The ClpP protease is required for the stress tolerance and biofilm formation in Actinobacillus pleuropneumoniae

In the respiratory tract and lung tissue, a balanced physiological response is essential for Actinobacillus pleuropneumoniae to survive various types of challenges. ClpP, the catalytic core of the Clp proteolytic complex, is involved in various stresses response and regulation of biofilm formation i...

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Bibliographic Details
Published in:PloS one 2013-01, Vol.8 (1), p.e53600
Main Authors: Xie, Fang, Zhang, Yanhe, Li, Gang, Zhou, Long, Liu, Siguo, Wang, Chunlai
Format: Article
Language:English
Subjects:
Actinobacillus pleuropneumoniae
Actinobacillus pleuropneumoniae - enzymology
Actinobacillus pleuropneumoniae - genetics
Actinobacillus pleuropneumoniae - physiology
Actinobacillus pleuropneumoniae - ultrastructure
Adaptation, Physiological - drug effects
Antibiotics
Bacteria
Biofilms
Biofilms - drug effects
Biofilms - growth & development
Bioinformatics
Biology
Biotechnology
Catalysis
Cell morphology
Cell size
Clonal deletion
ClpP gene
ClpP protein
Confocal microscopy
Cytology
Drug resistance
E coli
Electron microscopy
Endopeptidase Clp - deficiency
Endopeptidase Clp - metabolism
Escherichia coli
Gene Deletion
Gene expression
Gene Expression Regulation, Bacterial - drug effects
Gene sequencing
Genomics
High temperature
Hogs
Homologous recombination
Homology
Iron
Iron - metabolism
Iron - pharmacology
Laboratories
Lungs
Medicine
Oxidative stress
Physiological aspects
Plasmids
Polystyrenes
Protease
Proteases
Proteins
Proteolysis
Respiratory tract
Ribonucleic acid
RNA
RNA sequencing
Scanning electron microscopy
Scanning microscopy
Staphylococcus aureus
Strain
Streptococcus mutans
Stress response
Stress, Physiological - drug effects
Stresses
Temperature
Transcription
Veterinary Science
Virulence
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Summary:In the respiratory tract and lung tissue, a balanced physiological response is essential for Actinobacillus pleuropneumoniae to survive various types of challenges. ClpP, the catalytic core of the Clp proteolytic complex, is involved in various stresses response and regulation of biofilm formation in many pathogenic bacteria. To investigate the role of ClpP in the virulence of A. pleuropneumoniae, the clpP gene was deleted by homologous recombination, resulting in the mutant strain S8ΔclpP. The reduced growth of S8ΔclpP mutant at high temperatures and under several other stress conditions suggests that the ClpP protein is required for the stress tolerance of A. pleuropneumoniae. Interestingly, we observed that the S8ΔclpP mutant exhibited an increased ability to take up iron in vitro compared to the wild-type strain. We also found that the cells without ClpP displayed rough and irregular surfaces and increased cell volume relative to the wild-type strain using scanning electron microscopy (SEM). Confocal laser scanning microscopy (CLSM) revealed that the S8ΔclpP mutant showed decreased biofilm formation compared to the wild-type strain. We examined the transcriptional profiles of the wild type S8 and the S8ΔclpP mutant strains of A. pleuropneumoniae using RNA sequencing. Our analysis revealed that the expression of 16 genes was changed by the deletion of the clpP gene. The data presented in this study illustrate the important role of ClpP protease in the stress response, iron acquisition, cell morphology and biofilm formation related to A. pleuropneumoniae and further suggest a putative role of ClpP protease in virulence regulation.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0053600