title: Group B streptococcus GAPDH is released upon cell lysis, associates with bacterial surface, and induces apoptosis in murine macrophages.
abstract: Glyceraldehyde 3-phosphate dehydrogenases (GAPDH) are cytoplasmic glycolytic enzymes that, despite lacking identifiable secretion signals, have been detected at the surface of several prokaryotic and eukaryotic organisms where they exhibit non-glycolytic functions including adhesion to host components. Group B Streptococcus (GBS) is a human commensal bacterium that has the capacity to cause life-threatening meningitis and septicemia in newborns. Electron microscopy and fluorescence-activated cell sorter (FACS) analysis demonstrated the surface localization of GAPDH in GBS. By addressing the question of GAPDH export to the cell surface of GBS strain NEM316 and isogenic mutant derivatives of our collection, we found that impaired GAPDH presence in the surface and supernatant of GBS was associated with a lower level of bacterial lysis. We also found that following GBS lysis, GAPDH can associate to the surface of many living bacteria. Finally, we provide evidence for a novel function of the secreted GAPDH as an inducer of apoptosis of murine macrophages.
authors.affiliation: Universidade do Porto, ICBAS-Instituto de Ciências Biomédicas de Abel Salazar, Porto, Portugal.
authors.forename: Liliana
authors.initials: L
authors.lastname: Oliveira
authors.forename: Pedro
authors.initials: P
authors.lastname: Madureira
authors.forename: Elva Bonifácio
authors.initials: EB
authors.lastname: Andrade
authors.forename: Abdelouhab
authors.initials: A
authors.lastname: Bouaboud
authors.forename: Eric
authors.initials: E
authors.lastname: Morello
authors.forename: Paula
authors.initials: P
authors.lastname: Ferreira
authors.forename: Claire
authors.initials: C
authors.lastname: Poyart
authors.forename: Patrick
authors.initials: P
authors.lastname: Trieu-Cuot
authors.forename: Shaynoor
authors.initials: S
authors.lastname: Dramsi
mesh_terms: D000818:Animals; D000954:Antigens, Surface / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D017209:Apoptosis / Q000187:drug effects* / Q000502:physiology; D001422:Bacterial Adhesion / Q000502:physiology; D001426:Bacterial Proteins / Q000032:analysis / Q000378:metabolism* / Q000494:pharmacology* / Q000502:physiology; D002457:Cell Extracts / Q000737:chemistry / Q000378:metabolism; D002478:Cells, Cultured; D005260:Female; D010861:Fimbriae, Bacterial / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / Q000032:analysis / Q000378:metabolism* / Q000494:pharmacology* / Q000502:physiology; D008264:Macrophages / Q000187:drug effects* / Q000473:pathology / Q000502:physiology; D051379:Mice; D008810:Mice, Inbred C57BL; D030781:Organisms, Genetically Modified; D011485:Protein Binding; D013289:Streptococcaceae / Q000145:classification / Q000201:enzymology* / Q000254:growth & development; D013290:Streptococcal Infections / Q000276:immunology / Q000378:metabolism / Q000473:pathology; D000095983:Bacterial Lysates
chemical_list: D000954:Antigens, Surface; D001426:Bacterial Proteins; D002457:Cell Extracts; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); C030259:Broncho-Vaxom; D000095983:Bacterial Lysates; C518150:GAPDH protein, Streptococcus agalactiae