Isolation and characterization of mutants of Streptococcus mutans using selective removal of wild-type cells by agglutination with an agglutinin from Persea americana.

R. Curtiss, C. Pearce, J. Pollack, H. M. Murchison

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Persea americana agglutinin (PAA), a substance known to bind basic proteins and inhibit the sucrose-independent adherence of Streptococcus mutants to saliva = coated hydroxyapatite (Staat et al., 1980) was used to selectively enrich for mutants defective in a variety of cell surface associated virulence characteristics from cultures UAB62 (PS14 Riff, serotype c), UAB66 (6715 Strr Spcr, serotype g) and UAB77 (GS5, serotype c). Following mutagenesis and growth for segregation and phenotypic expression, washed cells of each strain were exposed to PAA overnight at 37 degrees C. Aggregated cells were removed by low-speed centrifugation and cells remaining in the supernatant fluids were concentrated, grown to stationary phase and the enrichment with PAA repeated. Mutants isolated following enrichment were phenotypically diverse and included strains defective in one or more of the following characteristics: adherence to glass in a sucrose-containing medium, aggregation with sucrose, dextran or PAA. dextranase production, colony morphology, cell or chain morphology, fermentation of sorbitol, lactose, galactose, raffinose, melibiose, or fructose, and production of surface protein antigen A (SpaA). The diversity of mutant phenotypes identified along with the observation that PAA could still cause aggregation (with a lower efficiency) of all mutants leads us to infer that the interaction of this agglutinin with proteins on the S. mutans cell surface is relatively nonspecific and that the observed inhibition of S. mutants attachment to saliva-coated hydroxyapatite caused by PAA is not due to a highly specific unique interaction of PAA with the protein(s) responsible for sucrose-independent adherence.

Original languageEnglish (US)
Pages (from-to)3-15
Number of pages13
JournalActa Microbiologica Polonica
Volume36
Issue number1-2
StatePublished - 1987
Externally publishedYes

Fingerprint

Persea
Streptococcus mutans
Agglutinins
Agglutination
Sucrose
Durapatite
Saliva
Dextranase
Melibiose
Raffinose
Sorbitol
Protein S
Lactose
Surface Antigens
Dextrans
Streptococcus
Fructose
Galactose
Centrifugation
Mutagenesis

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology

Cite this

Isolation and characterization of mutants of Streptococcus mutans using selective removal of wild-type cells by agglutination with an agglutinin from Persea americana. / Curtiss, R.; Pearce, C.; Pollack, J.; Murchison, H. M.

In: Acta Microbiologica Polonica, Vol. 36, No. 1-2, 1987, p. 3-15.

Research output: Contribution to journalArticle

@article{03d476033fa342a8996fb3320ed2f53d,
title = "Isolation and characterization of mutants of Streptococcus mutans using selective removal of wild-type cells by agglutination with an agglutinin from Persea americana.",
abstract = "Persea americana agglutinin (PAA), a substance known to bind basic proteins and inhibit the sucrose-independent adherence of Streptococcus mutants to saliva = coated hydroxyapatite (Staat et al., 1980) was used to selectively enrich for mutants defective in a variety of cell surface associated virulence characteristics from cultures UAB62 (PS14 Riff, serotype c), UAB66 (6715 Strr Spcr, serotype g) and UAB77 (GS5, serotype c). Following mutagenesis and growth for segregation and phenotypic expression, washed cells of each strain were exposed to PAA overnight at 37 degrees C. Aggregated cells were removed by low-speed centrifugation and cells remaining in the supernatant fluids were concentrated, grown to stationary phase and the enrichment with PAA repeated. Mutants isolated following enrichment were phenotypically diverse and included strains defective in one or more of the following characteristics: adherence to glass in a sucrose-containing medium, aggregation with sucrose, dextran or PAA. dextranase production, colony morphology, cell or chain morphology, fermentation of sorbitol, lactose, galactose, raffinose, melibiose, or fructose, and production of surface protein antigen A (SpaA). The diversity of mutant phenotypes identified along with the observation that PAA could still cause aggregation (with a lower efficiency) of all mutants leads us to infer that the interaction of this agglutinin with proteins on the S. mutans cell surface is relatively nonspecific and that the observed inhibition of S. mutants attachment to saliva-coated hydroxyapatite caused by PAA is not due to a highly specific unique interaction of PAA with the protein(s) responsible for sucrose-independent adherence.",
author = "R. Curtiss and C. Pearce and J. Pollack and Murchison, {H. M.}",
year = "1987",
language = "English (US)",
volume = "36",
pages = "3--15",
journal = "Polish Journal of Microbiology",
issn = "1733-1331",
publisher = "Polish Society of Microbiologists",
number = "1-2",

}

TY - JOUR

T1 - Isolation and characterization of mutants of Streptococcus mutans using selective removal of wild-type cells by agglutination with an agglutinin from Persea americana.

AU - Curtiss, R.

AU - Pearce, C.

AU - Pollack, J.

AU - Murchison, H. M.

PY - 1987

Y1 - 1987

N2 - Persea americana agglutinin (PAA), a substance known to bind basic proteins and inhibit the sucrose-independent adherence of Streptococcus mutants to saliva = coated hydroxyapatite (Staat et al., 1980) was used to selectively enrich for mutants defective in a variety of cell surface associated virulence characteristics from cultures UAB62 (PS14 Riff, serotype c), UAB66 (6715 Strr Spcr, serotype g) and UAB77 (GS5, serotype c). Following mutagenesis and growth for segregation and phenotypic expression, washed cells of each strain were exposed to PAA overnight at 37 degrees C. Aggregated cells were removed by low-speed centrifugation and cells remaining in the supernatant fluids were concentrated, grown to stationary phase and the enrichment with PAA repeated. Mutants isolated following enrichment were phenotypically diverse and included strains defective in one or more of the following characteristics: adherence to glass in a sucrose-containing medium, aggregation with sucrose, dextran or PAA. dextranase production, colony morphology, cell or chain morphology, fermentation of sorbitol, lactose, galactose, raffinose, melibiose, or fructose, and production of surface protein antigen A (SpaA). The diversity of mutant phenotypes identified along with the observation that PAA could still cause aggregation (with a lower efficiency) of all mutants leads us to infer that the interaction of this agglutinin with proteins on the S. mutans cell surface is relatively nonspecific and that the observed inhibition of S. mutants attachment to saliva-coated hydroxyapatite caused by PAA is not due to a highly specific unique interaction of PAA with the protein(s) responsible for sucrose-independent adherence.

AB - Persea americana agglutinin (PAA), a substance known to bind basic proteins and inhibit the sucrose-independent adherence of Streptococcus mutants to saliva = coated hydroxyapatite (Staat et al., 1980) was used to selectively enrich for mutants defective in a variety of cell surface associated virulence characteristics from cultures UAB62 (PS14 Riff, serotype c), UAB66 (6715 Strr Spcr, serotype g) and UAB77 (GS5, serotype c). Following mutagenesis and growth for segregation and phenotypic expression, washed cells of each strain were exposed to PAA overnight at 37 degrees C. Aggregated cells were removed by low-speed centrifugation and cells remaining in the supernatant fluids were concentrated, grown to stationary phase and the enrichment with PAA repeated. Mutants isolated following enrichment were phenotypically diverse and included strains defective in one or more of the following characteristics: adherence to glass in a sucrose-containing medium, aggregation with sucrose, dextran or PAA. dextranase production, colony morphology, cell or chain morphology, fermentation of sorbitol, lactose, galactose, raffinose, melibiose, or fructose, and production of surface protein antigen A (SpaA). The diversity of mutant phenotypes identified along with the observation that PAA could still cause aggregation (with a lower efficiency) of all mutants leads us to infer that the interaction of this agglutinin with proteins on the S. mutans cell surface is relatively nonspecific and that the observed inhibition of S. mutants attachment to saliva-coated hydroxyapatite caused by PAA is not due to a highly specific unique interaction of PAA with the protein(s) responsible for sucrose-independent adherence.

UR - http://www.scopus.com/inward/record.url?scp=0023074330&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023074330&partnerID=8YFLogxK

M3 - Article

C2 - 2442971

AN - SCOPUS:0023074330

VL - 36

SP - 3

EP - 15

JO - Polish Journal of Microbiology

JF - Polish Journal of Microbiology

SN - 1733-1331

IS - 1-2

ER -