Dissecting the properties of circulating IgG against streptococcal pathogens through a combined systems antigenomics-serology workflow
(2025) In Nature Communications 16. p.1-16- Abstract
This study showcases an integrative mass spectrometry-based strategy combining systems antigenomics and systems serology to characterize human antibodies in clinical samples. This strategy involves using antibodies circulating in plasma to affinity-enrich antigenic proteins in biochemically fractionated pools of bacterial proteins, followed by their identification and quantification using mass spectrometry. A selected subset of the identified antigens is then expressed recombinantly to isolate antigen-specific IgG, followed by characterization of the structural and functional properties of these antibodies. We focused on Group A streptococcus (GAS), a major human pathogen lacking an approved vaccine. The data shows that both healthy and... (More)
This study showcases an integrative mass spectrometry-based strategy combining systems antigenomics and systems serology to characterize human antibodies in clinical samples. This strategy involves using antibodies circulating in plasma to affinity-enrich antigenic proteins in biochemically fractionated pools of bacterial proteins, followed by their identification and quantification using mass spectrometry. A selected subset of the identified antigens is then expressed recombinantly to isolate antigen-specific IgG, followed by characterization of the structural and functional properties of these antibodies. We focused on Group A streptococcus (GAS), a major human pathogen lacking an approved vaccine. The data shows that both healthy and GAS-infected individuals have circulating IgG against conserved streptococcal proteins, including toxins and virulence factors. The antigenic breadth of these antibodies remains relatively constant across healthy individuals but changes considerably in GAS bacteremia. Moreover, antigen-specific IgG analysis reveals individual variation in titers, subclass distributions, and Fc-signaling capacity, despite similar epitope and Fc-glycosylation patterns. Finally, we show that GAS antibodies may cross-react with Streptococcus dysgalactiae (SD), a bacterial pathogen that occupies similar niches and causes comparable infections. Collectively, our results highlight the complexity of GAS-specific antibody responses and the versatility of our methodology to characterize immune responses to bacterial pathogens.
(Less)
- author
- organization
-
- Infection Medicine Proteomics (research group)
- Infection Medicine (BMC)
- Translational infection medicine (research group)
- BioMS (research group)
- Quantitative immunobiology (research group)
- epIgG (research group)
- LU Profile Area: Light and Materials
- LTH Profile Area: Nanoscience and Semiconductor Technology
- NanoLund: Centre for Nanoscience
- LTH Profile Area: Photon Science and Technology
- SEBRA Sepsis and Bacterial Resistance Alliance (research group)
- LTH Profile Area: Engineering Health
- publishing date
- 2025-02-24
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Humans, Immunoglobulin G/blood, Streptococcal Infections/immunology, Antigens, Bacterial/immunology, Streptococcus pyogenes/immunology, Antibodies, Bacterial/immunology, Bacterial Proteins/immunology, Cross Reactions/immunology, Streptococcus/immunology, Female, Workflow, Adult, Male, Mass Spectrometry
- in
- Nature Communications
- volume
- 16
- article number
- 1942
- pages
- 1 - 16
- publisher
- Nature Publishing Group
- external identifiers
-
- pmid:39994218
- scopus:85218502847
- ISSN
- 2041-1723
- DOI
- 10.1038/s41467-025-57170-5
- language
- English
- LU publication?
- yes
- additional info
- © 2025. The Author(s).
- id
- 33e1c92e-69a5-44a4-b306-30b03dac2ef9
- date added to LUP
- 2025-02-27 04:38:17
- date last changed
- 2025-07-14 14:40:40
@article{33e1c92e-69a5-44a4-b306-30b03dac2ef9, abstract = {{<p>This study showcases an integrative mass spectrometry-based strategy combining systems antigenomics and systems serology to characterize human antibodies in clinical samples. This strategy involves using antibodies circulating in plasma to affinity-enrich antigenic proteins in biochemically fractionated pools of bacterial proteins, followed by their identification and quantification using mass spectrometry. A selected subset of the identified antigens is then expressed recombinantly to isolate antigen-specific IgG, followed by characterization of the structural and functional properties of these antibodies. We focused on Group A streptococcus (GAS), a major human pathogen lacking an approved vaccine. The data shows that both healthy and GAS-infected individuals have circulating IgG against conserved streptococcal proteins, including toxins and virulence factors. The antigenic breadth of these antibodies remains relatively constant across healthy individuals but changes considerably in GAS bacteremia. Moreover, antigen-specific IgG analysis reveals individual variation in titers, subclass distributions, and Fc-signaling capacity, despite similar epitope and Fc-glycosylation patterns. Finally, we show that GAS antibodies may cross-react with Streptococcus dysgalactiae (SD), a bacterial pathogen that occupies similar niches and causes comparable infections. Collectively, our results highlight the complexity of GAS-specific antibody responses and the versatility of our methodology to characterize immune responses to bacterial pathogens.</p>}}, author = {{Gomez Toledo, Alejandro and Chowdhury, Sounak and Hjortswang, Elisabeth and Sorrentino, James T and Lewis, Nathan E and Bläckberg, Anna and Ekström, Simon and Kjellström, Sven and Izadi, Arman and Olofsson, Berit and Nordenfelt, Pontus and Malmström, Lars and Rasmussen, Magnus and Malmström, Johan}}, issn = {{2041-1723}}, keywords = {{Humans; Immunoglobulin G/blood; Streptococcal Infections/immunology; Antigens, Bacterial/immunology; Streptococcus pyogenes/immunology; Antibodies, Bacterial/immunology; Bacterial Proteins/immunology; Cross Reactions/immunology; Streptococcus/immunology; Female; Workflow; Adult; Male; Mass Spectrometry}}, language = {{eng}}, month = {{02}}, pages = {{1--16}}, publisher = {{Nature Publishing Group}}, series = {{Nature Communications}}, title = {{Dissecting the properties of circulating IgG against streptococcal pathogens through a combined systems antigenomics-serology workflow}}, url = {{http://dx.doi.org/10.1038/s41467-025-57170-5}}, doi = {{10.1038/s41467-025-57170-5}}, volume = {{16}}, year = {{2025}}, }