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In this study, we investigated the inhibitory effects of Sarcotoxin II 50, an insect-derived antimicrobial peptide, on\n                      <jats:italic toggle=\"yes\">K. pneumoniae<\/jats:italic>\n                      . Our findings show that Sarcotoxin II 50 exerts potent antibacterial activity by impairing capsular polysaccharide (CPS) production and fimbrial formation, which compromises bacterial adhesion and colonization capacity.\n                      <jats:italic toggle=\"yes\">In vitro<\/jats:italic>\n                      experiments demonstrated that Sarcotoxin II 50 effectively suppressed the growth of\n                      <jats:italic toggle=\"yes\">cKP<\/jats:italic>\n                      . Mechanistic analyses revealed that the peptide interferes with CPS biosynthesis and alters the structure and expression of type 1 fimbriae (\n                      <jats:italic toggle=\"yes\">fimA<\/jats:italic>\n                      ) and type 3 fimbriae (\n                      <jats:italic toggle=\"yes\">mrkA<\/jats:italic>\n                      ,\n                      <jats:italic toggle=\"yes\">mrkD<\/jats:italic>\n                      ,\n                      <jats:italic toggle=\"yes\">mrkH<\/jats:italic>\n                      ), which are associated with reduced bacterial tissue invasion and attenuated virulence in a murine abscess model. Overall, this study provides a detailed mechanistic understanding of how Sarcotoxin II 50 inhibits\n                      <jats:italic toggle=\"yes\">K. pneumoniae<\/jats:italic>\n                      both\n                      <jats:italic toggle=\"yes\">in vitro<\/jats:italic>\n                      and\n                      <jats:italic toggle=\"yes\">in vivo<\/jats:italic>\n                      under the tested experimental conditions. These results offer a mechanistic basis for the development of novel antimicrobial therapies targeting\n                      <jats:italic toggle=\"yes\">K. pneumoniae<\/jats:italic>\n                      infections and support the further exploration of this peptide as a promising antimicrobial candidate. Characterization of a new insect peptide, Sarcotoxin II 50, with anti-\n                      <jats:italic toggle=\"yes\">K<\/jats:italic>\n                      .\n                      <jats:italic toggle=\"yes\">pneumoniae<\/jats:italic>\n                      activity from the housefly for the first time.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        Sarcotoxin II 50 inhibited\n                        <jats:italic toggle=\"yes\">K. pneumoniae<\/jats:italic>\n                        invasion into A549 and BEAS-2B lung epithelial cells. Sarcotoxin II 50 inhibits\n                        <jats:italic toggle=\"yes\">K. pneumoniae<\/jats:italic>\n                        invasion into epithelial cells by affecting capsular polysaccharide synthesis, fimbriae formation, and cell division. This manuscript investigates, for the first time, the function and mechanism of the Sacrotoxin II family member in combating\n                        <jats:italic toggle=\"yes\">K. pneumoniae<\/jats:italic>\n                        , 40 years after its initial identification.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/spectrum.00962-25","type":"journal-article","created":{"date-parts":[[2026,3,17]],"date-time":"2026-03-17T13:24:38Z","timestamp":1773753878000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["Mechanistic insights into the inhibitory effects of eukaryotically expressed Sarcotoxin II 50 on\n                    <i>Klebsiella pneumoniae<\/i>\n                    invasion into pulmonary epithelial 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