Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells.

Åndersson, Bengt; Dahmén, Jan; Frejd, Torbjörn; Leffler, Hakon; Magnusson, Göran; Noori, Ghazi; Edén, C. Svanborg

doi:10.1084/jem.158.2.559

Cited by 237 publications

(151 citation statements)

References 40 publications

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“…Though Selinger and Reed (1979) proposed that the ability of S. pneumoniae to adhere to oropharyngeal cells might not be associated with virulency, Andersson et al (1981), have suggested that adherence of S. pneumoniae to oropharyngeal cells is an important step in the pathogenesis of otitis media, since this organism adhered avidly to pharyngeal cells from otitis media patients in an in vitro assay. They also have suggested that S. pneumoniae binds specifically to glycoconjugate receptors containing the disaccharide GIcNAcfll-~3Galfl (Andersson et al 1983). More recently, they demonstrated inhibition of S. pneumoniae attachment to pharyngeal cells by and nasal cultures human milk (Andersson et al 1986).…”

Section: Discussionmentioning

confidence: 98%

In vitro adherence of Streptococcus pneumoniae to oropharyngeal cells: Enhanced activity and colonization of the upper respiratory tract in patients with recurrent respiratory infections.

Mbaki

Rikitomi

Akiyama

et al. 1989

Tohoku J. Exp. Med.

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Section: Discussionmentioning

confidence: 98%

In vitro adherence of Streptococcus pneumoniae to oropharyngeal cells: Enhanced activity and colonization of the upper respiratory tract in patients with recurrent respiratory infections.

Mbaki

Rikitomi

Akiyama

et al. 1989

Tohoku J. Exp. Med.

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“…Human colostrum and milk inhibit pneumococcal colonization (19), and each contains neolactotetraose and lactotetraose (16,19). Both sugars contain the GlcNAc␤1-3Gal␤ disaccharide, which can inhibit attachment of pneumococci to human pharyngeal cells (20) and may contribute to the ability of breast-feeding to reduce pneumococcal colonization and otitis media (21, †).…”

mentioning

confidence: 99%

Pneumococcal carriage results in ganglioside-mediated olfactory tissue infection

Ginkel

McGhee

Watt

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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Streptococcus pneumoniae cause considerable morbidity and mortality, with persistent neurological sequelae, particularly in young children and the elderly. It is widely assumed that carriage occurs through direct mucosal colonization from the environment whereas meningitis results from invasion from the blood. However, the results of published studies can be interpreted that pneumococci may enter the brain directly from the nasal cavity by axonal transport through olfactory nerves. This hypothesis is based on findings that (i) teichoic acid of the pneumococcal cell wall interact with gangliosides (GLS), (ii) the interaction of GLS with cholera toxin leads to axonal transport through the olfactory nerves into the brain, and (iii) viruses enter the brain through axonal transport into olfactory nerves. After nasal inoculation, we observe high numbers of pneumococci in nasal washes and the olfactory nerves and epithelium. Significant numbers of pneumococci also infected the olfactory bulbs, brain, and the trigeminal ganglia. The absence of bacteremia in this model makes it unlikely that the bacteria entered the brain from the blood stream. Recovery of colony-forming units from the brain, lungs, olfactory nerves, and epithelium and nasal washes was inhibited by incubating pneumococci with GLS before nasal inoculation. These findings, confirmed by PCR and immunohistochemistry, support a GLSmediated process of infection and are consistent with pneumococci reaching the brain through retrograde axonal transport.

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“…Neolacto recognition has previously been described for other microbes and microbial toxins, such as, dengue virus (22), S. pneumoniae (23), N. meningitidis (24), H. influenzae (24), H. pylori (25), and the heat-labile enterotoxin of E. coli (LT) (26). Dissociation constants have not been determined for any of these interactions, thus it is not known whether they represent low-affinity binding as in the case of RF Borrelia.…”

Section: Discussionmentioning

confidence: 99%

Relapsing fever Borrelia binds to neolacto glycans and mediates rosetting of human erythrocytes

Guo

Teneberg

Münch

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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A hallmark of acute relapsing fever borreliosis is severe bacteremia. Some Borrelia species, such as B. duttonii and B. crocidurae, associate with erythrocytes and induce aggregation recognized as erythrocyte rosetting. Erythrocyte rosettes contribute to disease severity by increased tissue invasiveness (such as invasion of CNS and encephalitis), hemorrhaging, and reduced blood flow in affected microcapillaries. Here we report that relapsing fever Borrelia binds to neolacto (Gal␤4GlcNAc␤3Gal␤4Glc␤1)-carrying glycoconjugates that are present on human erythrocytes. This interaction is of low affinity but is compensated for by the multivalency of neo-lacto-oligosaccharides on the erythrocyte cell surface. Hence, the protein-carbohydrate interaction is dependent on multivalent neolacto-glycans to mediate binding. '' (1-4). Borrelia species capable of rosetting induce more severe symptoms, increased organ invasiveness, hemorrhaging, microemboli formation, and a delayed immune response (3, 4), suggesting that rosetting represents an important virulence factor. In vitro, rosette formation is influenced by both Borrelia species and temperature (1). However, the molecular mechanism that supports rosetting has not been described.Carbohydrates are abundant surface-exposed structures on all eukaryotic cells. Given their ubiquitous nature and immense diversity, it is not surprising that some common motifs have been exploited by pathogens as binding sites for adherence to host cells and in addition to facilitate and/or promote entry into and invasion of the host cells (5, 6). In this study, RF Borrelia bound specifically to a subset of glycosphingolipids (GSLs) isolated from human erythrocytes. The GSL was characterized as Gal␤4GlcNAc␤3Gal␤4Glc␤1Cer (neolactotetraosylceramide) by proton NMR and by liquid chromatography-mass spectrometry (LC/MS) of the saccharide released by hydrolysis with Macrobdella decora ceramide glycanase.* As a natural model system, B. hispanica was found to bind to Neisseria meningiditis, which expresses neolactotetra glycans in its LOS/LPS. The results show that the Borrelia interaction with neolacto glycans is of low affinity and that the interaction necessitates multivalent neolacto epitopes to achieve high affinity. Here we present for the first time a molecular mechanism based on a lectin-glycan interaction that supports RF Borrelia-mediated erythrocyte rosetting. ResultsVariable Erythrocyte Rosetting of RF Borrelia Species. We developed an in vitro rosetting assay measuring hemoglobin release of captured erythrocyte rosettes, allowing detection of subtle changes in rosetting. Assay results correlate with rosetting assessed by microscopy. B. hispanica displayed the greatest capability followed by B. duttonii and B. coriaceae, whereas B. hermsii, B. turicatae, B. recurrentis, and B. crocidurae produced few or no rosettes (Fig. 1). Previous reports have indicated that B. duttonii (2) and B. crocidurae (1, 3, 4) are high rosetters, whereas B. hermsii (1, 3, 4) and B. recurrentis (unpublished) are no...

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Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells.

Cited by 237 publications

References 40 publications

In vitro adherence of Streptococcus pneumoniae to oropharyngeal cells: Enhanced activity and colonization of the upper respiratory tract in patients with recurrent respiratory infections.

In vitro adherence of Streptococcus pneumoniae to oropharyngeal cells: Enhanced activity and colonization of the upper respiratory tract in patients with recurrent respiratory infections.

Pneumococcal carriage results in ganglioside-mediated olfactory tissue infection

Relapsing fever Borrelia binds to neolacto glycans and mediates rosetting of human erythrocytes

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