Chitin a common glycoconjugate found in insects and crustaceans is comprised of repeating GlcNAc residues. It is possible that C. GANT61 solubility dmso jejuni strains that recognise GlcNAc structures may use insects as vectors as described by Hald et al.[19], or that strains with GlcNAc recognition can better infect crustaceans to survive and propagate in fresh water
ponds and streams [19, 20]. Chitin recognition may therefore be important for environmental survival and spread, also offering advantages for re-infection of more preferred avian or mammalian hosts. In line with previously reported data [3], mannose was recognised more often after environmental stress by most of the C. jejuni strains tested. C. jejuni 331 and 81116 were the only strains to buy BIX 1294 recognise a wide variety of mannose structures under all growth/maintenance conditions. Several other strains, more common to the chicken isolates tested (Human isolate: C. jejuni 351; Chicken isolates: C. jejuni 108, 434 and 506), also recognised some of the branched mannose structures under all conditions tested. Branched mannose is far more common in complex N-linked glycans found on many different LDN-193189 concentration cell surface proteins. These branched mannose structures are typically capped by other sugars including Glc/GlcNAc, Gal/GalNAc
and sialic acid implying that either these interactions are through subterminal binding proteins that can recognise capped structures or are not biologically relevant to infection/colonisation. From the binding profile of C. jejuni to the complex sialylated structure, 11D,
it appears in all cases but C. jejuni 108 that subterminal recognition of mannose in complex N-linked glycans can be ruled out. Similar to C. jejuni binding to mannose, sialic acid recognition was only observed following a period of environmental stress, with all the C. jejuni strains tested exhibiting significantly more binding to sialylated glycans when maintained under Oxaprozin normal atmosphere and at room temperature. This indicates that an adhesion/lectin able to bind sialylated glycans is regulated by the exposure of C. jejuni to environmental stress. As yet, no such protein has been elucidated in C. jejuni. Sialic acid is a common glycan present on multiple cell types and is typically the terminal sugar presented. In the intestines MUC1 is the most heavily sialylated protein present, however, MUC1 acts as a decoy receptor for bacteria and other viral and microbial infecting agents [10]. When MUC1 is bound by pathogens it is released from the cell surface and allows the pathogen to be excreted into the environment through the lumen [10]. A number of pathogens, including C. jejuni, are more infectious, have a lower infectious dose or get into deeper tissues faster when administered to MUC1−/− mice [10]. Of the few sialylated structures that were bound more broadly by C. jejuni, 10A (C. jejuni strains 351, 375, 520, 331, 434, 506), 10B (C.