Enzymic activity of salivary amylase when bound to the surface of oral streptococci

Douglas, CW Ian

doi:10.1016/0378-1097(92)90511-l

Cited by 5 publications

(10 citation statements)

References 4 publications

(11 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…(1979) have reported that amylase displays growth-inhibitory activity against Neisseria gonorrhoeae. More recently, specific binding of salivary amylase to S. gordonii has been demonstrated by various investigators (Douglas, 1983;Scannapieco et al, 1989), although this binding appears to be more for the benefit of the guest, rather than for the host (bacterium-bound amylase allows the microbe to utilize starch as a carbohydrate source (Douglas et al, 1992). Studies to elucidate the role of amylase in other secretory fluids (tears, seminal fluid, sweat, bronchial mucus) have not been reported.…”

Section: Oc-amylasementioning

confidence: 99%

Biochemical Composition of Human Saliva in Relation To Other Mucosal Fluids

Schenkels

Veerman

Amerongen

1995

Critical Reviews in Oral Biology & Medicine

319

238

View full text Add to dashboard Cite

This paper describes several salivary components and their distribution in other mucosal secretions. Histatins are polypeptides which possess exceptional anti-fungal and anti-bacterial activities, but are nevertheless present only in saliva. Proline-rich proteins (PRPs) are members of a closely related family, of which the acidic PRPs are found solely in saliva, whereas the basic PRPs are also found in other secretions. Mucins are a group of glycoproteins that contribute to the visco-elastic character of the mucosal secretions. Despite the similarities in their structure and behavior, mucins have distinct tissue distributions and amino acid sequences. Other salivary proteins are present in one or more mucosal secretions. Lysozyme is an example of a component belonging to an ancient self-defense system, whereas secretory immunoglobulin A (sIgA) is the secreted part of a sophisticated adaptive immune system. Cystatins are closely related proteins which belong to a multigene family. Alpha-Amylase is a component that is believed to play a specific role in digestion, but is nevertheless present in several body fluids. Kallikrein and albumin are components of blood plasma. But whereas albumin diffuses into the different mucosal secretions, kallikrein is secreted specifically by the mucosal glands. The presence of these proteins specifically in saliva, or their distribution in other mucosal secretions as well, may provide important clues with respect to the physiology of those proteins in the oral cavity.

show abstract

Section: Oc-amylasementioning

confidence: 99%

Biochemical Composition of Human Saliva in Relation To Other Mucosal Fluids

Schenkels

Veerman

Amerongen

1995

Critical Reviews in Oral Biology & Medicine

319

238

View full text Add to dashboard Cite

show abstract

“…A number of specific interactions between salivary constituents and oral bacteria have been described, including ones which influence adherence of organisms to oral surfaces and other bacteria [1], result in the removal of organisms by direct killing or aggregation [2] and provide nutrients for metabolism [3,4]. One example of the latter is the binding of salivary amylase to the surfaces of certain oral streptococci and, when bound, amylase retains much of its enzymic activity [5][6][7][8]. This provides products of starch degradation for direct metabolism by the organisms and so appears to represent a parasitic mechanism whereby an organism makes use of a host enzyme for its own benefit.…”

Section: Introductionmentioning

confidence: 99%

Comparison of amylase-binding proteins in oral streptococci

Gwynn¹,

Douglas²

1994

FEMS Microbiology Letters

View full text Add to dashboard Cite

Certain species of oral streptococci bind salivary amylase to their cell surface. The patterns of amylase-binding proteins produced by a range of streptococci have been compared by ligand blotting and several characteristics of the binding proteins investigated. Streptococcus gordonii was the most homogeneous species and almost all strains produced proteins migrating with molecular mass 82 kDa and 20 kDa. Other species were more heterogeneous, releasing proteins that resolved at 87 or 82 kDa and/or between 20 and 36 kDa. Binding of amylase to the 82/87-kDa proteins on ligand blots was prevented by amylase inhibitors, amylase substrates and periodate treatment but these had limited or no effect on amylase binding to 20-36 kDa proteins. Also, the 20 kDa protein of S. gordonii Challis was released into culture medium before the 82-kDa protein. These data suggest that there is significant variation in amylase-binding proteins among streptococci and that the high and low molecular mass proteins differ in the way they interact with salivary amylase.

show abstract

“…Streptococcus gordonii is not able to use starch as a nutritional source unless extracellular amylase is present (Douglas, 1990;Scannapieco et al, 1990;. Salivary amylase binds to a specific receptor, AbpA, on the surface of S. gordonii, and retains its activity to degrade starch to provide a source of nutrition for the bacteria (Douglas, 1990;Douglas et al, 1992). The results of this study indicate that expression of the abpA gene is induced by both amylase and starch in the growth medium, whereas the presence of either component alone did not significantly alter expression of abpA.…”

Section: Discussionmentioning

confidence: 99%

“…Salivary a-amylase is an abundant enzyme in saliva and is best known for its ability to degrade starch by hydrolysing 1,4-glycosidic linkages, with subsequent formation of maltose and various linear maltooligosaccharides. Previous studies found that in vitro bound salivary amylase remains active and can be used by S. gordonii for carbohydrate metabolism in the presence of starch (Scannapieco et al, 1990;Douglas et al, 1992). In the absence of host amylase in the milieu, S. gordonii does not readily use starch and grows very poorly with starch as the sole nutrition source (Douglas et al, 1992;.…”

Section: Introductionmentioning

confidence: 99%

“…Previous studies found that in vitro bound salivary amylase remains active and can be used by S. gordonii for carbohydrate metabolism in the presence of starch (Scannapieco et al, 1990;Douglas et al, 1992). In the absence of host amylase in the milieu, S. gordonii does not readily use starch and grows very poorly with starch as the sole nutrition source (Douglas et al, 1992;. Hence, the ability of S. gordonii to bind salivary amylase may be important for growth of this and other amylase-binding streptococcal species.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Effect of starch and amylase on the expression of amylase‐binding protein A in Streptococcus gordonii

Nikitkova

Haase

Scannapieco

2012

Molecular Oral Microbiology

View full text Add to dashboard Cite

Summary Streptococcus gordonii is a common oral commensal bacterial species in tooth biofilm (dental plaque) and specifically binds to salivary amylase through the surface exposed amylase‐binding protein A (AbpA). When S. gordonii cells are pretreated with amylase, amylase bound to AbpA facilitates growth with starch as a primary nutrition source. The goal of this study was to explore possible regulatory effects of starch, starch metabolites and amylase on the expression of S. gordonii AbpA. An amylase ligand‐binding assay was used to assess the expression of AbpA in culture supernatants and on bacterial cells from S. gordonii grown in defined medium supplemented with 1% starch, 0.5 mg ml−1 amylase, with starch and amylase together, or with various linear malto‐oligosaccharides. Transcription of abpA was determined by reverse transcription quantitative polymerase chain reaction. AbpA was not detectable in culture supernatants containing either starch alone or amylase alone. In contrast, the amount of AbpA was notably increased when starch and amylase were both present in the medium. The expression of abpA was significantly increased (P < 0.05) following 40 min of incubation in defined medium supplemented with starch and amylase. Similar results were obtained in the presence of maltose and other short‐chain malto‐oligosacchrides. These results suggest that the products of starch hydrolysis produced from the action of salivary α‐amylase, particularly maltose and maltotriose, up‐regulate AbpA expression in S. gordonii.

show abstract

Enzymic activity of salivary amylase when bound to the surface of oral streptococci

Cited by 5 publications

References 4 publications

Biochemical Composition of Human Saliva in Relation To Other Mucosal Fluids

Biochemical Composition of Human Saliva in Relation To Other Mucosal Fluids

Comparison of amylase-binding proteins in oral streptococci

Effect of starch and amylase on the expression of amylase‐binding protein A in Streptococcus gordonii

Contact Info

Product

Resources

About