1. Functional and expression characteristics identification of Phormicins, novel AMPs from Musca domestica with anti-MRSA biofilm activity, in response to different stimuli.
- Author
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Wang, Bing, Wei, Peng-Wei, Yao, Yang, Song, Chao-Rong, Wang, Xu, Yang, Yong-Xin, Long, Yao-Hang, Yang, Su-Wen, Hu, Yong, Gai, Zhong-Chao, Wu, Jian-Wei, and Liu, Hong-Mei
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HOUSEFLY , *CELL membrane formation , *DRUG resistance in bacteria , *BIOFILMS , *ANTIMICROBIAL peptides , *GENTIAN violet , *QUORUM sensing - Abstract
Antibiotic-resistant bacteria (including MRSA) in the clinic pose a growing threat to public health, and antimicrobial peptides (AMPs) have great potential as efficient treatment alternatives. Houseflies have evolved over long periods in complex, dirty environments, developing a special immune system to overcome challenges in harmful environments. AMPs are key innate immune molecules. Herein, two differentially expressed AMPs, Phormicins A and B, were identified by screening transcriptomic changes in response to microbial stimulation. Structural mimic assays indicated that these AMPs exhibited functional divergence due to their C-terminal features. Expression analysis showed that they had different expression patterns. Phormicin B had higher constitutive expression than Phormicin A. However, Phormicin B was sharply downregulated, whereas Phormicin A was highly upregulated, after microbial stimulation. The MIC, MBC and time-growth curves showed the antibacterial spectrum of these peptides. Crystal violet staining and SEM showed that Phormicin D inhibited MRSA biofilm formation. TEM suggested that Phormicin D disrupted the MRSA cell membrane. Furthermore, Phormicin D inhibited biofilm formation by downregulating the expression of biofilm-related genes, including altE and embp. Therefore, housefly Phormicins were functionally characterized as having differential expression patterns and antibacterial & antibiofilm activities. This study provides a new potential peptide for clinical MRSA therapy. [Display omitted] • Characterization of a new AMP member Phormicin B with antibacterial and antibiofilm activity of MRSA from housefly • Phormicin A and Phormicin B with different expression patterns for functional complementary. • Phormicin A and Phormicin B exhibited functional divergence due to their C-terminal structure features. • Phormicin D inhibits biofilm formation by disrupt cell membrane and alter biofilm formation related gene expression [ABSTRACT FROM AUTHOR]
- Published
- 2022
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