{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T18:32:26Z","timestamp":1790793146271,"version":"4.1.0"},"reference-count":58,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2016,4,1]],"date-time":"2016-04-01T00:00:00Z","timestamp":1459468800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100003625","name":"Ministry of Health and Welfare","doi-asserted-by":"publisher","award":["HI13C1945"],"award-info":[{"award-number":["HI13C1945"]}],"id":[{"id":"10.13039\/501100003625","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Clin Vaccine Immunol"],"published-print":{"date-parts":[[2016,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Fimbrial protein fimbrillin (FimA), a major structural subunit of\n            <jats:named-content content-type=\"genus-species\">Porphyromonas gingivalis<\/jats:named-content>\n            , has been suggested as a vaccine candidate to control\n            <jats:named-content content-type=\"genus-species\">P. gingivalis<\/jats:named-content>\n            -induced periodontal disease. Previously, cDNAs encoding IgG monoclonal antibodies (MAbs) against purified FimA from\n            <jats:named-content content-type=\"genus-species\">P. gingivalis<\/jats:named-content>\n            2561 have been cloned, and the MAbs have been produced in rice cell suspension. Here we examined the biological activities of the plant-produced MAb specific for FimA (anti-FimA plantibody) of\n            <jats:named-content content-type=\"genus-species\">P. gingivalis<\/jats:named-content>\n            <jats:italic>in vitro<\/jats:italic>\n            and\n            <jats:italic>in vivo<\/jats:italic>\n            . The anti-FimA plantibody recognized oligomeric\/polymeric forms of native FimA in immunoblot analysis and showed high affinity for native FimA (\n            <jats:italic>\n              K\n              <jats:sub>D<\/jats:sub>\n            <\/jats:italic>\n            = 0.11 nM). Binding of\n            <jats:named-content content-type=\"genus-species\">P. gingivalis<\/jats:named-content>\n            (10\n            <jats:sup>8<\/jats:sup>\n            cells) to 2 mg of saliva-coated hydroxyapatite beads was reduced by 53.8% in the presence of 1 \u03bcg\/ml plantibody. Anti-FimA plantibody (10 \u03bcg\/ml) reduced invasion of periodontal ligament cells by\n            <jats:named-content content-type=\"genus-species\">P. gingivalis<\/jats:named-content>\n            (multiplicity of infection, 100) by 68.3%. Intracellular killing of\n            <jats:named-content content-type=\"genus-species\">P. gingivalis<\/jats:named-content>\n            opsonized with the anti-FimA plantibody by mouse macrophages was significantly increased (77.1%) compared to killing of bacterial cells with irrelevant IgG (36.7%). In a mouse subcutaneous chamber model, the number of recoverable\n            <jats:named-content content-type=\"genus-species\">P. gingivalis<\/jats:named-content>\n            cells from the chamber fluid was significantly reduced when the numbers of bacterial cells opsonized with anti-FimA plantibody were compared with the numbers of bacterial cells with irrelevant IgG, 66.7% and 37.1%, respectively. These\n            <jats:italic>in vitro<\/jats:italic>\n            and\n            <jats:italic>in vivo<\/jats:italic>\n            effects of anti-FimA plantibody were comparable to those of the parental MAb. Further studies with\n            <jats:named-content content-type=\"genus-species\">P. gingivalis<\/jats:named-content>\n            strains with different types of fimbriae are needed to investigate the usefulness of anti-FimA plantibody for passive immunization to control\n            <jats:named-content content-type=\"genus-species\">P. gingivalis<\/jats:named-content>\n            -induced periodontal disease.\n          <\/jats:p>","DOI":"10.1128\/cvi.00620-15","type":"journal-article","created":{"date-parts":[[2016,2,11]],"date-time":"2016-02-11T20:33:19Z","timestamp":1455222799000},"page":"346-352","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":15,"title":["Potent\n            <i>In Vitro<\/i>\n            and\n            <i>In Vivo<\/i>\n            Activity of Plantibody Specific for Porphyromonas gingivalis FimA"],"prefix":"10.1128","volume":"23","author":[{"given":"Young-Suk","family":"Choi","sequence":"first","affiliation":[{"name":"Department of Maxillofacial Biomedical Engineering, School of Dentistry, and Institute of Oral Biology, Kyung Hee University, Seoul, Republic of Korea"},{"name":"Department of Dental Hygiene, Shinsung University, Chungnam, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0286-5297","authenticated-orcid":false,"given":"Ji-Hoi","family":"Moon","sequence":"additional","affiliation":[{"name":"Department of Maxillofacial Biomedical Engineering, School of Dentistry, and Institute of Oral Biology, Kyung Hee University, Seoul, Republic of Korea"},{"name":"Department of Life and Nanopharmaceutical Sciences, Kyung Hee University, Seoul, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tae-Geum","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of 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