Proteomic profiling of clinical and environmental strains of Pseudomonas aeruginosa

• Published in: Molecular biology reports Vol. 48; no. 3; pp. 2325 - 2333
• Main Authors: Liew, Siew Mun, Puthucheary, Savithiri D., Rajasekaram, Ganeswrei, Chai, Hwa Chia, Chua, Kek Heng
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.03.2021; Springer Nature B.V
• Subjects: Animal Anatomy; Animal Biochemistry; Biomedical and Life Sciences; Chitin; Cluster Analysis; Disease transmission; Drug Resistance, Multiple, Bacterial; Environmental Microbiology; Gel electrophoresis; Gene Expression Regulation, Bacterial; Histology; Kinases; Life Sciences; Liquid chromatography; Mass Spectrometry; Mass spectroscopy; Morphology; Multidrug resistance; Original Article; Ornithine; Physiology; Principal Component Analysis; Protein kinase; Protein transport; Proteins; Proteomics; Pseudomonas aeruginosa; Pseudomonas aeruginosa - genetics; Pseudomonas aeruginosa - metabolism; Virulence; Clinical; Proteomic profiling; Environmental; Pseudomonas aeruginosa
• ISSN: 0301-4851; 1573-4978
• DOI: 10.1007/s11033-021-06262-8

Pseudomonas aeruginosa is a ubiquitous bacterium, which is able to change its physiological characteristics in response to different habitats. Environmental strains are presumably less pathogenic than clinical strains and whether or not the clinical strains originate from the environment or through inter-host transmission remains poorly understood. To minimize the risk of infection, a better understanding of proteomic profiling of P. aeruginosa is necessary for elucidating the correlation between environmental and clinical strains. Based on antimicrobial susceptibility and patterns of virulence, we selected 12 clinical and environmental strains: (i) environmental, (ii) multidrug resistant (MDR) clinical and (iii) susceptible clinical strains. Whole-cell protein was extracted from each strain and subjected to two-dimensional differential gel electrophoresis (2-D DIGE) and liquid chromatography tandem mass spectrometry quadrupole time-of-flight (LC-MS QTOF). All 12 strains were clustered into 3 distinct groups based on their variance in protein expression. A total of 526 matched spots were detected and four differentially expressed protein spots (p < 0.05) were identified and all differential spots were downregulated in MDR strain J3. Upregulation of chitin binding and BON domain proteins was present in the environmental and some MDR strains, whereas the clinical strains exhibited distinct proteomic profiles with increased expression of serine protein kinase and arginine/ornithine transport ATP-binding proteins. Significant difference in expression was observed between susceptible clinical and MDR strains, as well as susceptible clinical and environmental strains. Transition from an environmental saprophyte to a clinical strain could alter its physiological characteristics to further increase its adaptation.