MG2 and Lactoferrin Form a Heterotypic Complex in Salivary Secretions

Soares, Rodrigo Villamarim; Siqueira, Camille C.; Bruno, Lucila S; Oppenheim, Frank G.; Offner, Gwynneth D.; Troxler, Robert F.

doi:10.1177/154405910308200613

Cited by 36 publications

(31 citation statements)

References 30 publications

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“…Furthermore, effects on the cohesiveness and thickness of the salivary film by electrostatic interactions with anionic pellicle proteins may also be anticipated. The formation of complexes between cationic salivary proteins and the large anionic mucins have been reported in several studies [16][17][18].…”

Section: Introductionmentioning

confidence: 88%

“…Considering the 3D crystalline structure of lactoferrin obtained by X-ray diffraction (56Å × 95Å × 152Å, see Table 1), amounts corresponding to a bilayer was adsorbed at the highest concentrations on Table 2). Table 2 Mean adsorbed amounts after 120 min of adsorption, after PBS rinse, and after addition of 17 hydrophilic substrates, whereas on hydrophobized surfaces the adsorbed amount was in the range of an end-on monolayer (Table 2). However, the dimensions obtained by Small Angle Neutron Scattering (SANS; 47Å × 47Å × 190Å, Table 1) indicated that a mixed monolayer composed of both side-on and end-on adsorbed molecules, or possibly a tilted end-on layer, was formed at the higher concentrations on both types of surfaces.…”

Section: Adsorbed Amountsmentioning

confidence: 99%

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Adsorption behaviour and surfactant elution of cationic salivary proteins at solid/liquid interfaces, studied by in situ ellipsometry

Svendsen

Lindh

Arnebrant

2006

Colloids and Surfaces B: Biointerfaces

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Adsorption of the cationic salivary proteins lactoferrin, lactoperoxidase, lysozyme and histatin 5 to pure (hydrophilic) and methylated (hydrophobized) silica surfaces was investigated by in situ ellipsometry. Effects of concentration (≤10 g ml −1 , for lysozyme ≤200 g ml −1 ) and dependence of surface wettability, as well as adsorption kinetics and elutability of adsorbed films by buffer and sodium dodecyl sulphate (SDS) solutions were investigated. Results showed that the amounts adsorbed decreased in the order lactoferrin ≥ lactoperoxidase > lysozyme ≥ histatin 5. On hydrophilic silica, the adsorption was most likely driven by electrostatic interactions, which resulted in adsorbed amounts of lactoferrin that indicated the formation of a monolayer with both side-on and end-on adsorbed molecules. For lactoperoxidase the adsorbed amounts were somewhat higher than an end-on monolayer, lysozyme adsorption showed amounts corresponding to a side-on monolayer, and histatin 5 displayed adsorbed amounts in the range of a side-on monolayer. On hydrophobized substrata, the adsorption was also mediated by hydrophobic interactions, which resulted in lower adsorbed amounts of lactoferrin and lactoperoxidase; closer to side-on monolayer coverage. For both lysozyme and histatin 5 the adsorbed amounts were the same as on the hydrophilic silica. The investigated proteins exhibited fast adsorption kinetics, and the initial kinetics indicated mass transport controlled behaviour at low concentrations on both types of substrates. Buffer rinsing and SDS elution indicated that the proteins in general were more tightly bound to the hydrophobized surface compared to hydrophilic silica. Overall, the surface activity of the investigated proteins implicates their importance in the salivary film formation.

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Section: Introductionmentioning

confidence: 88%

Section: Adsorbed Amountsmentioning

confidence: 99%

Adsorption behaviour and surfactant elution of cationic salivary proteins at solid/liquid interfaces, studied by in situ ellipsometry

Svendsen

Lindh

Arnebrant

2006

Colloids and Surfaces B: Biointerfaces

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“…Salivary mucin MG2 is a 180-kDa glycoprotein (22). Mucin MG2 binds to several oral microbes, including S. mutans, Actinobacillus actinomycetemcomitans, and Candida albicans, and forms heterotypic complexes with salivary proteins, including secretory immunoglobulin A (SIgA) and lactoferrin (4,15,18,19,29).Enolase is a 47-kDa cytoplasmic enzyme in the glycolytic pathway (21). There are three distinct isoforms (␣, ␤, and ␥) of enolase, each with the same molecular mass.…”

mentioning

confidence: 99%

Streptococcus mutans Surface α-Enolase Binds Salivary Mucin MG2 and Human Plasminogen

Ge¹,

Catt

Gregory

2004

Infect Immun

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Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis identified enolase as a cell surface component of Streptococcus mutans, which was confirmed by enzyme-linked immunosorbent assay, Western blotting, and transmission electron microscopy. Surface enolase was demonstrated to bind to human plasminogen and salivary mucin MG2. The results suggested a role for enolase in S. mutans attachment, clearance, or breach of the bloodstream barrier.Streptococcus mutans is an alpha-hemolytic and nongroupable streptococcus, which causes dental caries and occasionally bacterial endocarditis (BE) (20). Some surface proteins of S. mutans are virulence factors with functions critical to viability, such as adhesion (2). Adhesion is one of the most important steps in the pathogenicity of microorganisms, and bacterial cell surface-mediated interactions with salivary proteins may be the first step in S. mutans attachment to a tooth surface coated with salivary pellicle or saliva-coated plaque (11). Liu et al. reported that S. mutans binds to salivary mucins, but the specific molecule responsible for this binding was unknown (18). Salivary mucin MG2 is a 180-kDa glycoprotein (22). Mucin MG2 binds to several oral microbes, including S. mutans, Actinobacillus actinomycetemcomitans, and Candida albicans, and forms heterotypic complexes with salivary proteins, including secretory immunoglobulin A (SIgA) and lactoferrin (4,15,18,19,29).Enolase is a 47-kDa cytoplasmic enzyme in the glycolytic pathway (21). There are three distinct isoforms (␣, ␤, and ␥) of enolase, each with the same molecular mass. ␣-Enolase is the isoform typically found in bacteria. Surface ␣-enolase has been recently identified on Streptococcus pyogenes, Streptococcus agalactiae, Streptococcus pneumonia, Streptococcus oralis, and A. actinomycetemcomitans (3,13,16,25,32). Surface enolase of S. pyogenes binds and activates human plasminogen, a molecule which plays a crucial role in fibrinolysis, homeostasis, and the degradation of extracellular matrix (8). Proteins, such as enolase, with exposed carboxyl-terminal lysines on the cell surface can bind and promote plasminogen activation (33).In the present study, we identified ␣-enolase from a cell surface protein preparation of S. mutans A32-2 by two-dimensional polyacrylamide gel electrophoresis (PAGE) and matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) analysis. The results of enzyme-linked immunosorbent assay (ELISA), Western blot, and transmission electron microscopy (TEM) confirmed ␣-enolase on the cell surface as well as in the cytoplasm of S. mutans. Results of Western blot, TEM, and ELISA experiments demonstrate that S. mutans surface enolase binds to human plasminogen and human salivary mucin MG2.S. mutans A32-2 was isolated from a highly-caries-active patient and expresses significantly more surface proteins than isolates from caries-free subjects (26). Surface protein, cell wall, and cytoplasmic samples were purified according to methods ...

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“…Parotid saliva is a serous fluid whose protein diffuses homogeneously. On the contrary, submandibular/sublingual saliva and whole saliva exhibit viscoelastic properties that have been related to the presence of the MG1 and MG2 mucins and to intermolecular interactions between them and with other salivary macromolecules (29,30). Both salivary subtypes display a biphasic mode of diffusion (25).…”

Section: Discussionmentioning

confidence: 99%

Molecular Alterations of Parotid Saliva in Infantile Chronic Recurrent Parotitis

et al. 2007

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Infantile chronic recurrent parotitis (ICRP) is an insidious disease whose etiopathogenesis remains an enigma. Alterations in the physical appearance of parotid saliva from ICRP patients have been frequently reported. However, sialochemical studies in regard to ICRP are very rare. The aim of this study was to determine whether saliva of ICRP patients presents major physicochemical and biochemical alterations compared with saliva from paired healthy controls. Parotid, whole, and submandibular/sublingual saliva was collected at an asymptomatic stage from 33 ICRP patients (5-16 y old, both sexes) and from 33 sex-and age-matched healthy controls. Saliva was analyzed for protein concentration, mode of protein diffusion on cellulose membranes, unidimensional sodium dodecylsulfate (SDS)-polyacrylamide gel electrophoresis protein profiles and zymographic profiles of metalloproteinase 2 (MMP-2) and metalloproteinase 9 (MMP-9). Parotid saliva of ICRP patients showed an increased protein concentration, altered mode of protein diffusion, a higher frequency of polypeptide bands of 43, 37,33,29,26,16, and 10 kD, higher asymmetry in the polypeptide profiles of both contralateral parotid saliva, and an increase in the frequency of MMP-2 and MMP-9. Parotid saliva of patients with ICRP is molecularly altered with respect to normal saliva. Some of the molecular differences could be related to the etiopathogenesis of the disease. ICRP is an inflammatory disease associated with nonobstructive glandular sialectasia. It is characterized by recurrent episodes of swelling of one or both parotid glands that alternate with remission intervals lasting for weeks or months in which glands are clinically asymptomatic (1,2). The onset of the disease usually occurs around age 3 y. Symptoms may diminish and disappear spontaneously after puberty. Sometimes the disease may persist until adulthood (1-3).Among the postulated etiological factors of ICRP are congenital ductal malformations, genetic factors, allergies, bacterial infections, local manifestations of autoimmune disease, and immunodeficiencies (1,2,4 -9). However, none of them has been demonstrated to play a causative role in the disease, and to date its etiopathogenesis remains an enigma.Likewise, consensus on the therapeutic management of ICRP has yet to be achieved. Different specialists have opted for different therapies. Among the therapeutic indications described in the specialized literature is a diversity of physical maneuvers to stimulate the salivary flux (1) and pharmacotherapy with nonsteroid anti-inflammatory agents (7) in combination with sialogogues and/or antibiotics (3,6,10). Recently, Nahlieli et al. (11) proposed an interventional approach using a sialendoscope. In cases in which irreversible damage has occurred, ligation of the excretory duct is indicated to produce glandular atrophy (1,2). In severe cases, partial or total parotidectomy is prescribed as a last resource (1,2,12).Studies on glandular tissue obtained from patients with ICRP have shown lymphocyt...

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MG2 and Lactoferrin Form a Heterotypic Complex in Salivary Secretions

Cited by 36 publications

References 30 publications

Adsorption behaviour and surfactant elution of cationic salivary proteins at solid/liquid interfaces, studied by in situ ellipsometry

Adsorption behaviour and surfactant elution of cationic salivary proteins at solid/liquid interfaces, studied by in situ ellipsometry

Streptococcus mutans Surface α-Enolase Binds Salivary Mucin MG2 and Human Plasminogen

Molecular Alterations of Parotid Saliva in Infantile Chronic Recurrent Parotitis

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