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ProteomicsAE-MS to profile SLO-human plasma protein interactome landscape; HDX-MS and XL-MS to study protein interaction and dynamics of PLG-SLO
Group A Streptococcus is known to exploit the human fibrinolysis system, particularly by targeting the plasminogen/plasmin pathway through redundant pathomechanisms. In this study, we began with affinity-enrichment mass spectrometry to map the interaction landscape between streptolysin O and human p...
ORGANISM(S): Homo sapiens (Human) Streptococcus pyogenes MGAS315 
2024-10-17 | PXD051261 | Pride
Ae-ms Human Streptolysin o Streptococcus pyogenes Xl-ms Hdx-ms Plasminogen Lc-ms/ms 
UnknownStreptolysin O accelerates the conversion of plasminogen to plasmin.
Not available
S-EPMC11589678 | biostudies-literature
ProteomicsAffinity-purification mass spectrometry on i) streptolysin O or C5a peptidase with human plasma or saliva; ii) human plasminogen with streptococcal proteins
In this project, we tried to use affinity-purification mass spectrometry (AP-MS) to study host-pathogen protein interaction, focusing initially on two major virulence factors of group A streptococcus (GAS), streptolysin O (SLO) and C5a peptidase (C5AP) with the immediate host microenvironment (human...
ORGANISM(S): Streptococcus pyogenes M1 GAS Homo sapiens (Human) Streptococcus pyogenes MGAS315 
2026-03-16 | PXD069402 | Pride
Group a streptococcus Protein-protein interaction Host-pathogen interaction Ap-ms 
UnknownTargeted amino acid substitutions impair streptolysin O toxicity and group A Streptococcus virulence.
Not available
S-EPMC3546560 | biostudies-literature
UnknownIncreased cytotoxicity and streptolysin O activity in group G streptococcal strains causing invasive tissue infections.
Not available
S-EPMC4658506 | biostudies-literature
TranscriptomicsRegulation of global gene expression in human Loa loa infection is a function of chronicity
Differential gene expression to parasite and nonparasite antigen was seen in infected patients with lifelong exposure to the human filarial parasite Loa loa (endemics) compared with patients who became infected due to temporary residence or travel in an endemic country (expatriates). CD4+ and CD8+ c...
ORGANISM(S): Homo sapiens 
2011-11-24 | E-GEOD-31894 | biostudies-arrayexpress
ProteomicsDe novo sequencing of an unknown monoclonal antibody using BU-MS and elucidation of the neutralizing antibody-Streptolysin O complex via cross-linking and hydrogen-deuterium exchange mass spectrometry
The identification of protective epitopes in bacterial pathogens using mass spectrometry proteomics is essential for advancing vaccine design, especially against the backdrop of increasing antibiotic resistance. Our study introduces an innovative strategy, leveraging multi-modal mass spectrometry te...
ORGANISM(S): Mus musculus (Mouse) Streptococcus pyogenes MGAS315 
2024-05-06 | PXD047461 | Pride
Host-pathogen interaction  antibody-antigen binding  mass spectrometry  structural proteomics 
UnknownAn anti-perfringolysin O monoclonal antibody cross-reactive with streptolysin O protects against streptococcal toxic shock syndrome.
Not available
S-EPMC7487723 | biostudies-literature
UnknownStudy of streptococcal antibody (anti-streptolysin O) among healthy children in Bangladesh.
Not available
S-EPMC9244936 | biostudies-literature
UnknownDual modes of membrane binding direct pore formation by Streptolysin O.
Not available
S-EPMC4692278 | biostudies-literature
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