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@ARTICLE{Day:605249,
      author       = {Day, Christopher J. and Favuzza, Paola and Bielfeld,
                      Sabrina and Haselhorst, Thomas and Seefeldt, Leonie and
                      Hauser, Julia and Shewell, Lucy K. and Flueck, Christian and
                      Poole, Jessica and Jen, Freda E.-C. and Schäfer, Anja and
                      Dangy, Jean-Pierre and Gilberger, Tim-W. and França, Camila
                      Tenorio and Duraisingh, Manoj T. and Tamborrini, Marco and
                      Brancucci, Nicolas M. B. and Grüring, Christof and
                      Filarsky, Michael and Jennings, Michael P. and Pluschke,
                      Gerd},
      title        = {{T}he essential malaria protein {P}f{C}y{RPA} targets
                      glycans to invade erythrocytes},
      journal      = {Cell reports},
      volume       = {43},
      number       = {4},
      issn         = {2211-1247},
      address      = {[New York, NY]},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2024-01367},
      pages        = {114012},
      year         = {2024},
      abstract     = {Plasmodium falciparum is a human-adapted apicomplexan
                      parasite that causes the most dangerous form of malaria. P.
                      falciparum cysteine-rich protective antigen (PfCyRPA) is an
                      invasion complex protein essential for erythrocyte invasion.
                      The precise role of PfCyRPA in this process has not been
                      resolved. Here, we show that PfCyRPA is a lectin targeting
                      glycans terminating with α2-6-linked N-acetylneuraminic
                      acid (Neu5Ac). PfCyRPA has a >50-fold binding preference for
                      human, α2-6-linked Neu5Ac over non-human, α2-6-linked
                      N-glycolylneuraminic acid. PfCyRPA lectin sites were
                      predicted by molecular modeling and validated by mutagenesis
                      studies. Transgenic parasite lines expressing endogenous
                      PfCyRPA with single amino acid exchange mutants indicated
                      that the lectin activity of PfCyRPA has an important role in
                      parasite invasion. Blocking PfCyRPA lectin activity with
                      small molecules or with lectin-site-specific monoclonal
                      antibodies can inhibit blood-stage parasite multiplication.
                      Therefore, targeting PfCyRPA lectin activity with drugs,
                      immunotherapy, or a vaccine-primed immune response is a
                      promising strategy to prevent and treat malaria.},
      cin          = {CSSB-BNITM-TG / CSSB-UHH-MF},
      ddc          = {610},
      cid          = {I:(DE-H253)CSSB-BNITM-TG-20210520 /
                      I:(DE-H253)CSSB-UHH-MF-20210701},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38573856},
      UT           = {WOS:001226320900001},
      doi          = {10.1016/j.celrep.2024.114012},
      url          = {https://bib-pubdb1.desy.de/record/605249},
}