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Assessment of glycan interactions of clinical and avian isolates of Campylobacter jejuni.

Day CJ, Tram G, Hartley-Tassell LE, Tiralongo J, Korolik V - BMC Microbiol. (2013)

Bottom Line: Chicken isolates were found to bind to a broader range of glycans compared to the human isolates, recognising branched mannose and carageenan (red seaweed) glycans.Glycan array data was confirmed using cell-based lectin inhibition assays with the fucose (UEA-I) and mannose (ConA) binding lectins.This study confirms that all C. jejuni strains tested bind to a broad range of glycans, with the majority of strains (all except 81116) altering recognition of sialic acid and mannose after environmental stress.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute for Glycomics, G26, Griffith University Gold Coast Campus, Queensland 4222, Australia. v.korolik@griffith.edu.au.

ABSTRACT

Background: Campylobacter jejuni strain 11168 was demonstrated to have a broad specificity for eukaryotic surface glycosylation using glycan array analysis. The initial screen indicated that sialic acid and mannose are important binding partners after environmental stress, while galactose and fucose structures are likely to be involved in persistent infection.

Results: In this broader study, five additional human/clinical isolates and six chicken isolates were fully assessed to determine their glycan binding capacity using an extended glycan array. C. jejuni 11168 was rescreened here due to the presence of glycoaminoglycan (GAG) and other structures that were not available on our previous glycan array. The current array analysis of additional C. jejuni strains confirmed the growth condition dependent differences in glycan binding that was previously observed for C. jejuni 11168. We noted strain to strain variations, particularly for the human isolates C. jejuni 520 and 81116 and the chicken isolate C. jejuni 331, with the majority of differences observed in galactose, mannose and GAG binding. Chicken isolates were found to bind to a broader range of glycans compared to the human isolates, recognising branched mannose and carageenan (red seaweed) glycans. Glycan array data was confirmed using cell-based lectin inhibition assays with the fucose (UEA-I) and mannose (ConA) binding lectins.

Conclusions: This study confirms that all C. jejuni strains tested bind to a broad range of glycans, with the majority of strains (all except 81116) altering recognition of sialic acid and mannose after environmental stress. Galactose and fucose structures were bound best by all strains when C. jejuni was grown under host like conditions confirming the likelihood of these structures being involved in persistent infection.

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Related in: MedlinePlus

Lectin and free glycan competition assays. Comparison between normal adherence (100%) and inhibition with lectin or glycan pre-treatment. The smaller the bar the less C. jejuni adhered in the presence of the lectin/glycan. A. ConA competition of C. jejuni adherence to Caco-2 cells; B. UEA-I competition of C. jejuni adherence to Caco-2 cells. C. Competion assays with free glycans with C. jejuni 11168 and 331 adhering to Caco-2 cells.
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Figure 1: Lectin and free glycan competition assays. Comparison between normal adherence (100%) and inhibition with lectin or glycan pre-treatment. The smaller the bar the less C. jejuni adhered in the presence of the lectin/glycan. A. ConA competition of C. jejuni adherence to Caco-2 cells; B. UEA-I competition of C. jejuni adherence to Caco-2 cells. C. Competion assays with free glycans with C. jejuni 11168 and 331 adhering to Caco-2 cells.

Mentions: As predicted from the array results, ConA had the greatest inhibitory effects on the adherence of C. jejuni 81116 and 331 with reductions of more than 70%, no significant difference was observed for the other strains tested (Figure 1A). UEA-I resulted in significant reduction in adherence for all strains tested but did not affect the adherence of the control E. coli DH5a strain (Figure 1B).


Assessment of glycan interactions of clinical and avian isolates of Campylobacter jejuni.

Day CJ, Tram G, Hartley-Tassell LE, Tiralongo J, Korolik V - BMC Microbiol. (2013)

Lectin and free glycan competition assays. Comparison between normal adherence (100%) and inhibition with lectin or glycan pre-treatment. The smaller the bar the less C. jejuni adhered in the presence of the lectin/glycan. A. ConA competition of C. jejuni adherence to Caco-2 cells; B. UEA-I competition of C. jejuni adherence to Caco-2 cells. C. Competion assays with free glycans with C. jejuni 11168 and 331 adhering to Caco-2 cells.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3852789&req=5

Figure 1: Lectin and free glycan competition assays. Comparison between normal adherence (100%) and inhibition with lectin or glycan pre-treatment. The smaller the bar the less C. jejuni adhered in the presence of the lectin/glycan. A. ConA competition of C. jejuni adherence to Caco-2 cells; B. UEA-I competition of C. jejuni adherence to Caco-2 cells. C. Competion assays with free glycans with C. jejuni 11168 and 331 adhering to Caco-2 cells.
Mentions: As predicted from the array results, ConA had the greatest inhibitory effects on the adherence of C. jejuni 81116 and 331 with reductions of more than 70%, no significant difference was observed for the other strains tested (Figure 1A). UEA-I resulted in significant reduction in adherence for all strains tested but did not affect the adherence of the control E. coli DH5a strain (Figure 1B).

Bottom Line: Chicken isolates were found to bind to a broader range of glycans compared to the human isolates, recognising branched mannose and carageenan (red seaweed) glycans.Glycan array data was confirmed using cell-based lectin inhibition assays with the fucose (UEA-I) and mannose (ConA) binding lectins.This study confirms that all C. jejuni strains tested bind to a broad range of glycans, with the majority of strains (all except 81116) altering recognition of sialic acid and mannose after environmental stress.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute for Glycomics, G26, Griffith University Gold Coast Campus, Queensland 4222, Australia. v.korolik@griffith.edu.au.

ABSTRACT

Background: Campylobacter jejuni strain 11168 was demonstrated to have a broad specificity for eukaryotic surface glycosylation using glycan array analysis. The initial screen indicated that sialic acid and mannose are important binding partners after environmental stress, while galactose and fucose structures are likely to be involved in persistent infection.

Results: In this broader study, five additional human/clinical isolates and six chicken isolates were fully assessed to determine their glycan binding capacity using an extended glycan array. C. jejuni 11168 was rescreened here due to the presence of glycoaminoglycan (GAG) and other structures that were not available on our previous glycan array. The current array analysis of additional C. jejuni strains confirmed the growth condition dependent differences in glycan binding that was previously observed for C. jejuni 11168. We noted strain to strain variations, particularly for the human isolates C. jejuni 520 and 81116 and the chicken isolate C. jejuni 331, with the majority of differences observed in galactose, mannose and GAG binding. Chicken isolates were found to bind to a broader range of glycans compared to the human isolates, recognising branched mannose and carageenan (red seaweed) glycans. Glycan array data was confirmed using cell-based lectin inhibition assays with the fucose (UEA-I) and mannose (ConA) binding lectins.

Conclusions: This study confirms that all C. jejuni strains tested bind to a broad range of glycans, with the majority of strains (all except 81116) altering recognition of sialic acid and mannose after environmental stress. Galactose and fucose structures were bound best by all strains when C. jejuni was grown under host like conditions confirming the likelihood of these structures being involved in persistent infection.

Show MeSH
Related in: MedlinePlus