{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T20:27:26Z","timestamp":1792787246514,"version":"4.5.0"},"reference-count":49,"publisher":"American Society for Microbiology","issue":"10","license":[{"start":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T00:00:00Z","timestamp":1791244800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T00:00:00Z","timestamp":1791244800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"name":"Key Program of the Natural Science Foundation of Gansu Province","award":["25JRRA350"],"award-info":[{"award-number":["25JRRA350"]}]},{"name":"National Natural Science Foundation of China","award":["32072863"],"award-info":[{"award-number":["32072863"]}],"id":[{"id":"https:\/\/ror.org\/01h0zpd94","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Microbiol Spectr"],"published-print":{"date-parts":[[2026,10,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title\/>\n                    <jats:p>\n                      <jats:italic toggle=\"yes\">Mycoplasmopsis synoviae<\/jats:italic>\n                      is an important pathogen in poultry that primarily causes synovitis, tenosynovitis, eggshell abnormalities, and respiratory diseases, resulting in significant economic losses to the poultry industry worldwide. The aim of this study was to systematically screen and characterize the proteins secreted by\n                      <jats:italic toggle=\"yes\">M. synoviae<\/jats:italic>\n                      and to investigate the role of SSB in\n                      <jats:italic toggle=\"yes\">M. synoviae<\/jats:italic>\n                      infection. We first identified 13 proteins secreted by\n                      <jats:italic toggle=\"yes\">M. synoviae<\/jats:italic>\n                      using liquid chromatography\u2012tandem mass spectrometry analysis. Bioinformatic analysis of SSBs revealed that they lack a transmembrane domain and the characteristic features of a cleavable signal peptide and are potential virulence factors. After induced expression and purification of SSB from\n                      <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                      , rabbit anti-SSB serum was prepared. Subcellular localization analysis by immunogold labeling and Western blotting further confirmed that SSB is present mainly in the cytoplasm and culture supernatant of\n                      <jats:italic toggle=\"yes\">M. synoviae<\/jats:italic>\n                      . ELISA and indirect immunofluorescence analyses revealed that SSB binds to membrane proteins and adheres to the surface of chicken DF-1 cells and that rabbit anti-SSB serum significantly inhibits\n                      <jats:italic toggle=\"yes\">M. synoviae<\/jats:italic>\n                      adhesion to DF-1 cells.\n                      <jats:italic toggle=\"yes\">In vitro<\/jats:italic>\n                      experiments confirmed that SSB could interact directly with plasminogen and fibronectin in a dose-dependent manner. In addition, our study revealed that SSB significantly promoted Annexin A2 (AnxA2) protein expression in DF-1 cells during adhesion, significantly colocalized with AnxA2, and promoted its enrichment at the membrane. These findings offer a novel experimental foundation for understanding the molecular mechanisms underlying the role of the secreted protein SSB in\n                      <jats:italic toggle=\"yes\">M. synoviae<\/jats:italic>\n                      infection.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        Pathogenic bacteria transport proteins to the extracellular compartment through a variety of secretion systems, and most of these secreted proteins act as adhesins, toxins, or immunomodulatory molecules in host cells, playing an important role in bacterial pathogenesis. However, studies on secreted proteins of\n                        <jats:italic toggle=\"yes\">Mycoplasmopsis synoviae<\/jats:italic>\n                        are still incomplete. In our study, we systematically screened and identified the secreted proteins of\n                        <jats:italic toggle=\"yes\">M. synoviae<\/jats:italic>\n                        strain WVU1853 for the first time and conducted an in-depth investigation of the role of SSB, one of the secreted proteins, in the infection process,\n                        <jats:italic toggle=\"yes\">in vitro<\/jats:italic>\n                        . Our results not only reveal the key role of SSB in the infection process of\n                        <jats:italic toggle=\"yes\">M. synoviae<\/jats:italic>\n                        but also provide a new theoretical basis for studying the invasion mechanisms of\n                        <jats:italic toggle=\"yes\">Mycoplasma<\/jats:italic>\n                        -secreted proteins and related processes.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/spectrum.00858-26","type":"journal-article","created":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T13:00:10Z","timestamp":1787835610000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["A secreted protein of\n                    <i>Mycoplasmopsis synoviae<\/i>\n                    , SSB, is a critical adhesion factor that promotes the enrichment of Annexin A2 at the cell membrane"],"prefix":"10.1128","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-1231-5848","authenticated-orcid":false,"given":"Qing","family":"Wang","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05ym42410","id-type":"ROR","asserted-by":"publisher"}],"name":"College of Veterinary Medicine, Gansu Agricultural University","place":["Lanzhou, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yunhai","family":"Zhao","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05ym42410","id-type":"ROR","asserted-by":"publisher"}],"name":"College of Veterinary Medicine, Gansu Agricultural University","place":["Lanzhou, China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haiyun","family":"Ma","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05ym42410","id-type":"ROR","asserted-by":"publisher"}],"name":"College of Veterinary Medicine, Gansu Agricultural University","place":["Lanzhou, 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