{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T06:04:14Z","timestamp":1790316254003,"version":"4.1.0"},"reference-count":176,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2025,7,9]],"date-time":"2025-07-09T00:00:00Z","timestamp":1752019200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2025,7,9]],"date-time":"2025-07-09T00:00:00Z","timestamp":1752019200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["AI007476, AI172194"],"award-info":[{"award-number":["AI007476, AI172194"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["AI043987, AI175460"],"award-info":[{"award-number":["AI043987, AI175460"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007155","name":"Medical Research Council","doi-asserted-by":"publisher","award":["MR\/R017662\/1, MR\/W000814\/1"],"award-info":[{"award-number":["MR\/R017662\/1, MR\/W000814\/1"]}],"id":[{"id":"10.13039\/501100007155","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["mBio"],"published-print":{"date-parts":[[2025,7,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title\/>\n                    <jats:p>\n                      Prior analyses suggested that the type II secretion system (T2SS) of\n                      <jats:italic toggle=\"yes\">Legionella pneumophila<\/jats:italic>\n                      secretes \u226547 proteins beyond its 26 known substrates. Upon examination of mutants of wild-type strain 130b that lack those exoproteins most conserved across the\n                      <jats:italic toggle=\"yes\">Legionella<\/jats:italic>\n                      genus, we discovered that protein \u201c06635\u201d majorly promotes\n                      <jats:italic toggle=\"yes\">L. pneumophila<\/jats:italic>\n                      replication within amoebae. Immunoblotting, proteomics, and whole-cell enzyme-linked immunosorbent assay (ELISA) confirmed that 06635 exists in culture supernatants and on the bacterial outer surface and does so in a T2SS-dependent manner. Bioinformatic analyses identified 06635 as a novel member of the carbohydrate esterase family 4, whose members deacetylate bacterial surface polysaccharides, peptidoglycan, chitins, and\/or xylans. Given 06635\u2019s T2SS-dependent secretion, low-level amino acid similarity to known peptidoglycan deacetylases, and the unaltered lysozyme resistance of a\n                      <jats:italic toggle=\"yes\">06635<\/jats:italic>\n                      mutant, we pursued the hypothesis that 06635 deacetylates a polysaccharide on\n                      <jats:italic toggle=\"yes\">L. pneumophila<\/jats:italic>\n                      \u2019s surface. Supporting this, the\n                      <jats:italic toggle=\"yes\">06635<\/jats:italic>\n                      mutant exhibited increased binding to both wheat germ agglutinin (i.e., more surface\n                      <jats:italic toggle=\"yes\">N<\/jats:italic>\n                      -acetylglucosamine) and antibodies that recognize acetylated lipopolysaccharide (LPS). Nuclear magnetic resonance (NMR) analysis of isolated mutant vs wild-type LPS confirmed that 06635 promotes LPS deacetylation. Thus, we designated 06635 as PdaA, for\n                      <jats:underline>p<\/jats:underline>\n                      olysaccharide\n                      <jats:underline>d<\/jats:underline>\n                      e\n                      <jats:underline>a<\/jats:underline>\n                      cetylase\n                      <jats:underline>A<\/jats:underline>\n                      . Compatible with its altered surface, the\n                      <jats:italic toggle=\"yes\">pdaA<\/jats:italic>\n                      mutant showed greater autoaggregation, increased biofilm formation, and heightened sensitivity to both polymyxin and human serum. Thus, we hypothesize that, following its secretion via the T2SS, PdaA deacetylates LPS, and perhaps other moieties, impacting many significant processes. While defining PdaA, we identified many more putative substrates of the\n                      <jats:italic toggle=\"yes\">L. pneumophila<\/jats:italic>\n                      T2SS, bringing the size of the T2SS output to approximately 120.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        <jats:italic toggle=\"yes\">Legionella pneumophila<\/jats:italic>\n                        is the principal cause of Legionnaires\u2019 disease, an increasingly common form of pneumonia. Although prior work demonstrated that the bacterium utilizes its type II protein secretion system (T2SS) to survive in aquatic environments and to cause lung infection, the full scope and impact of this\n                        <jats:italic toggle=\"yes\">Legionella<\/jats:italic>\n                        secretion system is still relatively underappreciated. By utilizing an expanded proteomic approach and testing newly made mutants in a wide range of assays, we have determined that the\n                        <jats:italic toggle=\"yes\">L. pneumophila<\/jats:italic>\n                        type II secretome encompasses approximately 120 proteins, and among these proteins is a novel polysaccharide deacetylase (PdaA) that modulates the\n                        <jats:italic toggle=\"yes\">L. pneumophila<\/jats:italic>\n                        surface and lipopolysaccharide, impacting intracellular infection, biofilm formation, and resistance to both antibiotics and human serum. Moreover, since T2SSs and homologs of PdaA were found in many other bacteria, our findings should also have implications for understanding other infectious diseases and environmental processes.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/mbio.01393-25","type":"journal-article","created":{"date-parts":[[2025,6,20]],"date-time":"2025-06-20T09:00:32Z","timestamp":1750410032000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":7,"title":["<i>Legionella pneumophila<\/i>\n                    type II secretome reveals a polysaccharide deacetylase that impacts intracellular infection, biofilm formation, and resistance to polymyxin- and serum-mediated killing"],"prefix":"10.1128","volume":"16","author":[{"given":"Carlton 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