In silico analysis of essential and non-homologous proteins in Salmonella typhimurium biofilm

• Published in: Journal of physics. Conference series Vol. 1349; no. 1; pp. 12133 - 12138
• Main Authors: Othman, N A, Yahya, M F Z R
• Format: Journal Article
• Language: English
• Published: Bristol IOP Publishing 01.11.2019
• Subjects: Antibiotics; Biofilms; Bioinformatics; Homology; Physics; Protein synthesis; Proteins; Salmonella
• ISSN: 1742-6588; 1742-6596
• DOI: 10.1088/1742-6596/1349/1/012133

Salmonella typhimurium is a Gram negative pathogen that commonly causes severe gastroenteritis. It is resistant to a wide range of antibiotics and is able to form biofilm on both biotic and abiotic surfaces. To date, essential and non-homologous proteins in S. typhimurium biofilm remain not well investigated. Therefore, the present work was performed to analyze essential and non-homologous proteins in S. typhimurium biofilm using a combination of one-dimensional SDS-PAGE, HPLC - ESI - QTOF and bioinformatics. Results demonstrated that seven major protein bands (78.1 kDa, 51.2 kDa, 41.5 kDa, 37.3 kDa, 35.1 kDa, 27.6 kDa, and 25.4 kDa) were present in whole-cell protein extract of S. typhimurium biofilm. A total of 75 proteins were successfully identified from both 25.4 kDa and 51.2 kDa protein bands. Approximately 54.67% of QTOF-identified whole-cell proteins were found to be essential to the survival of S. typhimurium biofilm and were non-homologous to human proteome. Majority of essential and non-homologous S. typhimurium biofilm proteins were associated with transport and protein synthesis. The findings from the present work may be useful for development of novel antibiofilm agent.