Exploring new biological functions of amyloids : bacteria cell agglutination mediated by host protein aggregation
Torrent Burgas, Marc (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Pulido-Gomez, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Nogués Bara, Maria Victòria (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Boix i Borràs, Esther (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)

Fecha:	2012
Resumen:	Antimicrobial proteins and peptides (AMPs) are important effectors of the innate immune system that play a vital role in the prevention of infections. Recent advances have highlighted the similarity between AMPs and amyloid proteins. Using the Eosinophil Cationic Protein as a model, we have rationalized the structure-activity relationships between amyloid aggregation and antimicrobial activity. Our results show how protein aggregation can induce bacteria agglutination and cell death. Using confocal and total internal reflection fluorescence microscopy we have tracked the formation in situ of protein amyloid-like aggregates at the bacteria surface and on membrane models. In both cases, fibrillar aggregates able to bind to amyloid diagnostic dyes were detected. Additionally, a single point mutation (Ile13 to Ala) can suppress the protein amyloid behavior, abolishing the agglutinating activity and impairing the antimicrobial action. The mutant is also defective in triggering both leakage and lipid vesicle aggregation. We conclude that ECP aggregation at the bacterial surface is essential for its cytotoxicity. Hence, we propose here a new prospective biological function for amyloid-like aggregates with potential biological relevance.
Derechos:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.
Lengua:	Anglès
Documento:	Article ; Versió publicada
Materia:	Bacterial pathogens ; Cell membranes ; Sodium phosphate ; Antimicrobials ; Membrane characteristics ; Liposomes ; Bacteria
Publicado en:	PLOS pathogens, Vol. 8, Issue 11 (November 2012) , p. e1003005, ISSN 1553-7374

DOI: 10.1371/journal.ppat.1003005
PMID: 23133388

8 p, 1.8 MB

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