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Title: Comparative analysis of methicillin-sensitive and resistant Staphylococcus aureus exposed to emodin based on proteomic profiling

Journal Article · · Biochemical and Biophysical Research Communications
 [1];  [2]; ; ;  [1];  [3]
  1. Research Center of Chinese Herbal Resource Science and Engineering, Guangzhou University of Chinese Medicine, Guangzhou 510006 (China)
  2. Sun Yat-sen Memorial Hospital, Sun Yat-sen University, Guangzhou 510120 (China)
  3. Department of Mathematics and Statistics, South Dakota State University, Box 2220, Brookings, SD 57007 (United States)

Highlights: • Emodin is effective against methicillin-sensitive and resistant Staphylococcus aureus strains. • Global proteomic profiling revealed 145 and 122 significant changes in MSSA and MRSA after emodin treatment, respectively. • Profiling interaction network analysis demonstrated emodin potentially targeted MRSA via multiple mechanisms. Emodin has a strong antibacterial activity, including methicillin-resistant Staphylococcus aureus (MRSA). However, the mechanism by which emodin induces growth inhibition against MRSA remains unclear. In this study, the isobaric tags for relative and absolute quantitation (iTRAQ) proteomics approach was used to investigate the modes of action of emodin on a MRSA isolate and methicillin-sensitive S. aureus ATCC29213(MSSA). Proteomic analysis showed that expression levels of 145 and 122 proteins were changed significantly in MRSA and MSSA, respectively, after emodin treatment. Comparative analysis of the functions of differentially expressed proteins between the two strains was performed via bioinformatics tools blast2go and STRING database. Proteins related to pyruvate pathway imbalance induction, protein synthesis inhibition, and DNA synthesis suppression were found in both methicillin-sensitive and resistant strains. Moreover, Interference proteins related to membrane damage mechanism were also observed in MRSA. Our findings indicate that emodin is a potential antibacterial agent targeting MRSA via multiple mechanisms.

OSTI ID:
22897526
Journal Information:
Biochemical and Biophysical Research Communications, Vol. 494, Issue 1-2; Other Information: Copyright (c) 2017 Elsevier Inc. All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
Country of Publication:
United States
Language:
English