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In general, hemagglutination can be considered the ability to adhere to host cells; however,\n            <jats:italic>P. gingivalis<\/jats:italic>\n            -mediated hemagglutination has special significance because heme markedly accelerates growth of this bacterium. Although a number of studies have indicated that a major hemagglutinin of\n            <jats:italic>P. gingivalis<\/jats:italic>\n            is intragenically encoded by\n            <jats:italic>rgpA<\/jats:italic>\n            ,\n            <jats:italic>kgp<\/jats:italic>\n            , and\n            <jats:italic>hagA<\/jats:italic>\n            , direct evidence has not been obtained. We demonstrated in this study that recombinant HGP44\n            <jats:sub>720-1081<\/jats:sub>\n            , a fully processed HGP44 domain protein, had hemagglutinating activity but that an unprocessed form, HGP44\n            <jats:sub>720-1138<\/jats:sub>\n            , did not. A peptide corresponding to residues 1083 to 1102, which was included in HGP44\n            <jats:sub>720-1138<\/jats:sub>\n            but not in HGP44\n            <jats:sub>720-1081<\/jats:sub>\n            , could bind HGP44\n            <jats:sub>720-1081<\/jats:sub>\n            in a dose-dependent manner and effectively inhibited HGP44\n            <jats:sub>720-1081<\/jats:sub>\n            -mediated hemagglutination, indicating that the interdomain regional amino acid sequence may function as an intramolecular suppressor of hemagglutinating activity. Analyses by solid-phase binding and chemical cross-linking suggested that HGP44 interacted with glycophorin A on the erythrocyte membrane. Glycophorin A and, more effectively, asialoglycophorin, which were added exogenously, inhibited HGP44\n            <jats:sub>720-1081<\/jats:sub>\n            -mediated hemagglutination. Treatment of erythrocytes with RgpB proteinase resulted in degradation of glycophorin A on the membrane and a decrease in HGP44\n            <jats:sub>720-1081<\/jats:sub>\n            -mediated hemagglutination. Surface plasmon resonance detection analysis revealed that HGP44\n            <jats:sub>720-1081<\/jats:sub>\n            could bind to asialoglycophorin with a dissociation constant of 3.0 \u00d7 10\n            <jats:sup>\u22127<\/jats:sup>\n            M. These results indicate that the target of HGP44 on the erythrocyte membrane appears to be glycophorin A.\n          <\/jats:p>","DOI":"10.1128\/jb.01691-06","type":"journal-article","created":{"date-parts":[[2007,3,24]],"date-time":"2007-03-24T00:52:54Z","timestamp":1174697574000},"page":"3977-3986","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":33,"title":["Construction of Recombinant Hemagglutinin Derived from the Gingipain-Encoding Gene of\n            <i>Porphyromonas gingivalis<\/i>\n            , Identification of Its Target Protein on Erythrocytes, and Inhibition of Hemagglutination by an Interdomain Regional Peptide"],"prefix":"10.1128","volume":"189","author":[{"given":"Eiko","family":"Sakai","sequence":"first","affiliation":[{"name":"Division of Oral Pathopharmacology, Department of Developmental and Reconstructive Medicine"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mariko","family":"Naito","sequence":"additional","affiliation":[{"name":"Division of Microbiology and Oral Infection, Department of Molecular Microbiology and Immunology"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Keiko","family":"Sato","sequence":"additional","affiliation":[{"name":"Division of Microbiology and Oral Infection, Department of Molecular Microbiology and Immunology"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hitoshi","family":"Hotokezaka","sequence":"additional","affiliation":[{"name":"Division of Orthodontics and Dentofacial Orthopedics, Department of Developmental and Reconstructive Medicine, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tomoko","family":"Kadowaki","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Graduate School of Dental Science, Kyushu University, Fukuoka, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Arihide","family":"Kamaguchi","sequence":"additional","affiliation":[{"name":"Department of Oral Microbiology, School of Dentistry, Health Sciences University of Hokkaido, Sapporo, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kenji","family":"Yamamoto","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Graduate School of Dental Science, Kyushu University, Fukuoka, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kuniaki","family":"Okamoto","sequence":"additional","affiliation":[{"name":"Division of Oral Pathopharmacology, Department of Developmental and Reconstructive Medicine"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Koji","family":"Nakayama","sequence":"additional","affiliation":[{"name":"Division of Microbiology and Oral Infection, Department of Molecular Microbiology and Immunology"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.179.15.4778-4788.1997"},{"key":"e_1_3_2_3_2","first-page":"229","volume":"14","year":"1988","unstructured":"Aminoff, D. 1988. 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