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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

A quantitative Streptococcus pyogenes - human protein - protein interaction map reveals localization of opsonizing antibodies. / Happonen, Lotta; Hauri, Simon; Svensson Birkedal, Gabriel; Karlsson, Christofer; de Neergaard, Therese; Khakzad, Hamed; Nordenfelt, Pontus; Wikström, Mats; Wisniewska, Magdalena; Björck, Lars; Malmström, Lars; Malmström, Johan.

In: Nature Communications, Vol. 10, 2727, 2019.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Happonen, L, Hauri, S, Svensson Birkedal, G, Karlsson, C, de Neergaard, T, Khakzad, H, Nordenfelt, P, Wikström, M, Wisniewska, M, Björck, L, Malmström, L & Malmström, J 2019, 'A quantitative Streptococcus pyogenes - human protein - protein interaction map reveals localization of opsonizing antibodies', Nature Communications, vol. 10, 2727. https://doi.org/10.1038/s41467-019-10583-5

APA

Happonen, L., Hauri, S., Svensson Birkedal, G., Karlsson, C., de Neergaard, T., Khakzad, H., Nordenfelt, P., Wikström, M., Wisniewska, M., Björck, L., Malmström, L., & Malmström, J. (2019). A quantitative Streptococcus pyogenes - human protein - protein interaction map reveals localization of opsonizing antibodies. Nature Communications, 10, [2727]. https://doi.org/10.1038/s41467-019-10583-5

Vancouver

Happonen L, Hauri S, Svensson Birkedal G, Karlsson C, de Neergaard T, Khakzad H et al. A quantitative Streptococcus pyogenes - human protein - protein interaction map reveals localization of opsonizing antibodies. Nature Communications. 2019;10. 2727. https://doi.org/10.1038/s41467-019-10583-5

Author

Happonen, Lotta ; Hauri, Simon ; Svensson Birkedal, Gabriel ; Karlsson, Christofer ; de Neergaard, Therese ; Khakzad, Hamed ; Nordenfelt, Pontus ; Wikström, Mats ; Wisniewska, Magdalena ; Björck, Lars ; Malmström, Lars ; Malmström, Johan. / A quantitative Streptococcus pyogenes - human protein - protein interaction map reveals localization of opsonizing antibodies. In: Nature Communications. 2019 ; Vol. 10.

Bibtex

@article{61f98f77b37349b8a53c8426f8403618,
title = "A quantitative Streptococcus pyogenes - human protein - protein interaction map reveals localization of opsonizing antibodies",
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.",
author = "Lotta Happonen and Simon Hauri and {Svensson Birkedal}, Gabriel and Christofer Karlsson and {de Neergaard}, Therese and Hamed Khakzad and Pontus Nordenfelt and Mats Wikstr{\"o}m and Magdalena Wisniewska and Lars Bj{\"o}rck and Lars Malmstr{\"o}m and Johan Malmstr{\"o}m",
year = "2019",
doi = "10.1038/s41467-019-10583-5",
language = "English",
volume = "10",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - A quantitative Streptococcus pyogenes - human protein - protein interaction map reveals localization of opsonizing antibodies

AU - Happonen, Lotta

AU - Hauri, Simon

AU - Svensson Birkedal, Gabriel

AU - Karlsson, Christofer

AU - de Neergaard, Therese

AU - Khakzad, Hamed

AU - Nordenfelt, Pontus

AU - Wikström, Mats

AU - Wisniewska, Magdalena

AU - Björck, Lars

AU - Malmström, Lars

AU - Malmström, Johan

PY - 2019

Y1 - 2019

N2 - 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.

AB - 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.

U2 - 10.1038/s41467-019-10583-5

DO - 10.1038/s41467-019-10583-5

M3 - Journal article

C2 - 31227708

VL - 10

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 2727

ER -

ID: 223130398