In vitro genomic and proteomic evidence of a type IV pili-like structure in the fish pathogen Piscirickettsia salmonis

Piscirickettsia salmonis is an intracellular γ-proteobacteria and the etiological agent of piscirickettsiosis, which causes massive economic losses in the Chilean salmon industry. The type IV pili (T4P) play an important role in adherence to host cell surfaces and bacterial pathogenicity. T4P contai...

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Bibliographic Details
Published in:FEMS microbiology letters 2018-08, Vol.365 (16), p.1
Main Authors: Sánchez, Patricio, Oliver, Cristian, Hernández, Mauricio, Cortés, Marcos, Cecilia Rauch, María, Valenzuela, Karla, Garduño, Rafael A, Avendaño-Herrera, Rubén, Yáñez, Alejandro J
Format: Article
Language:English
Subjects:
Amino acid sequence
Amino acids
Animals
Bacteria
Bacterial infections
Bioinformatics
Biosynthesis
Causes of
Conserved sequence
Diseases
Drug resistance
Economic impact
Etiology
Fishes
Gene expression
Genes
Genetic aspects
Genomes
Health aspects
Infections
Laboratories
Microbiology
Pathogenicity
Pathogens
PilA protein
Pili
Piscirickettsia salmonis
Proteins
Proteobacteria
Proteomes
Proteomics
Salmon
Sequence analysis
Transcription
Virulence
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Summary:Piscirickettsia salmonis is an intracellular γ-proteobacteria and the etiological agent of piscirickettsiosis, which causes massive economic losses in the Chilean salmon industry. The type IV pili (T4P) play an important role in adherence to host cell surfaces and bacterial pathogenicity. T4P contains a variable number of components, as predicted in P. salmonis genomes. However, no studies have determined if P. salmonis possesses T4P. The aims of this investigation were to identify T4P components in the P. salmonis type strain LF-89T, evaluate respective transcript expressions, and analyze the main putative T4P proteins using bioinformatics and proteomic approaches. Two main clusters of P. salmonis T4P genes were found. Expression of the pilA gene was upregulated at 4 h post-infection (hpi), while pilQ was upregulated 4 days post-infection. At 16 hpi, pilB and pilD were strongly upregulated. The PilA amino acid sequence analysis showed a conserved N-terminal domain and sequence motifs critical for T4P biosynthesis. MudPIT analysis revealed PilA in the P. salmonis LF-89T proteome, and TEM showed pili-like filamentous structures on the P. salmonis surface. These results strongly suggest the presence of a T4P-like structure in P. salmonis.
ISSN:1574-6968
0378-1097
1574-6968
DOI:10.1093/femsle/fny169