Impact Factor 2021 : 1.514 (@Clarivate Analytics)
5-Year Impact Factor: 2.699 (@Clarivate Analytics)
  • Users Online: 1039
  • Print this page
  • Email this page
ORIGINAL ARTICLE
Year : 2022  |  Volume : 12  |  Issue : 11  |  Page : 483-494

Inhibition mechanisms of secretome proteins from Paenibacillus polymyxa Kp10 and Lactococcus lactis Gh1 against methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus


1 Laboratory of Halal Science Research, Halal Products Research Institute; Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia
2 Laboratory of Halal Science Research, Halal Products Research Institute, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia
3 Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia
4 Department of Science, University of Technology and Applied Sciences, Rustaq 10 P.C. 329, Oman
5 Agro-Biotechnology Institute, Malaysia, National Institutes of Biotechnology Malaysia, 43400 UPM Serdang, Selangor, Malaysia
6 Department of Microbiology, Faculty of Biotechnology and Biomolecular Science, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia
7 Laboratory of Halal Science Research, Halal Products Research Institute; Department of Microbiology, Faculty of Biotechnology and Biomolecular Science, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia

Correspondence Address:
Mohd Nasir Mohd Desa
Laboratory of Halal Science Research, Halal Products Research Institute; Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor
Malaysia
Login to access the Email id

Source of Support: This study was supported by the funds of Ministry of Higher Education, Malaysia and Universiti Putra Malaysia through Fundamental Research Grant Scheme (FRGS/1/2017/SKK11/UPM/01/1) and Putra Grant (GP/2017/9571800), Conflict of Interest: None


DOI: 10.4103/2221-1691.360564

Rights and Permissions

Objective: To determine the inhibition mechanisms of secretome protein extracted from Paenibacillus polymyxa Kp10 (Kp10) and Lactococcus lactis Gh1 (Gh1) against methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococcus (VRE). Methods: The sensitivity and viability of MRSA and VRE treated with secretome proteins of Kp10 and Gh1 were determined using minimal inhibitory concentration, minimum bactericidal concentration, and time-to-kill assays. The morphological changes were observed using scanning electron microscopy and transmission electron microscopy. To elucidate the antimicrobial mechanism of secretome protein of Kp10 and Gh1 against MRSA and VRE, 2D gel proteomic analysis using liquid chromatography-mass spectrometry was run by comparing upregulated and downregulated proteins, and the proton motive force study including the efflux of ATP, pH gradient, and the membrane potential study were conducted. Results: MRSA and VRE were sensitive to Kp10 and Gh1 secretome protein extracts and displayed apparent morphological and internal composition changes. Several proteins associated with cellular component functions were either downregulated or upregulated in treated MRSA and VRE by changing the membrane potential gradient. Conclusions: Kp10 and Gh1 secretome proteins reduce the growth of VRE and MRSA by damaging the cell membrane. Cell division, cell wall biosynthesis, and protein synthesis are involved in the inhibition mechanism.


[FULL TEXT] [PDF]*
Print this article     Email this article
 Next article
 Previous article
 Table of Contents

 Similar in PUBMED
   Search Pubmed for
   Search in Google Scholar for
 Related articles
 Citation Manager
 Access Statistics
 Reader Comments
 Email Alert *
 Add to My List *
 * Requires registration (Free)
 

 Article Access Statistics
    Viewed491    
    Printed4    
    Emailed0    
    PDF Downloaded69    
    Comments [Add]    

Recommend this journal