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A quantitative Streptococcus pyogenes–human protein–protein interaction map reveals localization of opsonizing antibodies

Author

Listed:
  • Lotta Happonen

    (Lund University)

  • Simon Hauri

    (Lund University)

  • Gabriel Svensson Birkedal

    (Lund University
    Cantargia AB)

  • Christofer Karlsson

    (Lund University)

  • Therese Neergaard

    (Lund University)

  • Hamed Khakzad

    (University of Zurich
    University of Zurich
    Swiss Institute of Bioinformatics)

  • Pontus Nordenfelt

    (Lund University)

  • Mats Wikström

    (University of Copenhagen
    Attributes Sciences)

  • Magdalena Wisniewska

    (University of Copenhagen)

  • Lars Björck

    (Lund University)

  • Lars Malmström

    (Lund University
    University of Zurich
    University of Zurich
    Swiss Institute of Bioinformatics)

  • Johan Malmström

    (Lund University)

Abstract

A fundamental challenge in medical microbiology is to characterize the dynamic protein–protein interaction networks formed at the host–pathogen interface. Here, we generate a quantitative interaction map between the significant human pathogen, Streptococcus pyogenes, and proteins from human saliva and plasma obtained via complementary affinity-purification and bacterial-surface centered enrichment strategies and quantitative mass spectrometry. Perturbation of the network using immunoglobulin protease cleavage, mixtures of different concentrations of saliva and plasma, and different S. pyogenes serotypes and their isogenic mutants, reveals how changing microenvironments alter the interconnectivity of the interaction map. The importance of host immunoglobulins for the interaction with human complement proteins is demonstrated and potential protective epitopes of importance for phagocytosis of S. pyogenes cells are localized. The interaction map confirms several previously described protein–protein interactions; however, it also reveals a multitude of additional interactions, with possible implications for host–pathogen interactions involving other bacterial species.

Suggested Citation

  • Lotta Happonen & Simon Hauri & Gabriel Svensson Birkedal & Christofer Karlsson & Therese Neergaard & Hamed Khakzad & Pontus Nordenfelt & Mats Wikström & Magdalena Wisniewska & Lars Björck & Lars Malms, 2019. "A quantitative Streptococcus pyogenes–human protein–protein interaction map reveals localization of opsonizing antibodies," Nature Communications, Nature, vol. 10(1), pages 1-15, December.
  • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10583-5
    DOI: 10.1038/s41467-019-10583-5
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    Cited by:

    1. Qianqiao Liu & Beth M. Stadtmueller, 2023. "SIgA structures bound to Streptococcus pyogenes M4 and human CD89 provide insights into host-pathogen interactions," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Arman Izadi & Yasaman Karami & Eleni Bratanis & Sebastian Wrighton & Hamed Khakzad & Maria Nyblom & Berit Olofsson & Lotta Happonen & Di Tang & Martin Sundwall & Magdalena Godzwon & Yashuan Chao & Ale, 2024. "The hinge-engineered IgG1-IgG3 hybrid subclass IgGh47 potently enhances Fc-mediated function of anti-streptococcal and SARS-CoV-2 antibodies," Nature Communications, Nature, vol. 15(1), pages 1-22, December.
    3. Alejandro Gomez Toledo & Eleni Bratanis & Erika Velásquez & Sounak Chowdhury & Berit Olofsson & James T. Sorrentino & Christofer Karlsson & Nathan E. Lewis & Jeffrey D. Esko & Mattias Collin & Oonagh , 2023. "Pathogen-driven degradation of endogenous and therapeutic antibodies during streptococcal infections," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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