Adhesive properties of strains of Fusobacterium nucleatum of the subspecies nucleatum, vincentii and polymorphum.
This study surveyed some adhesive properties of strains of Fusobacterium nucleatum representative of the 3 recently defined groups or subspecies that could relate to their colonization and virulence. With one exception, F. nucleatum strains agglutinated sheep erythrocytes, but the quantity of bacteria required and the sensitivity of the hemagglutination reactions to inhibition by 0.05 M galactose or arginine varied between strains, and did not exhibit clear-cut correlations with subspecies. Neuraminidase treatment of erythrocytes generally enhanced the hemagglutinating activity of most strains, but trypsin treatment had no effect. Strains of F. nucleatum also attached in moderate numbers to buccal epithelial cells. Treatment of the epithelial cells with neuraminidase or with trypsin increased the numbers of all Fusobacterium strains that attached. Treatment of hydroxyapatite (HA) beads with submandibular or parotid saliva also promoted the adhesion of all strains of F. nucleatum studied. Treatment of HA with human serum or albumin produced a selective effect. Adhesion of some strains was promoted by serum and albumin treatment, and that of other strains was unaffected. Adhesion of all strains of F. nucleatum was enhanced to statherin-treated HA, whereas HA treated with salivary proline-rich protein-1 did not foster F. nucleatum attachment. Three of 4 strains of the subspecies vincentii, and each of 2 polymorphum strains studied exhibited strong adhesion to HA treated with either human type I or type IV collagen. However, only 1 of 5 strains of the subspecies nucleatum bound well to collagen-treated HA.(ABSTRACT TRUNCATED AT 250 WORDS)
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Forsyth Dental Center, Boston, Massachusetts.
Gibbons
R J
RJ
Hay
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D000328:Adult; D001422:Bacterial Adhesion; D003094:Collagen / Q000502:physiology; D016967:Fusobacterium nucleatum / Q000502:physiology*; D006384:Hemagglutination; D006801:Humans; D006882:Hydroxyapatites; D009439:Neuraminidase / Q000378:metabolism; D010455:Peptides / Q000502:physiology; D055232:Proline-Rich Protein Domains; D012463:Saliva / Q000382:microbiology; D012471:Salivary Proteins and Peptides / Q000502:physiology; D013045:Species Specificity; D014357:Trypsin / Q000378:metabolism
D006882:Hydroxyapatites; D010455:Peptides; C018149:STATH protein, human; D012471:Salivary Proteins and Peptides; D003094:Collagen; D009439:Neuraminidase; D014357:Trypsin