Subcellular location of Piscirickettsia salmonis heat shock protein 60 (Hsp60) chaperone by using immunogold labeling and proteomic analysis
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Fecha
2020
Profesor/a Guía
Facultad/escuela
Idioma
en
Título de la revista
ISSN de la revista
Título del volumen
Editor
MDPI AG
Nombre de Curso
Licencia CC
Attribution 4.0 International (CC BY 4.0)
Licencia CC
Resumen
Piscirickettsia salmonis is the causative bacterial agent of piscirickettsiosis, a systemic fish disease that significantly impacts the Chilean salmon industry. This bacterium possesses a type IV secretion system (T4SS), several proteins of the type III secretion system (T3SS), and a single heat shock protein 60 (Hsp60/GroEL). It has been suggested that due to its high antigenicity, the P. salmonis Hsp60 could be surface-exposed, translocated across the membrane, and (or) secreted into the extracellular matrix. This study tests the hypothesis that P. salmonis Hsp60 could be located on the bacterial surface. Immunogold electron microscopy and proteomic analyses suggested that although P. salmonis Hsp60 was predominantly associated with the bacterial cell cytoplasm, Hsp60-positive spots also exist on the bacterial cell envelope. IgY antibodies against P. salmonis Hsp60 protected SHK-1 cells against infection. Several bioinformatics approaches were used to assess Hsp60 translocation by the T4SS, T3SS, and T6SS, with negative results. These data support the hypothesis that small amounts of Hsp60 must reach the bacterial cell surface in a manner probably not mediated by currently characterized secretion systems, and that they remain biologically active during P. salmonis infection, possibly mediating adherence and (or) invasion.
Notas
Indexación: Scopus.
Palabras clave
Fish pathology, IgY, Piscirickettsia salmonis, Secretion systems, SRS, Vaccination, Piscirickettsia Salmonis, Francisella, Rickettsia-like Organisms
Citación
Microorganisms, Volume 8, Issue 1, January 2020, Article number 117
DOI
DOI: 10.3390/microorganisms8010117