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

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 gr

SUBMITTER: Day CJ 

PROVIDER: S-EPMC3852789 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature