Characterization of tufted streptococci isolated from the "corn cob" configuration of human dental plaque

Mouton, Christian; Reynolds, Homer S.; Genco, Robert J.

doi:10.1128/iai.27.1.235-245.1980

Cited by 52 publications

(32 citation statements)

References 21 publications

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“…However, the exquisite specificity of the three inhibition reactions with F tiucleatwn strains ATCC 10953, FDC 364 and B. matruchotii ptovides convincing evidence that LTA plays an itnportant role either directly or indirectly in corncob formation. Mouton and co-workers (27,28) have shown, by immunofluorescence, that LTA is exposed on the surface at one polar end of corncob-forming isolates of S. sanguis . Coincidently, we have previously shown that 5. sanguis CC5A binds to the fusobacteria through tufts of fimbriae that appear to be located on one polar end of the bacterium (21).…”

Section: Discussionmentioning

confidence: 99%

“…Although piliation of F nucleatum did not appear to be an important factor in corncob formation, previously published electron microscopy data suggested that the binding of F. nucleatum to S. sanguis CC5A was mediated by localized polar fimbriae found on the surface of the streptococci (21), These polar fimbrial tufts were exceedingly resistant to physical and chemical disruption methods. Since Mouton and coworkers (27,28) showed, by immunofluorescent labelling of ititact cells, that the fimbrial tufts contained LTA, extraction with hot phenol-water might provide one method for disrupting the fimbriae. When these extracts were tested for the ability to inhibit corncob antiCC5A PW D4C3C4AI Fig.…”

Section: Inhibition Of Corncob Formation With Iipoteichoic Acid (Lta)mentioning

confidence: 99%

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Evidence for the existence of two classes of corncob (coaggregation) receptor in Fusobacterium nucleatum

Kaufman

DiRienzo

1988

Oral Microbiology and Immunology

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Oral isolates of Fusobacterium nucleatum have the ability to form distinct coaggregation units, termed corncobs, when mixed with Streptococcus sanguis. Saturation binding kinetics determined for 12 strains of F. nucleatum revealed that these strains could be divided into two groups. One group, represented by F. nucleatum ATCC 10953 reproducibly bound twice as many streptococci as the other group, exemplified by F. nucleatum FDC 364. Other Fusobacterium species tested, including F. mortiferum, Fusobacterium periodonticum, Fusobacterium simiae and Fusobacterium necrophporum, failed to form corncobs with S. sanguis. In inhibition experiments lipoteichoic acid (LTA)‐enriched cell extracts from S. sanguis blocked corncob formation between this bacterium and strain FDC 364 with material containing as little as 50 ng phosphate exhibiting greater than 50% inhibition. Alternatively, 40 times as much material failed to inhibit corncob formation between S. sanguis and F. nucleatum ATCC 10953 or Bacterionema matruchotti. Deacylation of the LTA destroyed its ability to inhibit the fusobacterial coaggregation but produced an active inhibitor in the case of B. matruchotii corncobs. Concerning the fusobacterial coaggregation partner, membrane fractions obtained from strain ATCC 10953 blocked corncob formation while the inhibitory activity of strain FDC 364 was confined to the soluble protein fraction. Corncob‐deficient mutants of F. nucleatum FDC 364 were produced by treating the cells with acridine orange. However, this agent had no effect on the corncob‐forming ability of strain ATCC 10953. The results of these experiments provide convincing evidence that at least 2 independent strain‐specific receptors on F. nucleatum are involved in corncob formation between this bacterium and S. sanguis.

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Section: Discussionmentioning

confidence: 99%

Section: Inhibition Of Corncob Formation With Iipoteichoic Acid (Lta)mentioning

confidence: 99%

Evidence for the existence of two classes of corncob (coaggregation) receptor in Fusobacterium nucleatum

Kaufman

DiRienzo

1988

Oral Microbiology and Immunology

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“…no ABAAS AND HOLME It has also been shown in vitro that oral actinomycetes coaggregate with a high degree of specificity with certain species of oral streptococci (3,4,25,27). Both protein or glycoprotein and carbohydrate receptors were shown to be involved in the binding of the cells (3).…”

mentioning

confidence: 98%

“…The mechanisms of homot>'pic aod heterotypic aggregation are not yet clarified. Fibriliar structures have been ascribed some significance in streptococci similar to S, mitis ATCC 903 (27), and in Actinomyces viscosus (25). In the binding of oral streptococci to Actinomyces species, several mechanisms have been suggested.…”

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confidence: 99%

Development of aggregating ability in cells of Streptococcus mitis ATCC 903 grown under glucose‐limiting conditions in continuous culture

Abaas

Holme

1982

European J Oral Sciences

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– Streptococcus mitis ATCC903 grown under glucose‐limiting conditions in continuous culture did not aggregate upon incubation in 10mM phosphate buffer at pH 5–7 unless a metabolizable sugar was added. aggregation started 45–50 min after the addition of glucose or sucrose whereas slowly metabolized sugars as gadlactose and lactose required several hours to cause aggregation. Active metabolism of the carbohydrate was a prerequisite for aggregation as indicated by acid formation. Chloramphenicol inhibited the development of aggregating ability in the presence of glucose or sucrose. The addition of a source of nitrogen (peptides and amino acids) enhanced aggregation and shortened the time for development of aggregating ability. No aggregation occurred at 0°C and the ability to aggregate was markedly delayed at 20°C as compared to 30°C. Trypsin treatment of the bacteria abolished aggregation, indicating that surface components of protein or glycoprotein nature contributed to the capacity to aggregate.

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“…Eibrils are short (<70 nrn), have no definite width, and can clump together, whereas fimbriae are longer (< 1.0 /um), do not clump, and have a definite width (3-4 nrn) (9). The strains with tufts of fibrils are able to coaggregate speeifieally with Bacterionema matruchotii to form 'eorncobs' in mature plaque (14,17), and in vitro (9). The peritriehously fibrillar 5.…”

mentioning

confidence: 99%

Fibrillar strains of Streptococcus sanguis biotype I carry a surface protein which cross‐reacts with Antigen B from Streptococcus mutans Ingbritt

Wyatt

Willcox

Russell

et al. 1988

Oral Microbiology and Immunology

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Eleven strains of Streptococcus sanguis biotype I carrying peritrichous fibrils and 4 strains with lateral tufts of fibrils were screened for crossreactivity with Antigen B (AgB), a protein with a molecular weight of 190,000, isolated from Streptococcus mutans Ingbritt. An antigen of similar molecular weight, which cross‐reacted serologically with AgB was detected by immunodiffusion, Western blotting and dot immuno‐binding in strains of S. sanguis biotype I with peritrichous fibrils but not in tufted strains. One strain, S. sanguis LGR2 carried dense fibrils (5+ density) and the gold label appeared to be associated with the fibrils. However, over all the strains there was no correlation between the density of fibrils and the amount of AgB labelling. Immunonegative staining confirmed the absence of AgB cross reactivity in the tufted strains of S. sanguis I, although the gold labelled the tuft fibrils non‐specifically. Antigen B was located on the cell surface of S. mutans Ingbritt and the label extended 45.9±9.9 nm from the cell wall although the strain was non‐fibrillar.

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Characterization of tufted streptococci isolated from the "corn cob" configuration of human dental plaque

Cited by 52 publications

References 21 publications

Evidence for the existence of two classes of corncob (coaggregation) receptor in Fusobacterium nucleatum

Evidence for the existence of two classes of corncob (coaggregation) receptor in Fusobacterium nucleatum

Development of aggregating ability in cells of Streptococcus mitis ATCC 903 grown under glucose‐limiting conditions in continuous culture

Fibrillar strains of Streptococcus sanguis biotype I carry a surface protein which cross‐reacts with Antigen B from Streptococcus mutans Ingbritt

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