Inner membrane proteins YgdD and SbmA are required for the complete susceptibility of Escherichia coli to the proline-rich antimicrobial peptide arasin 1(1–25)

Abstract

Inner membrane proteins YgdD and SbmA are required for the complete susceptibility of Escherichia coli to the proline-rich antimicrobial peptide arasin 1(1-25) Arasin 1 from the spider crab Hyas araneus is a proline-rich antimicrobial peptide (PR-AMP), which kills target bacteria by a non-membranolytic mechanism. By using a fluorescent derivative of the peptide, we showed that arasin 1 rapidly penetrates into Escherichia coli cells without membrane damage. To unravel its mode of action, a knockout gene library of E. coli was screened and two types of mutants with a less susceptible phenotype to the arasin 1 fragment (1-23) were found. The first bore the mutation of sbmA, a gene coding for an inner membrane protein involved in the uptake of different antibiotic peptides. The second mutation was located in the ygdD gene, coding for a conserved inner membrane protein of unknown function. Functional studies showed that YgdD is required for the full susceptibility to arasin 1(1-25), possibly by supporting its uptake and/or intracellular action. These results indicated that different bacterial proteins are exploited by arasin 1(1-25) to exert its antibacterial activity and add new insights on the complex mode of action of PR-AMPs.

Unveiling the Multifaceted Mechanisms of Antibacterial Activity of Buforin II and Frenatin 2.3S Peptides from Skin Micro-Organs of the Orinoco Lime Treefrog (Sphaenorhynchus lacteus)

“…We hypothesize that transcription upregulation of 16S and the topoisomerase parE upon bacterial incubation with BF2 can constitute an adaptation response mechanism to the peptide binding to nucleic acids. On the other hand, modulation of the MprF gene, involved in the synthesis of the bacterial wall exposed positively charged LPG has been related to bacterial evasion of cationic peptides action [55,56]. However, the present results suggest that the assayed conditions were not sufficient to induce a significant bacterial response to BF2 and F2.3S exposure.…”

Identification and elucidation of proline‐rich antimicrobial peptides with enhanced potency and delivery

“…The inner membrane protein SbmA is considered as the major transporter for most PrAMPs (Mattiuzzo et al, ). Recently, other inner membrane proteins were found to facilitate transportation as well (Krizsan et al, ; Paulsen et al, ). In particular, the YgdD protein was reported to be essential for the complete susceptibility of E. coli for arasin 1(1–25) (Paulsen et al, ).…”

“…Recently, other inner membrane proteins were found to facilitate transportation as well (Krizsan et al, ; Paulsen et al, ). In particular, the YgdD protein was reported to be essential for the complete susceptibility of E. coli for arasin 1(1–25) (Paulsen et al, ). It is informative to test the role of SbmA and YgdD proteins to the antimicrobial activities for apidaecin‐1b, pyrrhocoricin and Bac7(1–16) derivatives.…”

“…The inner membrane protein MdtM was reported as a transporter protein for some PrAMPs (Krizsan, Knappe, & Hoffmann, ). In addition, YgdD protein was found to be essential for the complete susceptibility of E. coli for arasin 1(1–25) (Paulsen et al, ).…”

Modulation of global transcriptional regulatory networks as a strategy for increasing kanamycin resistance of EF-G mutants

“…S10). The product of this gene is involved in the transport of peptide antibiotics and its deletion results in increase of resistance to antimicrobial peptides (Laviña, Pugsley & Moreno, 1986;Yorgey et al, 1994;Salomón & Farías, 1995;Saier et al, 2009;Corbalan et al, 2013;Runti et al, 2013;Paulsen et al, 2016).…”