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Identification of a molecule of Porphyromonas gingivalis that binds to Streptococcus gordonii
Affiliation:1. Department of Electrical and Computer Engineering, University of Florida, Gainesville, FL 32610, USA;2. Department of Microbiology and Immunology, State University of New York at Buffalo, Buffalo, NY 14201, USA;3. Mayo Clinic, Jacksonville, FL 32216, USA;4. Department of Epidemiology, Emerging Pathogens Institute, University of Florida, Gainesville, FL 32610, USA;5. Department of Computer Science and Engineering, Department of Biostatistics, State University of New York at Buffalo, Buffalo, NY 14201, USA;1. Department of Biotechnology, Delhi Technological University, Bawana Road, Delhi 110 042, India;2. Aqua Research Lab, Department of Zoology, University of Delhi, Delhi 110 007, India;3. Central Institute of Fisheries Education, Rohtak Centre, Lahli, Rohtak, Haryana 124 411, India
Abstract:The molecules that mediate the adherence of Porphyromonas gingivalis, a periodontal pathogen, to Streptococcus gordonii, a commensal plaque organism, were investigated. Outer membrane proteins of P. gingivalis were labelled with biotin, extracted by EDTA and reacted with S. gordonii cells. Interactive porphyromonas components were identified by SDS-PAGE of the S. gordonii cells followed by electroblotting and visualization of the adsorbed porphyromonas molecules with streptavidin-alkaline phosphatase. A P. gingivalis molecule of 35 kDa bound to S. gordonii. Monospecific polyclonal antibodies to the 35 kDa protein inhibited binding of P. gingivalis to S. gordonii by 71%. The antibodies also reacted with the P. gingivalis fimbriae, indicating that the 35 kDa molecule is antigenically related to, or associated with, the fimbriae.
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