{"id":"c4395288-a004-5a8c-858e-d98acdb6821d","stable_key":"c836a883-ac18-5eb2-9971-2f0b542feba8:saureus-redox","predicate":"increases_in_recorded_experiment","statement":"Allicin shifted the bacillithiol redox potential toward a more oxidized state in Staphylococcus aureus.","claim_class":"observational","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"057013ce-7fd5-5922-9d7b-fcd85c28c95c","mechanism_event_label":"Allicin shifted the bacillithiol redox potential toward a more oxidized state in Staphylococcus aureus.","subject":{"id":"85c86fcf-3060-5fae-b567-4f089990ab2d","slug":"allicin","display_name":"Allicin","entity_type_key":"small_molecule"},"object":{"id":"ef3aac9b-a884-5c49-a19d-09c13eb4b071","slug":"saureus-bacillithiol-redox","display_name":"Bacillithiol redox potential in Staphylococcus aureus","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"057013ce-7fd5-5922-9d7b-fcd85c28c95c","stable_key":"c836a883-ac18-5eb2-9971-2f0b542feba8:saureus-redox-event","event_type":"experimental_observation","label":"Allicin shifted the bacillithiol redox potential toward a more oxidized state in Staphylococcus aureus.","description":"**Bacterial thiol systems differ.** Staphylococcus aureus uses bacillithiol rather than treating glutathione as its universal buffer. The 2019 study reported a bacillithiol redox shift, protein S-thioallylation, and reversal through bacilliredoxin/bacillithiol/YpdA chemistry; YpdA could use the allyl-bacillithiol adduct to regenerate bacillithiol. These are organism-specific repair findings, not evidence for the same proteins in humans. [Loi 2019](https://pubmed.ncbi.nlm.nih.gov/31121222/)","status":"provisional","compartment":null,"participants":[{"entity":{"id":"85c86fcf-3060-5fae-b567-4f089990ab2d","slug":"allicin","display_name":"Allicin","entity_type_key":"small_molecule"},"role":"tested factor","stoichiometry":null,"state_label":"Allicin stress","sequence_order":0,"notes":""},{"entity":{"id":"ef3aac9b-a884-5c49-a19d-09c13eb4b071","slug":"saureus-bacillithiol-redox","display_name":"Bacillithiol redox potential in Staphylococcus aureus","entity_type_key":"cellular_process"},"role":"measured outcome","stoichiometry":null,"state_label":"increase","sequence_order":1,"notes":""},{"entity":{"id":"620cbc68-d6a2-5826-bed1-e13bc3dd895e","slug":"bacillithiol","display_name":"Bacillithiol / BSH","entity_type_key":"small_molecule"},"role":"organism-specific low-molecular-weight thiol","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_contrast","value_text":"{\"intervention\": \"Allicin stress\", \"comparator\": \"Matched unstressed bacterial cells\", \"endpoint\": \"Allicin shifted the bacillithiol redox potential toward a more oxidized state in Staphylococcus aureus.\", \"effect_direction\": \"increase\", \"combination\": \"single\", \"conditions\": []}","comparator":null,"unit":null,"notes":"Explicit extracted experimental comparison; source-derived draft.","entity":null},{"dimension":"experimental_model","value_text":"Bacterial redox-biosensor study; primary abstract; exact dose/time unextracted.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"interpretation_status","value_text":"Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Redox potential is not total bacillithiol depletion; no equivalence to human GSH physiology.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Allicin shifted the bacillithiol redox potential toward a more oxidized state in Staphylococcus aureus.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Staphylococcus aureus responds to allicin by global S-thioallylation - Role of the Brx/BSH/YpdA pathway and the disulfide reductase MerA to overcome allicin stress. | 2019 | DOI 10.1016/j.freeradbiomed.2019.05.018 | PMID 31121222 | https://pubmed.ncbi.nlm.nih.gov/31121222/ | https://doi.org/10.1016/j.freeradbiomed.2019.05.018","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"source_locator","value_text":"Reviewed reference lines 51-51; exact primary location described in quoted passage where extracted.","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"f88b620a-4f08-5419-aa45-645cedea988b","evidence_kind":"source_excerpt","locator":"Lines 51-51","start_line":51,"end_line":51,"excerpt":"**Bacterial thiol systems differ.** Staphylococcus aureus uses bacillithiol rather than treating glutathione as its universal buffer. The 2019 study reported a bacillithiol redox shift, protein S-thioallylation, and reversal through bacilliredoxin/bacillithiol/YpdA chemistry; YpdA could use the allyl-bacillithiol adduct to regenerate bacillithiol. These are organism-specific repair findings, not evidence for the same proteins in humans. [Loi 2019](https://pubmed.ncbi.nlm.nih.gov/31121222/)","model_system":"Bacterial redox-biosensor study; primary abstract; exact dose/time unextracted.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Exact excerpt of the retained AI-assisted reviewed reference; primary sources are cited in primary_references and access scope is retained. 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