A novel multifunctional peptide oligomer of bacitracin with possiblebioindustrial and therapeutic applications from a Korean food-sourceBacillus strain

Collection with item attached
2017
Item details URL
http://open-repository.kisti.re.kr/cube/handle/open_repository/473848.do
DOI
10.1371/journal.pone.0176971
Title
A novel multifunctional peptide oligomer of bacitracin with possiblebioindustrial and therapeutic applications from a Korean food-sourceBacillus strain
Description
Support was provided by: The National Research Foundation of Korea (NRF)grant funded by the Korean government (MEST) (NRF- 2015R1A2A1A15056120,NRF- 2015R1D1A1A01059483); and Bio-industry Technology DevelopmentProgram, Ministry of Agriculture, Food and Rural Affairs (115073-2).
abstract
Investigating the effects of a multifunctional microbial peptide possessing strong anti-inflammatory activity against pathogenic bacteria. The antimicrobial activity of the purified peptide (CSP32) against various multidrug-resistant as well as anaerobic pathogens was determined. Anti-inflammatory activity was determined by an enzyme-linked immunosorbent assay, western blotting, and RT-PCR in RAW 264.7 macrophages. Molecular weight and structural elucidation were performed by several analytical methods such as mass spectrometry and chemoinformatic analysis. CSP32, purified from newly isolated Bacillus sp. CS32, was active against methicillin-resistant Staphylococcus aureus, vancomycin-resistant S. aureus, vancomycin-resistant enterococci, and anaerobic pathogens Propionibacterium acne and Clostridium difficile. Furthermore, CSP32 showed strong inhibitory effects on lipopolysaccharide (LPS)-induced nitric oxide (NO) production and nitric oxide synthase (iNOS) and cyclooxygenase 2 (COX-2) expression in RAW 264.7 macrophages. At concentrations of 10, 50, and 100 mu g/mL, CSP32 treatment attenuated LPS-induced expression of nuclear factor kappa B (NF-kappa B)and mitogen-activated protein kinases (MAPKs) as well as other proinflammatory mediators such as tumor necrosis factor alpha (TNF-alpha), interleukin 6 (IL6), and IL-1 beta. CSP32 potently inhibited translocation of NF-kappa B into the nucleus by suppressing degradation of I.B kinase (I kappa Ba) and its phosphorylation, thereby causing NF-.B to remain inactive. CSP32 may be the first oligomer of bacitracin with anti-inflammatory properties.
Conclusion
CSP32 has stable characteristics and may find bio-industrial and therapeutic applications.
provenance
Made available in Cube on 2018-09-28T10:30:28Z (GMT). No. of bitstreams: 0
language
English
author
Choi, Yun Hee
Cho, Seung Sik
Simkhada, Jaya Ram
Rahman, Md. Saifur
Choi, Yoon Seok
Kim, Chun Sung
Yoo, Jin Cheol
accessioned
2018-09-28T10:30:28Z
available
2018-09-28T10:30:28Z
issued
2017
citation
PLOS ONE(12): 5
issn
1932-6203
uri
http://open-repository.kisti.re.kr/cube/handle/open_repository/473848.do
Funder
미래창조과학부
Funding Program
중견연구자지원
Project ID
1711031645
Jurisdiction
Rep.of Korea
Project Name
Development of next generation peptide antibiotics for mulidrug resistant bacteria control
rights
openAccess
type
article


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