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Differential carbohydrate recognition by Campylobacter jejuni strain 11168: influences of temperature and growth conditions.

Day CJ, Tiralongo J, Hartnell RD, Logue CA, Wilson JC, von Itzstein M, Korolik V - PLoS ONE (2009)

Bottom Line: Significantly, it was found that only when challenged with normal oxygen at room temperature did 11168-O consistently bind to sialic acid or terminal mannose structures, while 11168-GS bound these structures regardless of growth/maintenance conditions.These binding differences identified through glycan array analysis were confirmed by the ability of specific lectins to competitively inhibit the adherence of C. jejuni to a Caco-2 intestinal cell line.Our data suggests that the binding of mannose and/or N-acetylneuraminic acid may provide the initial interactions important for colonisation following environmental exposure.

View Article: PubMed Central - PubMed

Affiliation: Institute for Glycomics, Griffith University Gold Coast Campus, Queensland, Australia.

ABSTRACT
The pathogenic clinical strain NCTC11168 was the first Campylobacter jejuni strain to be sequenced and has been a widely used laboratory model for studying C. jejuni pathogenesis. However, continuous passaging of C. jejuni NCTC11168 has been shown to dramatically affect its colonisation potential. Glycan array analysis was performed on C. jejuni NCTC11168 using the frequently passaged, non-colonising, genome sequenced (11168-GS) and the infrequently passaged, original, virulent (11168-O) isolates grown or maintained under various conditions. Glycan structures recognised and bound by C. jejuni included terminal mannose, N-acetylneuraminic acid, galactose and fucose. Significantly, it was found that only when challenged with normal oxygen at room temperature did 11168-O consistently bind to sialic acid or terminal mannose structures, while 11168-GS bound these structures regardless of growth/maintenance conditions. Further, binding of un-capped galactose and fucosylated structures was significantly reduced when C. jejuni was maintained at 25 degrees C under atmospheric oxygen conditions. These binding differences identified through glycan array analysis were confirmed by the ability of specific lectins to competitively inhibit the adherence of C. jejuni to a Caco-2 intestinal cell line. Our data suggests that the binding of mannose and/or N-acetylneuraminic acid may provide the initial interactions important for colonisation following environmental exposure.

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Relative adherence of C. jejuni 11168 to sialidase treated Caco-2 cells.Relative adherence of 11168-GS (left) and 11168-O (right) to sialidase treated Caco-2 cells with respect to normal adherence levels (25°C, black bar; 37°C, grey bar; and 42°C, white bar).
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pone-0004927-g007: Relative adherence of C. jejuni 11168 to sialidase treated Caco-2 cells.Relative adherence of 11168-GS (left) and 11168-O (right) to sialidase treated Caco-2 cells with respect to normal adherence levels (25°C, black bar; 37°C, grey bar; and 42°C, white bar).

Mentions: To further explore the significance of Neu5Ac in C. jejuni 11168 adherence to Caco-2 cells, the effect of Neu5Ac removal by sialidase treatment of Caco-2 cells was explored. Sialidase treatment of Caco-2 cells resulted in a 50% reduction in the adherence of both 11168-GS 25°C and 11168-O 25°C compared to non-sialidase treated controls (P = 0.03 and 0.02 respectively, Figure 7). Reduction in adherence to sialidase treated Caco-2 cells was also observed for 11168-GS grown at 37° (40% reduction) and 42°C (12% reduction); however, only 11168-GS 37°C was significantly different to untreated controls (P = 0.02, Figure 7). The opposite was observed for the adherence of 11168-O 37°C and 42°C to sialidase treated Caco-2 cells with increases of 47% and 109%, respectively. However, only the increase observed for 11168-O 42°C was significantly different to normal adherence observed for untreated Caco-2 cells (P = 0.04).


Differential carbohydrate recognition by Campylobacter jejuni strain 11168: influences of temperature and growth conditions.

Day CJ, Tiralongo J, Hartnell RD, Logue CA, Wilson JC, von Itzstein M, Korolik V - PLoS ONE (2009)

Relative adherence of C. jejuni 11168 to sialidase treated Caco-2 cells.Relative adherence of 11168-GS (left) and 11168-O (right) to sialidase treated Caco-2 cells with respect to normal adherence levels (25°C, black bar; 37°C, grey bar; and 42°C, white bar).
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Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2654152&req=5

pone-0004927-g007: Relative adherence of C. jejuni 11168 to sialidase treated Caco-2 cells.Relative adherence of 11168-GS (left) and 11168-O (right) to sialidase treated Caco-2 cells with respect to normal adherence levels (25°C, black bar; 37°C, grey bar; and 42°C, white bar).
Mentions: To further explore the significance of Neu5Ac in C. jejuni 11168 adherence to Caco-2 cells, the effect of Neu5Ac removal by sialidase treatment of Caco-2 cells was explored. Sialidase treatment of Caco-2 cells resulted in a 50% reduction in the adherence of both 11168-GS 25°C and 11168-O 25°C compared to non-sialidase treated controls (P = 0.03 and 0.02 respectively, Figure 7). Reduction in adherence to sialidase treated Caco-2 cells was also observed for 11168-GS grown at 37° (40% reduction) and 42°C (12% reduction); however, only 11168-GS 37°C was significantly different to untreated controls (P = 0.02, Figure 7). The opposite was observed for the adherence of 11168-O 37°C and 42°C to sialidase treated Caco-2 cells with increases of 47% and 109%, respectively. However, only the increase observed for 11168-O 42°C was significantly different to normal adherence observed for untreated Caco-2 cells (P = 0.04).

Bottom Line: Significantly, it was found that only when challenged with normal oxygen at room temperature did 11168-O consistently bind to sialic acid or terminal mannose structures, while 11168-GS bound these structures regardless of growth/maintenance conditions.These binding differences identified through glycan array analysis were confirmed by the ability of specific lectins to competitively inhibit the adherence of C. jejuni to a Caco-2 intestinal cell line.Our data suggests that the binding of mannose and/or N-acetylneuraminic acid may provide the initial interactions important for colonisation following environmental exposure.

View Article: PubMed Central - PubMed

Affiliation: Institute for Glycomics, Griffith University Gold Coast Campus, Queensland, Australia.

ABSTRACT
The pathogenic clinical strain NCTC11168 was the first Campylobacter jejuni strain to be sequenced and has been a widely used laboratory model for studying C. jejuni pathogenesis. However, continuous passaging of C. jejuni NCTC11168 has been shown to dramatically affect its colonisation potential. Glycan array analysis was performed on C. jejuni NCTC11168 using the frequently passaged, non-colonising, genome sequenced (11168-GS) and the infrequently passaged, original, virulent (11168-O) isolates grown or maintained under various conditions. Glycan structures recognised and bound by C. jejuni included terminal mannose, N-acetylneuraminic acid, galactose and fucose. Significantly, it was found that only when challenged with normal oxygen at room temperature did 11168-O consistently bind to sialic acid or terminal mannose structures, while 11168-GS bound these structures regardless of growth/maintenance conditions. Further, binding of un-capped galactose and fucosylated structures was significantly reduced when C. jejuni was maintained at 25 degrees C under atmospheric oxygen conditions. These binding differences identified through glycan array analysis were confirmed by the ability of specific lectins to competitively inhibit the adherence of C. jejuni to a Caco-2 intestinal cell line. Our data suggests that the binding of mannose and/or N-acetylneuraminic acid may provide the initial interactions important for colonisation following environmental exposure.

Show MeSH
Related in: MedlinePlus