1993
DOI: 10.1177/00220345930720120501
|View full text |Cite
|
Sign up to set email alerts
|

Interaction of the Salivary Glycoprotein EP-GP with the Bacterium Streptococcus salivarius HB

Abstract: The interaction of the human salivary glycoprotein EP-GP with a number of oral bacterial species, following incubation with human whole saliva, has been investigated. EP-GP could be detected with a specific monoclonal antibody, by means of ELISA or by electrophoresis in combination with Western Transfer. The results indicated that EP-GP is bound only by Streptococcus salivarius, and not by the other tested strains of bacteria, Actinomyces viscosus, A. naeslundii, Actinobacillus actinomycetemcomitans, Bacteroid… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
18
0

Year Published

1994
1994
2018
2018

Publication Types

Select...
8

Relationship

0
8

Authors

Journals

citations
Cited by 30 publications
(18 citation statements)
references
References 20 publications
0
18
0
Order By: Relevance
“…We can conclude that the latter is most likely because S. mutans attachment and biofilm formation in the presence of MUC5B are significantly decreased at most time points compared to the levels in the presence of methylcellulose. There are at least three potential mechanisms by which MUC5B could protect the surface from bacterial colonization: (i) MUC5B could bind or agglutinate bacteria, which would allow planktonic bacteria to be swept out of the oral cavity with salivary flow but enhance bacterial attachment to surfaces coated with MUC5B (14,25,(37)(38)(39)(40)(41)(42)(43)(44), (ii) MUC5B could have the opposite effect, where its heterogeneous glycan chains repel bacteria, thereby preventing surface attachment (9,11,(45)(46)(47), or (iii) MUC5B could directly downregulate S. mutans genes involved in attachment and biofilm formation. In our case, it appears that MUC5B is repelling S. mutans and/or directly influencing genetic modifications that protect the glass and hydroxyapatite surfaces from bacterial attachment and biofilm formation.…”
Section: Sucrose Enhances S Mutans Attachment and Biofilm Formationmentioning
confidence: 99%
“…We can conclude that the latter is most likely because S. mutans attachment and biofilm formation in the presence of MUC5B are significantly decreased at most time points compared to the levels in the presence of methylcellulose. There are at least three potential mechanisms by which MUC5B could protect the surface from bacterial colonization: (i) MUC5B could bind or agglutinate bacteria, which would allow planktonic bacteria to be swept out of the oral cavity with salivary flow but enhance bacterial attachment to surfaces coated with MUC5B (14,25,(37)(38)(39)(40)(41)(42)(43)(44), (ii) MUC5B could have the opposite effect, where its heterogeneous glycan chains repel bacteria, thereby preventing surface attachment (9,11,(45)(46)(47), or (iii) MUC5B could directly downregulate S. mutans genes involved in attachment and biofilm formation. In our case, it appears that MUC5B is repelling S. mutans and/or directly influencing genetic modifications that protect the glass and hydroxyapatite surfaces from bacterial attachment and biofilm formation.…”
Section: Sucrose Enhances S Mutans Attachment and Biofilm Formationmentioning
confidence: 99%
“…Although MG2 seems to bind to a wide variety of bacteria suspended in saliva (Biesbrock et al, 1991;Brack et al, 1987;Gibbons et al, 1978;Hogg et al, 1979;Levine et al, 1978;Scannapieco et al, 1987;Schenkels et al, 1993), highly purified MG2 does not bind directly to these same bacteria (Biesbrock et al, 1991). Mucins appear to lose the ability to interact with bacteria as a result of the purification process.…”
Section: Mucinsmentioning
confidence: 99%
“…While as yet not described as an agglutinin, EP-GP (extra-parotid glycoprotein) has been found to bind to strains of Streptococcus salivarius (Schenkels et al, 1993). EP-GP is a 19 to 20-kDa glycoprotein secreted by submandibular salivary glands (Rathman et al, 1990).…”
Section: Other Agglutininsmentioning
confidence: 99%
“…Another interesting function of salivary lipocalins is that the proteins have an affinity for actin-binding proteins (79,82). VEG protein specifically binds to Streptococcus salivarius, just as lipocalin inhibits the growth of S. salivarius (83). VEG protein inhibits papain activity to a similar extent as do s a l i v a r y c y s t a t i n s ( 8 4 ) , s u g g e s t i n g t h a t t h e biophysiological activities of VEG protein lipocalins are involved in certain antimicrobial processes in the oral cavity as well as in ocular tissue.…”
Section: Lipocalinsmentioning
confidence: 99%