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Proteomic analysis of the mechanism of recombinant actifensin and defensin-d2 against multidrug-resistant Pseudomonas aeruginosa and Candida albicans

ABSTRACT: In this study, we evaluated the protein expression changes in multidrug-resistant P. aeruginosa and C. albicans treated with recombinant defensin-d2 and actifensin from spinach and Actinomyces ruminicola, respectively, for 1 h. The proteome changes in the test organisms were analyzed by LC-MS/MS ESI using label-free data-dependent acquisition (DDA) quantitative proteomics technique. A total of 28 and 9 differentially expressed proteins (DEPs) were identified in the treated P. aeruginosa and C. albicans, respectively, with a 2-fold change threshold and p-value < 0.05. The GO and KEGG enrichment analysis found that DEPs related to binding, catalytic activity, cellular component organization and biogenesis, structural molecule activity and response to stimulus were significantly expressed in actifensin and defensin-treated P. aeruginosa, and the DEPs were mainly involved in DNA replication and repair, translation, membrane transport, energy metabolism, environmental adaptation, and signal transduction. DEPs in actifensin and defensin-treated C. albicans were related to cell growth and death, translation, lipid metabolism and energy metabolism were significantly expressed, and these DEPs mainly involved oxidative phosphorylation, RNA degradation, carbohydrate metabolism, and cell cycle pathways. We also established evidently through the different pathways affected, that the recombinant peptides exerted multiple mechanisms of action against the test organisms, sequentially or simultaneously.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Candida Albicans (yeast)

TISSUE(S): Cell Culture

SUBMITTER: Ifeoluwa Gbala

LAB HEAD: IFEOLUWA DEBORAH GBALA

PROVIDER: PXD034169 | Pride | 2022-09-17

REPOSITORIES: pride

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Project description:The interaction of clinically relevant microorganisms is the focus of various studies, e.g. the interaction between the pathogenic yeast, Candida albicans, and the bacterium, Pseudomonas aeruginosa and these interactions can alter the outcome of infection, growth dynamics of each species and antimicrobial resistance of pathogens. During infection, both C. albicans and P. aeruginosa can elicit the release arachidonic acid (AA) from host cells membranes through the action of phospholipases. This polyunsaturated fatty acid can be transformed into immune-modulating compounds, termed eicosanoids, by both host-derived and microbial-derived enzymatic reactions. In its free form, AA can affect the growth of both C. albicans and P. aeruginosa, inhibiting the morphogenesis of C. albicans as well as reducing resistance towards antifungal agents. However, the mechanism of this is unknown. Previous studies on the effect of polyunsaturated fatty acids have indicated a possible alteration in plasma membrane organisation and permeability. Our group aimed to address how AA affects C. albicans in both single species biofilms, as well as in polymicrobial biofilms with P. aeruginosa. RNAseq was performed on single and polymicrobial biofilms in the presence and absence of a sub-inhibitory (100 µM) concentration of AA. Differential expression was determined between C. albicans single species biofilms in the presence and absence of AA. Secondly, the influence of co-incubation of C. albicans with P. aeruginosa in the absence of AA was evaluated to identify novel facets of interaction not previously identified, and to establish a baseline to determine the effect of AA on C. albicans in polymicrobial biofilms. Lastly, the effect of AA on C. albicans in polymicrobial biofilms was determined through comparison with polymicrobial biofilms in the absence of AA. This study provides a comprehensive analysis of the effect of AA and both co-incubation of C. albicans with P. aeruginosa focused on the transcriptome.

			Action	DRS
	22P05630001.mgf	Mgf
	22P05630001.msf	Msf
	22P05630001.raw	Raw
	22P05630002.mgf	Mgf
	22P05630002.msf	Msf

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Proteomic analysis of the mechanism of recombinant actifensin and defensin-d2 against multidrug-resistant Pseudomonas aeruginosa and Candida albicans

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