A quantitative Streptococcus pyogenes-human protein-protein interaction map reveals localization of opsonizing antibodies
(2019) In Nature Communications 10(1). p.2727-2727- 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... (More)
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.
(Less)
- author
- organization
- publishing date
- 2019-06-21
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Nature Communications
- volume
- 10
- issue
- 1
- pages
- 2727 - 2727
- publisher
- Nature Publishing Group
- external identifiers
-
- pmid:31227708
- scopus:85067619339
- ISSN
- 2041-1723
- DOI
- 10.1038/s41467-019-10583-5
- language
- English
- LU publication?
- yes
- id
- 134b6187-87e6-4e8d-acb6-7ae81e041294
- date added to LUP
- 2019-06-27 01:07:27
- date last changed
- 2024-09-18 04:34:45
@article{134b6187-87e6-4e8d-acb6-7ae81e041294, abstract = {{<p>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.</p>}}, author = {{Happonen, Lotta and Hauri, Simon and Svensson Birkedal, Gabriel and Karlsson, Christofer and de Neergaard, Therese and Khakzad, Hamed and Nordenfelt, Pontus and Wikström, Mats and Wisniewska, Magdalena and Björck, Lars and Malmström, Lars and Malmström, Johan}}, issn = {{2041-1723}}, language = {{eng}}, month = {{06}}, number = {{1}}, pages = {{2727--2727}}, publisher = {{Nature Publishing Group}}, series = {{Nature Communications}}, title = {{A quantitative Streptococcus pyogenes-human protein-protein interaction map reveals localization of opsonizing antibodies}}, url = {{http://dx.doi.org/10.1038/s41467-019-10583-5}}, doi = {{10.1038/s41467-019-10583-5}}, volume = {{10}}, year = {{2019}}, }