Abstract
In recent years the antimicrobial peptides (AMPs) have been prospected and designed as new alternatives to conventional antibiotics. Indeed, AMPs have presented great potential toward pathogenic bacterial strains by means of complex mechanisms of action. However, reports have increasingly emerged regarding the mechanisms by which bacteria resist AMP administration. In this context, we performed a comparative proteomic study by using the total bacterial lysate of magainin I-susceptible and –resistant E. coli strains. After nanoUPLC-MSE analyses we identified 742 proteins distributed among the experimental groups, and 25 proteins were differentially expressed in the resistant strains. Among them 10 proteins involved in bacterial resistance, homeostasis, nutrition and protein transport were upregulated, while 15 proteins related to bacterial surface modifications, genetic information and β-lactams binding-protein were downregulated. Moreover, 60 exclusive proteins were identified in the resistant strains, among which biofilm and cell wall formation and multidrug efflux pump proteins could be observed. Thus, differentially from previous studies that could only associate single proteins to AMP bacterial resistance, data here reported show that several metabolic pathways may be related to E. coli resistance to AMPs, revealing the crucial role of multiple “omics” studies in order to elucidate the global molecular mechanisms involved in this resistance.
Highlights
One of the proposed strategies to avoid the bacterial resistance phenomenon includes the usage of antimicrobial peptides (AMPs)
Here we focused on a deep comparative nanoUPLC-MSE analysis by using the total lysate extract from E. coli strains that are susceptible and resistant to the AMP magainin I, evaluating the differential expressed, as well as exclusive proteins in order to shed some light on the global molecular mechanisms involved in this resistance
NanoUPLC-MSE was applied in order to compare the proteomic profile of the total bacterial lysate for all strains, identifying the significant differences between the experimental groups ATCC, magainin I-susceptible and -resistant strains cultured under optimal growth conditions
Summary
One of the proposed strategies to avoid the bacterial resistance phenomenon includes the usage of antimicrobial peptides (AMPs). These well-known multifunctional molecules have been widely prospected from several www.nature.com/scientificreports/. Studies have related that magainin’s amphiphilic α-helical structure can form ion-permeable channels, resulting in membrane depolarization, irreversible cytolysis and leading to cell death[20] ® magainin peptide analogues (e.g. pexiganan , an antibacterial drug) represent a select group of AMPs, with more than 1,158 patents deposited in the US Patent Ful-Text Database Boolean Search server This group of AMPs were evaluated in advanced clinical trials and submitted for the approval of the Food and Drug Administration (FDA), revealing the importance behind bacterial resistance to these cathelicidin members. Here we focused on a deep comparative nanoUPLC-MSE analysis by using the total lysate extract from E. coli strains that are susceptible and resistant to the AMP magainin I, evaluating the differential expressed, as well as exclusive proteins in order to shed some light on the global molecular mechanisms involved in this resistance
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