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PMID:30227935
| Citation |
Rashmi, M, Meena, H, Meena, C, Kushveer, JS, Busi, S, Murali, A and Sarma, VV (2018) Anti-quorum sensing and antibiofilm potential of Alternaria alternata, a foliar endophyte of Carica papaya, evidenced by QS assays and in-silico analysis. Fungal Biol 122:998-1012 |
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| Abstract |
In the present study, secondary metabolites from an endophytic fungus, Alternaria alternata, colonizing Carica papaya, demonstrated antiquorum sensing properties against Pseudomonas aeruginosa. This study reports the antagonistic effects of fungal crude extract of A. alternata against the various quorum sensing (QS) associated virulent factors such as percentage decrease in production of pyocyanin, alginate, chitinase and rhamnolipid; significant decrease in proteases activity such as LasA protease activity, staphylolytic activity, Las B elastase; and a marked decrease in biofilm formation and associated factors such as exopolysaccharide (EPS) production and cell surface hydrophobicity (CSH). Further, motility pattern i.e., swimming and swarming was also found to be inhibited. This down regulation of QS and associated factors are further supported by in-silico analysis of interaction between QS receptor LasR and bioactive molecules viz., sulfurous acid, 2-propyl tridecyl ester and 1,2-benzenedicarboxylic acid, bis(2-methylpropyl) ester present in fungal crude extract, found based on GCMS analysis, sketches the modulating ability of QS expression. This is the first report on an endophytic fungus of C. papaya having a role in QS inhibition against P. aeruginosa and lays a platform to explore further the endophytes for potent therapeutic agents in QS. |
| Links |
PubMed Online version:10.1016/j.funbio.2018.07.003 |
| Keywords |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004175: endopeptidase activity |
ECO:0000314: |
F |
The fifth group of columns in Fig. 4A (labeled lasB elastase activity) shows that the elastase activity of P. aeruginosa lasB (identified in Uniprot as elastase) is inhibited by the introduction of A. alternata extract. |
complete | ||||
| GO:0004175: peptidase inhibitor activity |
ECO:0000314: |
F |
The third group of columns in Fig. 4A (labeled lasA protease) Shows that the protease (peptidase) activity of P. aeruginosa lasA is inhibited by the introduction of A. alternata extract. |
complete | ||||
| GO:0009253: peptidoglycan catabolic process |
ECO:0000314: |
P |
The fourth group of columns in Fig. 4A (labeled lasA staphylolytic activity) Shows that the peptidoglycan degradation (staphylolytic) activity of P. aeruginosa lasA is inhibited by the introduction of A. alternata extract. |
complete | ||||
| GO:0061785: peptidoglycan endopeptidase activity |
ECO:0000314: |
F |
The fourth group of columns in Fig. 4A (labeled lasA staphylolytic activity) Shows that the peptidoglycan degradation (staphylolytic) activity of P. aeruginosa lasA is inhibited by the introduction of A. alternata extract. |
complete | ||||
Notes
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References
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