{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T18:42:04Z","timestamp":1785436924957,"version":"3.56.0"},"reference-count":18,"publisher":"American Society for Microbiology","issue":"10","license":[{"start":{"date-parts":[[2025,10,7]],"date-time":"2025-10-07T00:00:00Z","timestamp":1759795200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2025,10,7]],"date-time":"2025-10-07T00:00:00Z","timestamp":1759795200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"name":"The Hunan Provincial Key Laboratory of Anti-ResistanceMicrobial Drugs, the Third Hospital of Changsha","award":["2023TP1013"],"award-info":[{"award-number":["2023TP1013"]}]},{"DOI":"10.13039\/501100004735","name":"Natural Science Foundation of Hunan Province","doi-asserted-by":"crossref","award":["2023JJ30301"],"award-info":[{"award-number":["2023JJ30301"]}],"id":[{"id":"10.13039\/501100004735","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Microbiol Spectr"],"published-print":{"date-parts":[[2025,10,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title\/>\n                    <jats:p>\n                      Multi-drug-resistant\n                      <jats:italic toggle=\"yes\">Aeromonas hydrophila<\/jats:italic>\n                      infections are becoming increasingly threatening, and the development of novel antimicrobial drugs is indispensable. Herein, we demonstrate that this novel peptide is highly active against colistin-resistant\n                      <jats:italic toggle=\"yes\">A. hydrophila<\/jats:italic>\n                      strain and shows sustained killing efficacy\n                      <jats:italic toggle=\"yes\">in vivo<\/jats:italic>\n                      . Mechanistic studies showed that D-Q7 interacted with phosphatidylglycerol and lipopolysaccharide in the bacterial cell membrane, with an increase in intracellular ROS as well as a decrease in ATP level, ultimately leading to cell membrane disruption and bacterial death. Importantly, our study identified gene3832 as a potential regulator of membrane permeability, which may act as a potential modulator of bacterial susceptibility to D-Q7. The role of gene3832 was further confirmed by gene knockout and complementation assays. Consistently, we observed that gene3832 was also involved in biofilm formation in the colistin-resistant\n                      <jats:italic toggle=\"yes\">A. hydrophila<\/jats:italic>\n                      strain. Collectively, our study provides an effective antimicrobial strategy with potential targets for the treatment of drug-resistant\n                      <jats:italic toggle=\"yes\">A. hydrophila<\/jats:italic>\n                      infection.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        As an environmental, zoonotic pathogen,\n                        <jats:italic toggle=\"yes\">Aeromonas hydrophila<\/jats:italic>\n                        remains a major pathogenic bacterium, bringing large economic losses and eco-environmental pressure during the event of large-scale infection. Currently, the occurrence of colistin-resistant\n                        <jats:italic toggle=\"yes\">A. hydrophila<\/jats:italic>\n                        poses a threat to public health owing to the lack of effective prevention and therapeutics. D-Q7 is a D-type antimicrobial peptide (AMP) with potent sterilization activity against gram-negative ESKAPE pathogens; it is thus of considerable interest to evaluate whether D-Q7 represents a promising therapeutic candidate against this pathogen. Consequently, we found that D-Q7 was a potent antibacterial agent that killed colistin-resistant\n                        <jats:italic toggle=\"yes\">A. hydrophila 23-c-23 in vitro<\/jats:italic>\n                        and in a mouse epicutaneous model of\n                        <jats:italic toggle=\"yes\">23-c-23<\/jats:italic>\n                        infection. In addition, we found that\n                        <jats:italic toggle=\"yes\">gene3832<\/jats:italic>\n                        , as a potential transmembrane autotransporter, is related to bacterial resistance to D-Q7. Importantly, our study here will help guide the future design and optimization of novel AMPs to combat colistin-resistant\n                        <jats:italic toggle=\"yes\">A. hydrophila<\/jats:italic>\n                        .\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/spectrum.00590-25","type":"journal-article","created":{"date-parts":[[2025,8,29]],"date-time":"2025-08-29T13:00:32Z","timestamp":1756472432000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":1,"title":["Killing of colistin-resistant\n                    <i>Aeromonas hydrophila<\/i>\n                    by a synthetic 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