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In this study, we investigated the coaggregation properties of both bacteria and identified the molecules that mediate their interaction. Among\n                      <jats:italic toggle=\"yes\">A. actinomycetemcomitans<\/jats:italic>\n                      serotypes a, b, c, d, and g,\n                      <jats:italic toggle=\"yes\">F. nucleatum<\/jats:italic>\n                      strains coaggregated specifically with serotypes b and d. The coaggregation between\n                      <jats:italic toggle=\"yes\">F. nucleatum<\/jats:italic>\n                      and\n                      <jats:italic toggle=\"yes\">A. actinomycetemcomitans<\/jats:italic>\n                      serotype b was significantly suppressed by the addition of lipopolysaccharide (LPS) extracted from\n                      <jats:italic toggle=\"yes\">A. actinomycetemcomitans<\/jats:italic>\n                      serotype b. Among the sugars comprising the O-polysaccharide (O-PS) of serotype b LPS, the addition of\n                      <jats:italic toggle=\"yes\">N<\/jats:italic>\n                      -acetyl-\n                      <jats:sub>D<\/jats:sub>\n                      -galactosamine markedly inhibited their coaggregation. Similarly, the coaggregation between\n                      <jats:italic toggle=\"yes\">F. nucleatum<\/jats:italic>\n                      and\n                      <jats:italic toggle=\"yes\">A. actinomycetemcomitans<\/jats:italic>\n                      serotype d was strongly inhibited by the addition of either the LPS extracted from\n                      <jats:italic toggle=\"yes\">A. actinomycetemcomitans<\/jats:italic>\n                      serotype d or the\n                      <jats:sub>L<\/jats:sub>\n                      -rhamnose present in serotype d O-PS. Furthermore, analysis of outer membrane autotransporter proteins as potential coaggregation factors of\n                      <jats:italic toggle=\"yes\">F. nucleatum<\/jats:italic>\n                      revealed that mutants lacking functional\n                      <jats:italic toggle=\"yes\">fap2<\/jats:italic>\n                      or\n                      <jats:italic toggle=\"yes\">cmpA<\/jats:italic>\n                      exhibited significantly reduced coaggregation with\n                      <jats:italic toggle=\"yes\">A. actinomycetemcomitans<\/jats:italic>\n                      serotype b or d, respectively. Additionally, we found that these coaggregations significantly promoted biofilm formation during coculture. These findings suggest that the coaggregation between\n                      <jats:italic toggle=\"yes\">F. nucleatum<\/jats:italic>\n                      and\n                      <jats:italic toggle=\"yes\">A. actinomycetemcomitans<\/jats:italic>\n                      serotypes b and d is mediated through interactions between autotransporter proteins and LPSs, thereby contributing to the development of mature biofilms.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>IMPORTANCE<\/jats:title>\n                    <jats:p>\n                      <jats:italic toggle=\"yes\">Fusobacterium nucleatum<\/jats:italic>\n                      is a periodontal pathogen that acts as a bridging organism by coaggregating with various oral microbes, including other periodontal pathogens. Recently, this bacterium has been reported to be associated with systemic diseases, including cardiovascular diseases, adverse pregnancy outcomes, and cancer.\n                      <jats:italic toggle=\"yes\">F. nucleatum<\/jats:italic>\n                      possesses numerous adhesins, including autotransporter proteins that are considered to mediate colonization in human tissues. Our study demonstrated that\n                      <jats:italic toggle=\"yes\">F. nucleatum<\/jats:italic>\n                      utilizes two autotransporter proteins (Fap2 and CmpA) to coaggregate with another periodontal pathogen,\n                      <jats:italic toggle=\"yes\">Aggregatibacter actinomycetemcomitans<\/jats:italic>\n                      , through specific interactions with bacterial surface polysaccharides. In addition to the roles of these autotransporters in periodontitis through bacterial coaggregation with other oral bacterial species, our findings potentially provide new insights into the mechanism underlying systemic diseases caused by\n                      <jats:italic toggle=\"yes\">F. nucleatum<\/jats:italic>\n                      binding to host cell carbohydrates and glycoproteins.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/aem.01132-25","type":"journal-article","created":{"date-parts":[[2025,10,20]],"date-time":"2025-10-20T13:00:54Z","timestamp":1760965254000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":3,"title":["The outer membrane autotransporters Fap2 and CmpA facilitate specific coaggregation between\n                    <i>Fusobacterium nucleatum<\/i>\n                    and\n                    <i>Aggregatibacter actinomycetemcomitans<\/i>\n                 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