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However, the molecular signals, such as cross-kingdom interactions between bacteria and fungi in natural environments, remain largely unexplored.\n                      <jats:italic toggle=\"yes\">Lysobacter enzymogenes<\/jats:italic>\n                      is a widespread predatory bacterium that produces the antifungal secondary metabolite heat-stable antifungal factor (HSAF), which enables interactions with diverse fungi. Here, we investigated the interkingdom interactions between\n                      <jats:italic toggle=\"yes\">L. enzymogenes<\/jats:italic>\n                      and the environmental fungus\n                      <jats:italic toggle=\"yes\">Candida krusei<\/jats:italic>\n                      , both of which are widely distributed, to elucidate the bacterial-fungal communication. We found that the antagonistic effect of bacteria-fungi was significant under both contact and non-contact co-culture conditions, indicating the involvement of diffusible metabolites. Given that farnesol is a common quorum-sensing (QS) molecule in\n                      <jats:italic toggle=\"yes\">Candida<\/jats:italic>\n                      , metabolite profiling combined with exogenous addition and biosynthesis inhibition experiments demonstrated that farnesol functions as a cross-kingdom signal regulating HSAF production and bacterial antagonism. Further mechanistic analysis of the intrinsic mechanism revealed that the two-component system (TCS) RcsB\/C in\n                      <jats:italic toggle=\"yes\">L. enzymogenes<\/jats:italic>\n                      can sense farnesol and activate the production of HSAF through the MarR family regulators, mediating the antagonistic pathway. In addition, our work identified the key amino acid residues in RcsC of\n                      <jats:italic toggle=\"yes\">L. enzymogenes<\/jats:italic>\n                      responsible for recognizing farnesol. In summary, we report the bacterial TCS involved in farnesol sensing and reveal a novel bacterial-fungal antagonistic mechanism, in which\n                      <jats:italic toggle=\"yes\">L. enzymogenes<\/jats:italic>\n                      \u201chijacks\u201d a fungal QS molecule to enhance its antifungal capacity, uncovering a previously unrecognized strategy of cross-kingdom communication.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        Bacteria and fungi frequently interact in shared habitats, yet the chemical cues that shape these cross-kingdom relationships remain poorly defined. Farnesol is a well-known quorum-sensing molecule in\n                        <jats:italic toggle=\"yes\">Candida<\/jats:italic>\n                        , but its ecological roles beyond fungal communication are unclear. Here, we show that\n                        <jats:italic toggle=\"yes\">Lysobacter enzymogenes<\/jats:italic>\n                        directly senses fungal-derived farnesol through the RcsB\/C two-component system, which activates the downstream regulator MarR-2 and induces the production of the antifungal metabolite heat-stable antifungal factor (HSAF). This signal hijacking strategy allows\n                        <jats:italic toggle=\"yes\">L. enzymogenes<\/jats:italic>\n                        to convert a fungal communication molecule into a cue that strengthens its antagonistic capacity. We further identify key amino acid residues in RcsC responsible for farnesol recognition, revealing the bacterial two-component system (TCS) known to detect this molecule. These findings expand the functional scope of fungal quorum-sensing signals, uncover a previously unrecognized mechanism of interkingdom antagonism, and provide insights with potential applications in microbiome-based biocontrol.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/aem.00304-26","type":"journal-article","created":{"date-parts":[[2026,4,3]],"date-time":"2026-04-03T13:00:31Z","timestamp":1775221231000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["Hijacking competitor-derived signals: RcsB\/C drives\n                    <i>Lysobacter enzymogenes<\/i>\n                    to exploit farnesol for enhanced antifungal capacity"],"prefix":"10.1128","volume":"92","author":[{"given":"Fang","family":"Nan","sequence":"first","affiliation":[{"name":"Marine Microbial Resource Center, MOE Key Laboratory of Evolution and Marine 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