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To fill this gap, we used\n                      <jats:italic>Klebsiella pneumoniae<\/jats:italic>\n                      (KP) and two different plasmid-encoded AmpCs [DHA-1 (AmpR regulator linked, inducible) and CMY-2 (constitutive)] as models to perform a study in which we show that blockade of peptidoglycan recycling through AmpG permease inactivation abolished DHA-1 inducibility but did not affect CMY-2 production and neither did it alter KP pathogenic behavior. Moreover, whereas regular production of both AmpC-type enzymes did not attenuate KP virulence, when\n                      <jats:italic>bla<\/jats:italic>\n                      DHA-1 was expressed in an\n                      <jats:italic>ampG<\/jats:italic>\n                      -defective mutant,\n                      <jats:italic>Galleria mellonella<\/jats:italic>\n                      killing was significantly (but not drastically) attenuated. Spontaneous DHA-1 hyperproducer mutants were readily obtained\n                      <jats:italic>in vitro<\/jats:italic>\n                      , showing slight or insignificant virulence attenuations together with high-level resistance to \u03b2-lactams only mildly affected by basal production (e.g., ceftazidime, ceftolozane\/tazobactam). By analyzing diverse DHA-1-harboring clinical KP strains, we demonstrate that the natural selection of these hyperproducers is not exceptional (&gt;10% of the collection), whereas mutational inactivation of the typical AmpC hyperproduction-related gene\n                      <jats:italic>mpl<\/jats:italic>\n                      was the most frequent underlying mechanism. The potential silent dissemination of this kind of strains, for which an important fitness cost-related contention barrier does not seem to exist, is envisaged as a neglected threat for most \u03b2-lactams effectiveness, including recently introduced combinations. Analyzing whether this phenomenon is applicable to other transferable \u03b2-lactamases and species as well as determining the levels of conferred resistance poses an essential topic to be addressed.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        Although there is solid knowledge about the regulation of transferable and especially chromosomal AmpC \u03b2-lactamases in Enterobacterales, there are still gaps to fill, mainly related to regulatory mechanisms and virulence interplays of the former. This work addresses them using\n                        <jats:italic>Klebsiella pneumoniae<\/jats:italic>\n                        as model, delving into a barely explored conception: the acquisition of a plasmid-encoded inducible AmpC-type enzyme whose production can be increased through selection of chromosomal mutations, entailing dramatically increased resistance compared to basal expression but minor associated virulence costs. Accordingly, we demonstrate that clinical\n                        <jats:italic>K. pneumoniae<\/jats:italic>\n                        DHA-1 hyperproducer strains are not exceptional. Through this study, we warn for the first time that this phenomenon may be a neglected new threat for \u03b2-lactams effectiveness (including some recently introduced ones) silently spreading in the clinical context, not only in\n                        <jats:italic>K. pneumoniae<\/jats:italic>\n                        but potentially also in other pathogens. These facts must be carefully considered in order to design future resistance-preventive strategies.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/aac.01315-23","type":"journal-article","created":{"date-parts":[[2024,3,22]],"date-time":"2024-03-22T09:01:13Z","timestamp":1711098073000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":6,"title":["Transferable AmpCs in\n                    <i>Klebsiella pneumoniae<\/i>\n                    : interplay with peptidoglycan recycling, mechanisms of hyperproduction, and virulence implications"],"prefix":"10.1128","volume":"68","author":[{"given":"Isabel M.","family":"Barcel\u00f3","sequence":"first","affiliation":[{"name":"Health Research Institute of the Balearic Islands (IdISBa), Palma, Spain"},{"name":"Microbiology Department, University Hospital Son Espases (HUSE), Palma, Spain"},{"name":"Centro de 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