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

• Published in: Journal of Physics: Conference Series
• Main Author: Othman N.A.; Yahya M.F.Z.R.
• Format: Conference paper
• Language: English
• Published: Institute of Physics Publishing 2019
• Online Access: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85077789673&doi=10.1088%2f1742-6596%2f1349%2f1%2f012133&partnerID=40&md5=18b7fb984f06b0c1d9d6198a0a64496e

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. © Published under licence by IOP Publishing Ltd.