Effect of lacto-N-neotetraose, asialoganglioside-GM1 and neuraminidase on adherence of otitis media-associated serotypes ofStreptococcus pneumoniaeto chinchilla tracheal epithelium

Tong, Hua Hua; McIver, Monroe A.; Fisher, Lisa M.; DeMaria, Thomas F.

doi:10.1006/mpat.1998.0257

Cited by 75 publications

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“…The theory has been proven in vitro with a range of bacterial species. For example, lacto-N-neotetraose and asialoganglioside-GM1 (asialo-GM1) inhibit attachment of S. pneumoniae to alveolar epithelial cells (Tong et al, 1999). Similarly 3-sialyllactose inhibits Helicobacter pylori attachment to gastric epithelial cells .…”

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confidence: 99%

Common oligosaccharide moieties inhibit the adherence of typical and atypical respiratory pathogens

Thomas

Brooks

2004

Journal of Medical Microbiology

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Intervention in bacterial adhesion to host cells is a novel method of overcoming current problems associated with antibiotic resistance. Antibiotic-resistant strains of bacteria that cause respiratory tract infections are a problem in hospitals and could be used in bioterrorist attacks. A range of bacterial species was demonstrated to attach to an alveolar epithelial (A549) cell line. In all cases, cell surface oligosaccharides were important in attachment, demonstrated by reduced adhesion when A549 cells were pre-treated with tunicamycin. Bacillus anthracis and Yersinia pestis displayed a restricted tropism for oligosaccharides compared to the environmental, opportunistic pathogens, Pseudomonas aeruginosa, Burkholderia cenocepacia, Burkholderia pseudomallei and Legionella pneumophila. The compound with the greatest anti-adhesion activity was p-nitrophenol. Other generic attachment inhibitors included the polymeric saccharides (dextran and heparin), GalNAcâ1-4Gal, GalNAcâ1-3Gal, Galâ1-4GlcNAc and Galâ1-3GlcNAc. Burkholderia pseudomallei attachment was particularly susceptible to oligosaccharide inhibition. Combinations of such compounds may serve as a novel generic therapeutics for respiratory tract infections. INTRODUCTIONThe development of antibiotic resistance amongst pathogenic bacteria is a frequent occurrence and of great concern for public health. This problem is associated with many bacteria that cause community-and hospital-acquired pneumonia such as Streptococcus pneumoniae, Haemophilus influenzae, Pseudomonas aeruginosa and Burkholderia cenocepacia (Lister, 2000;Lynch, 2001;Spencer, 1995;Tan, 2003). Problems with antibiotic resistance can also extend to those bacteria that could be used in bioterrorism. It is likely that such bacterial threat agents would be delivered by the aerosol route resulting in respiratory presentation of the disease (Cieslak & Eitzen, 2000;Leggiadro, 2000). Given the ease of natural acquisition of antibiotic resistance genes and genetic manipulation, it is prudent to research therapeutic alternatives to antibiotics.Attachment to cell surfaces is one of the key steps in bacterial pathogenesis, often involving oligosaccharides located on the host cell surface and bacterial adhesins (Karlsson et al., 1992;Ofek & Sharon, 1990). The terminal di-or trisaccharide units of these oligosaccharides may be used to inhibit these interactions, preventing attachment and hence disease (Zopf & Roth, 1996). The theory has been proven in vitro with a range of bacterial species. For example, lacto-N-neotetraose and asialoganglioside-GM1 (asialo-GM1) inhibit attachment of S. pneumoniae to alveolar epithelial cells (Tong et al., 1999). Similarly 3-sialyllactose inhibits Helicobacter pylori attachment to gastric epithelial cells . Asialoganglioside-GM1 and -GM2 are used as receptors by a number of respiratory pathogens, which specifically bind their terminal GalNAcâ1-3Gal and GalNAcâ1-4Gal moieties (Krivan et al., 1988a(Krivan et al., , b, 1991. The principle has also been proven to be valid in vivo...

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confidence: 99%

Common oligosaccharide moieties inhibit the adherence of typical and atypical respiratory pathogens

Thomas

Brooks

2004

Journal of Medical Microbiology

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“…The role of neuraminidase in adhesion has been demonstrated recently in the chinchilla respiratory tract ± neuraminidase treatment of the trachea increased pneumococcal adherence and reversed the inhibition produced by prior incubation with glycoconjugate analogues of known pneumococcal receptors. These data suggest that neuraminidase facilitates adhesion by increasing the number of adhesins available for pneumococcal binding [28].…”

Section: Invasionmentioning

confidence: 74%

Pathogenesis of pneumococcal infection

Gillespie

Balakrishnan

2000

Journal of Medical Microbiology

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“…1A). The catalytic domain (Thr-2 to Glu-342) adopts a typical (␤/␣) 8 TIM barrel with some distortions. Following the catalytic domain, a stretch of residues, Ser-337 to Ser-365, containing a short ␤-strand passes through the second ABD (Leu-489 to Lys-591), prior to joining the first ABD (Ser-366 to Pro-488).…”

Section: Resultsmentioning

confidence: 99%

“…Genome sequencing, in combination with exploration of new virulence factors, suggests that a large number of glycosidases are necessary for the full virulence of S. pneumoniae (5,6). For instance, three surface-exposed glycosidases, neuraminidase NanA, ␤-galactosidase BgaA, and N-acetyl-hexosaminidase StrH, have been identified to sequentially hydrolyze the glycoconjugates necessary for the colonization and pathogenesis of S. pneumoniae (7,8). The action of deglycosylation is believed not only to expose the binding sites for further invasion but also to supply an abundant carbon source from the hydrolysis products (9).…”

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“…Some ␤-galactosidases are grouped in the glycosidase families GH-1, GH-2, and GH-42 in addition to GH-35 (12,(17)(18)(19)(20). All of these families belong to a superfamily (or clan) termed GH-A, all members of which possess a catalytic domain of (␣/␤) 8 Table 1). Most of these enzymes possess specific hydrolysis activity toward ␤(1,4)-galactosyl bond, whereas H. sapiens ␤-gal shows hydrolysis activity toward both ␤(1,3)-and ␤(1,4)-galactosyl bonds (31)(32)(33), and the substrate specificity of B. thetaiotaomicron ␤-gal remains unknown.…”

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Structural Insights into the Substrate Specificity of Streptococcus pneumoniae β(1,3)-Galactosidase BgaC

Wang¹,

Wang²,

Jiang

et al. 2012

Journal of Biological Chemistry

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Background:Streptococcus pneumoniae BgaC is a GH-35 ␤-galactosidase of specific activity toward ␤(1,3)-linked galactose and N-acetylglucosamine. Results: Three aromatic residues, Trp-240, Trp-243, and Tyr-455, determine the substrate specificity of BgaC. Conclusion: BgaC and other GH-35 ␤-galactosidases adopt a similar domain organization and catalytic mechanism. Significance: Provided is the first structural insight into the substrate specificity of ␤-galactosidase toward the ␤(1,3)-linked galactosyl bond.

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Effect of lacto-N-neotetraose, asialoganglioside-GM1 and neuraminidase on adherence of otitis media-associated serotypes ofStreptococcus pneumoniaeto chinchilla tracheal epithelium

Cited by 75 publications

References 0 publications

Common oligosaccharide moieties inhibit the adherence of typical and atypical respiratory pathogens

Common oligosaccharide moieties inhibit the adherence of typical and atypical respiratory pathogens

Pathogenesis of pneumococcal infection

Structural Insights into the Substrate Specificity of Streptococcus pneumoniae β(1,3)-Galactosidase BgaC

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