{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T22:32:37Z","timestamp":1789597957812,"version":"build-2803163510"},"reference-count":55,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2024,1,9]],"date-time":"2024-01-09T00:00:00Z","timestamp":1704758400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Microbiol."],"abstract":"<jats:p><jats:italic>Mycoplasma synoviae<\/jats:italic> (<jats:italic>M. synoviae<\/jats:italic>) is one of the major poultry pathogens causing infectious synovitis, airsacculitis, a high incidence of shell breakage, and egg production loss. However, the pathogenesis of <jats:italic>M. synoviae<\/jats:italic> remains unclear. Adhesion of mycoplasmas to host cells is a crucial step in infection and colonization. The purpose of this study was to determine the adhesive function of a putative P80 family lipoprotein (LP78) and evaluate its application in the detection of antibodies against <jats:italic>M. synoviae<\/jats:italic>. Recombinant LP78 (rLP78) was expressed in the supernatant component of <jats:italic>Escherichia coli<\/jats:italic> and mouse anti-rLP78 serum was prepared. Bioinformatic analysis and western blotting results revealed that LP78 was conservative among <jats:italic>M. synoviae<\/jats:italic> strains. It was distributed not only in the cytoplasm but also on the membrane of <jats:italic>M. synoviae<\/jats:italic> through western blotting and indirect immunofluorescence (IFA). The adherence of <jats:italic>M. synoviae<\/jats:italic> to DF-1 cells was significantly inhibited by mouse anti-rLP78 serum (<jats:italic>p<\/jats:italic>\u2009&amp;lt;\u20090.01). IFA revealed that rLP78 adhered to DF-1 cells, and this adherence was prevented by mouse anti-rLP78 serum. Furthermore, rLP78 was found to bind to the DF-1 cells membrane proteins in a dose-dependent manner by enzyme-linked immunosorbent assay (ELISA). Screening of DF-1 cells membrane proteins by western blotting showed that proteins with molecular weight of 35\u201340\u2009kDa and 55\u201370\u2009kDa bound to rLP78. Moreover, rLP78 was identified to be a fibronectin\/plasminogen binding protein. The sensitivity and specificity of rLP78-based iELISA were 85.7 and 94.1%, respectively. The maximum dilution of positive serum (HI titer, 1:128) detected via rLP78-based iELISA was 1:6,400, whereas that detected using a commercial ELISA kit was 1:12,800\u20131:25,600. Both rLP78-based iELISA and the commercial ELISA kit detected seroconversion after 7\u2009days of challenge and immunization. No cross-reactivity with positive sera against other avian pathogens was observed in rLP78-based iELISA. Collectively, these results indicate that LP78 is a fibronectin\/plasminogen-binding adhesion protein of <jats:italic>M. synoviae<\/jats:italic> and a potential diagnostic antigen. The present study will facilitate a better understanding of the pathogenesis of <jats:italic>M. synoviae<\/jats:italic> and the development of new diagnostic.<\/jats:p>","DOI":"10.3389\/fmicb.2023.1335658","type":"journal-article","created":{"date-parts":[[2024,1,9]],"date-time":"2024-01-09T04:32:25Z","timestamp":1704774745000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":11,"title":["Mycoplasma synoviae LP78 is a fibronectin\/plasminogen binding protein, putative adhesion, and potential diagnostic antigen"],"prefix":"10.3389","volume":"14","author":[{"given":"Shuizhong","family":"Han","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ying","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lizhen","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wenchi","family":"Chang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bo","family":"Wen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Junyang","family":"Fang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaolan","family":"Hou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xuefeng","family":"Qi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jingyu","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2024,1,9]]},"reference":[{"key":"ref1","doi-asserted-by":"publisher","first-page":"2468","DOI":"10.1128\/IAI.65.6.2468-2471.1997","article-title":"Adherence of Mycoplasma gallisepticum involves variable surface membrane proteins","volume":"65","author":"Athamna","year":"1997","journal-title":"Infect. 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