapping and their inflammation phenotype was characterized using quantitative mass spectrometry-based proteomics and cell-based models of inflammation. We determined that M1 protein mediated release of platelet derived EVs that contained the M1 protein. The isolated EVs derived from pathogen-activated platelets contained a similar protein cargo to those from physiologically activated platelets (thrombin), and included platelet membrane proteins, granule proteins and cytoskeletal proteins, coagulation factors and immune mediators. Immunomodulatory cargo, complement proteins and IgG3, were significantly enriched in EVs isolated from M1 protein-stimulated platelets. Acoustically enriched EVs were functionally intact and exhibited proinflammatory effects on addition to blood, including platelet-neutrophil complex formation, neutrophil activation, and cytokine release. Collectively, our findings reveal novel aspects of pathogen-mediated platelet activation during invasive streptococcal infection.

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