title: The Sialic Acid Binding Protein, Hsa, in Streptococcus gordonii DL1 also Mediates Intergeneric Coaggregation with Veillonella Species.
abstract: Dental biofilm development involves initial colonization of the tooth's surface by pioneer colonizers, followed by cell-cell coaggregation between the pioneer and later colonizers. Streptococcus gordonii is one of the pioneer colonizers. In addition to its role in oral biofilm development, S. gordonii also is a pathogen in infective endocarditis in susceptible humans. A surface adhesin, Hsa, has been shown to play a critical role in colonization of S. gordonii on the heart tissue; however, its role in oral biofilm development has not been reported. In this study we demonstrate that Hsa is essential for coaggregation between S. gordonii and Veillonella sp., which are bridging species connecting the pioneer colonizers to the late colonizers. Interestingly, the same domains shown to be required for Hsa binding to sialic acid on the human cell surface are also required for coaggregation with Veillonella sp. However, sialic acid appeared not to be required for this intergeneric coaggregation. This result suggests that although the same domains of Hsa are involved in binding to eukaryotic as well as Veillonella cells, the binding mechanism is different. The gene expression pattern of hsa was also studied and shown not to be induced by coaggregation with Veillonella sp.
authors.affiliation: Department of Microbiology and Immunology, College of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, United States of America.
authors.forename: Peng
authors.initials: P
authors.lastname: Zhou
authors.affiliation: Department of Microbiology and Immunology, College of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, United States of America.
authors.forename: Jinman
authors.initials: J
authors.lastname: Liu
authors.affiliation: Department of Microbiology and Immunology, College of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, United States of America.
authors.forename: Xiaoli
authors.initials: X
authors.lastname: Li
authors.affiliation: Department of Microbiology, School of Life Dentistry at Tokyo, Nippon Dental University, 1-9-20 Fujimi, Chiyoda-ku, Tokyo 102-8159, Japan.
authors.forename: Yukihiro
authors.initials: Y
authors.lastname: Takahashi
authors.affiliation: Department of Microbiology and Immunology, College of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, United States of America.|Department of Oral Biology, College of Dentistry, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, United States of America.
authors.forename: Fengxia
authors.initials: F
authors.lastname: Qi
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001422:Bacterial Adhesion; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D015964:Gene Expression Regulation, Bacterial; D017930:Genes, Reporter; D006389:Hemagglutinins, Viral; D009154:Mutation; D019158:N-Acetylneuraminic Acid / Q000378:metabolism; D054730:Protein Interaction Domains and Motifs; D054773:Streptococcus gordonii / Q000502:physiology*; D014678:Veillonella / Q000502:physiology*
chemical_list: D018829:Adhesins, Bacterial; D002352:Carrier Proteins; D006389:Hemagglutinins, Viral; C450840:hsa protein, Streptococcus gordonii; D019158:N-Acetylneuraminic Acid