{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T14:45:47Z","timestamp":1791902747845,"version":"4.3.4"},"reference-count":48,"publisher":"American Society for Microbiology","license":[{"start":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:00:00Z","timestamp":1791849600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:00:00Z","timestamp":1791849600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI173544"],"award-info":[{"award-number":["AI173544"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI187284"],"award-info":[{"award-number":["AI187284"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM131729"],"award-info":[{"award-number":["GM131729"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","award":["GT17580"],"award-info":[{"award-number":["GT17580"]}],"id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title\/>\n                    <jats:p>\n                      <jats:italic toggle=\"yes\">Mycobacterium abscessus<\/jats:italic>\n                      is a non-tuberculous\n                      <jats:italic toggle=\"yes\">Mycobacterium<\/jats:italic>\n                      (NTM) that is often associated with respiratory infections in persons with cystic fibrosis. High levels of antibiotic resistance make\n                      <jats:italic toggle=\"yes\">M. abscessus<\/jats:italic>\n                      infections difficult to treat, highlighting the urgent need for alternative therapeutic strategies. Mycobacteriophage therapy\u2014treatment of infections with viruses that infect\n                      <jats:italic toggle=\"yes\">Mycobacterium<\/jats:italic>\n                      hosts\u2014shows considerable promise, but the narrow host specificity of the current mycobacteriophage repertoire limits this approach to personalized therapies. Here, we characterize the anti-\n                      <jats:italic toggle=\"yes\">M<\/jats:italic>\n                      .\n                      <jats:italic toggle=\"yes\">abscessus<\/jats:italic>\n                      activity of mycobacteriophage-encoded Lysin B enzymes (lysterases). Lysterases are serine-esterases that cleave the ester bonds linking mycolic acids to either arabinogalactan or trehalose in the mycobacterial cell envelope to complete the lysis process. In this study, we explored their ability to kill a spectrum of clinically isolated\n                      <jats:italic toggle=\"yes\">M. abscessus<\/jats:italic>\n                      strains when administered exogenously. Six phylogenetically distinct lysterases were purified, characterized on the surrogate\n                      <jats:italic toggle=\"yes\">M. smegmatis<\/jats:italic>\n                      , and their activity against a diverse panel of 24\n                      <jats:italic toggle=\"yes\">M. abscessus<\/jats:italic>\n                      clinical strains was assessed. The enzymes exhibit a range of activities against these strains, but most have broad-spectrum activity with only minor variations among the\n                      <jats:italic toggle=\"yes\">M. abscessus<\/jats:italic>\n                      isolates. However, the activities can be quite potent, resulting in up to six orders of magnitude of reduction in viability within 4 h with one activity unit of the enzymes, and act synergistically with amikacin. Overall, mycobacteriophage-encoded lysterases show considerable potential for antimycobacterial control, especially for topical applications.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        <jats:italic toggle=\"yes\">Mycobacterium<\/jats:italic>\n                        infections are clinically challenging, and there is a high failure of resolving\n                        <jats:italic toggle=\"yes\">Mycobacterium abscessus<\/jats:italic>\n                        infections using antibiotics. Mycobacteriophages show promise in treating\n                        <jats:italic toggle=\"yes\">M. abscessus<\/jats:italic>\n                        infections, but there is substantial variation among clinical isolates in their phage infection profiles. Mycobacteriophages are unusual in coding for lysis enzymes\u2014lysterases\u2014that target cell wall exposed constituents, and these can have potential antibacterial activity. Exploring the vast sequence diversity of thousands of phage-encoded lysterases identifies a subset that was expressed, purified, and tested for their ability to kill a broad range of\n                        <jats:italic toggle=\"yes\">M. abscessus<\/jats:italic>\n                        clinical strains. Lysterases with the broadest and greatest activity offer substantial potential for treatment of\n                        <jats:italic toggle=\"yes\">M. abscessus<\/jats:italic>\n                        infection, especially where they display synergism with current antibiotics.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/jb.00410-26","type":"journal-article","created":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T13:48:43Z","timestamp":1791899323000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["Anti-mycobacterial activity of phage-encoded lysterases"],"prefix":"10.1128","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8638-1972","authenticated-orcid":true,"given":"Jindanuch","family":"Maneekul","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05dte6685","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biological Sciences, University of Pittsburgh","place":["Pittsburgh, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Krista G.","family":"Freeman","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05dte6685","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biological Sciences, University of Pittsburgh","place":["Pittsburgh, USA"]},{"id":[{"id":"https:\/\/ror.org\/051fd9666","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Physics, Case Western Reserve University","place":["Cleveland, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0001-0104-2945","authenticated-orcid":false,"given":"Elizabeth D.","family":"Amarh","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05dte6685","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biological Sciences, University of Pittsburgh","place":["Pittsburgh, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julia M.","family":"Kovalski","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05dte6685","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biological Sciences, University of Pittsburgh","place":["Pittsburgh, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emma","family":"Skeel","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05dte6685","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biological Sciences, University of 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