Interaction of the salivary low-molecular-weight mucin (MG2) with Actinobacillus actinomycetemcomitans

Groenink, J.; Ligtenberg, A.J.M.; Veerman, E.C.I.; Bolscher, Jan G. M.; Amerongen, A. van Nieuw

doi:10.1007/bf00393572

Cited by 54 publications

(48 citation statements)

References 42 publications

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“…These include mucins, which are complex glycoproteins. The mucin interferes with the colonization and aggregation of Aggregatibacter actinomycetemcomitans [14]. Lysozyme, an antimicrobial enzyme, is another nonspecific marker which cleaves the chemical bonds on the bacterial cell resulting in lysis of the microbe.…”

Section: Salivary Biomarkersmentioning

confidence: 99%

Saliva: A Cutting Edge in Diagnostic Procedures

Sindhu

Jagannathan

2014

Journal of Oral Diseases

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The ability to monitor the health and disease status of the patient through saliva is a highly desirable goal for the health professionals. Considering the microconcentration of salivary constituents, saliva is explored to be diagnostic tool as it also meets the demands for an inexpensive, noninvasive and easy to use screening method. The incorporation of salivary diagnostics into clinical practice is gaining reality and will be of diagnostic value in the prospective future. The investigative use of saliva is not being applied only in dental health but also in various other systemic disorders. The advent of molecular techniques is gaining attention and this has triggered its application as a specific and sensitive biomarker in proteomics, genomics, and transcriptomics. This review discusses the basics of salivary diagnostics, expectoration techniques, and its application in various local and systemic disorders.

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Section: Salivary Biomarkersmentioning

confidence: 99%

Saliva: A Cutting Edge in Diagnostic Procedures

Sindhu

Jagannathan

2014

Journal of Oral Diseases

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“…5 It is thought to function in a protective capacity by promoting the clearance of bacteria in the oral cavity and to aid in mastication, speech and swallowing. 19 ± 21 It has been shown to interact with a variety of bacteria, including four strains of streptococci, 21 Actinobacillus actinomycetemcomitans, 22 Staphylococcus aureus and Pseudomonas aeruginosa. 18 MUC7 has been shown to be expressed in the bronchial tree as well as in the salivary glands.…”

Section: Introductionmentioning

confidence: 99%

Genetic polymorphism of MUC7: Allele frequencies and association with asthma

et al. 2001

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MUC7 encodes a small salivary mucin, previously called MG2, a glycoprotein with a putative role in facilitating the clearance of oral bacteria. The central domain of this glycoprotein was previously shown to comprise five or six tandemly repeated units of 23 amino-acids which carry most of the O-linked glycans. The polymorphism of these two allelic forms (MUC7*5 or MUC7*6) has been confirmed in this study in which we have analysed a large cohort of subjects (n = 375) of various ethnic origins. We have also identified a novel rare allele with eight tandem repeats (MUC7*8). MUC7*6 was the most common allele (0.78 ± 0.95) in all the populations tested. The tandem repeat arrays of 22 MUC7*5 alleles and 34 MUC7*6 alleles were sequenced. No sequence differences were detected in any of the MUC7*6 alleles. Twenty-one MUC7*5 alleles sequenced lacked the 4th tandem repeat (structure TR12356), while one showed the structure TR12127. The structure of the MUC7*8 allele was TR12343456. Because of the known role of MUC7 in bacterial binding, and thus its potential involvement in susceptibility to chest disease we also tested MUC7 in our previously described series of Northern European atopic individuals with and without associated asthma. The MUC7*5 allele was rarer in the atopic asthmatics than in the atopic non-asthmatics (P = 0.014, OR for no asthma in atopic individuals 3.13, CI 1.01 ± 6.10), and the difference in frequency between all asthmatics and all non-asthmatics was statistically significant (P = 0.009) while there was no difference between atopy and non-atopy (P = 0.199). In this study we also report the electrophoretic analysis of the MUC7 glycoprotein in saliva from individuals of different MUC7 genotype.

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“…Saliva fulfills the latter function by virtue of its antimicrobial activity (9,10) and by promoting selective microbial clearance or adherence (11)(12)(13)(14). The diverse functions attributed to saliva are allocated among its many components, which include amylases, cystatins, proline-rich proteins, proline-rich glycoproteins, carbonic anhydrases, peroxidases, statherins, histatins, lactoferrin, lysozyme, sIgA, mucins, and salivary agglutinin.…”

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confidence: 99%

Salivary Agglutinin, Which Binds Streptococcus mutansand Helicobacter pylori, Is the Lung Scavenger Receptor Cysteine-rich Protein gp-340

Prakobphol¹,

Xu²,

Hoang³

et al. 2000

Journal of Biological Chemistry

200

220

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Salivary agglutinin is a high molecular mass component of human saliva that binds Streptococcus mutans, an oral bacterium implicated in dental caries. To study its protein sequence, we isolated the agglutinin from human parotid saliva. After trypsin digestion, a portion was analyzed by matrix-assisted laser/desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS), which gave the molecular mass of 14 unique peptides. The remainder of the digest was subjected to high performance liquid chromatography, and the separated peptides were analyzed by MALDI-TOF/post-source decay; the spectra gave the sequences of five peptides. The molecular mass and peptide sequence information showed that salivary agglutinin peptides were identical to sequences in lung (lavage) gp-340, a member of the scavenger receptor cysteine-rich protein family. Immunoblotting with antibodies that specifically recognized either lung gp-340 or the agglutinin confirmed that the salivary agglutinin was gp-340. Immunoblotting with an antibody specific to the sialyl Le x carbohydrate epitope detected expression on the salivary but not the lung glycoprotein, possible evidence of different glycoforms. The salivary agglutinin also interacted with Helicobacter pylori, implicated in gastritis and peptic ulcer disease, Streptococcus agalactiae, implicated in neonatal meningitis, and several oral commensal streptococci. These results identify the salivary agglutinin as gp-340 and suggest it binds bacteria that are important determinants of either the oral ecology or systemic diseases.

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Interaction of the salivary low-molecular-weight mucin (MG2) with Actinobacillus actinomycetemcomitans

Cited by 54 publications

References 42 publications

Saliva: A Cutting Edge in Diagnostic Procedures

Saliva: A Cutting Edge in Diagnostic Procedures

Genetic polymorphism of MUC7: Allele frequencies and association with asthma

Salivary Agglutinin, Which Binds Streptococcus mutansand Helicobacter pylori, Is the Lung Scavenger Receptor Cysteine-rich Protein gp-340

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