Abstract: A novel lipoteichoic acid (LTA) was isolated from C. difficile, the structure of which is illustrated below wherein n is an integer between 1 and 20, R3 and R4 are independently selected from C 14:0, C 16:0, C 16:1, C 18:0 or C18:1 fatty acid or any combination thereof wherein one of COR3 or COR4 may be replaced by H. Further described are conjugates comprising the novel LTA and vaccines produced using the isolated LTA and the LTA conjugates. The invention also encompasses methods of conferring immunity against C. difficile comprising administering a vaccine of the invention, and methods of detecting C. difficile using the isolated LTA of the invention.

Abstract: A novel lipoteichoic acid (LTA) was isolated from C. difficile, the structure of which is illustrated below wherein n is an integer between 1 and 20, R3 and R4 are independently selected from C 14:0, C 16:0, C 16:1, C 18:0 or C18:1 fatty acid or any combination thereof wherein one of COR3 or COR4 may be replaced by H. Further described are conjugates comprising the novel LTA and vaccines produced using the isolated LTA and the LTA conjugates. The invention also encompasses methods of conferring immunity against C. difficile comprising administering a vaccine of the invention, and methods of detecting C. difficile using the isolated LTA of the invention.

Abstract: Multiple strains and species of Campylobacter share a common glycan moiety which is present in a plurality of surface-exposed glycoproteins. This glycan has the formula: GalNAc-a1, 4-GalNAc-a1,4-[Glc-?1,3]GalNAc-a1,4-GalNAc-a1,4-GalNAc-a1,3-Bac, wherein Bac is 2, 4-diacetamido-2,4,6-trideoxy-D-glucopyranose. This glycan and immunologically active fragments of it have use as vaccines against campylobacter infection in humans and animals. As well, antibodies which specifically bind these compounds may be provided. Such antibodies and vaccines may be used to prevent or neutralize campylobacter infections in livestock thereby preventing this pathogen from entering the human food chain. The glycan may be linked to one or more amino acids to form a glycopeptide. As well, a method for determining the glycan structure of an intact glycoprotein consists of subjecting a sample to high resolution magic angle spinning nuclear magnetic resonance (HR-MAS-NMR) spectroscopy.

Abstract: Multiple strains and species of Campylobacter were found to share a common glycan moitie which is present in a plurality of surface-exposed glycoproteins. This glycan has the formula: GalNAc-a1,4-GalNAc-a1,4-[Glc-?1,3]GalNAc-a1,4-GalNAc-a1,4-GalNAc-a1,3-Bac, wherein Bac is 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose. This glycan and immunologically active fragments of it have use as vaccines against campylobacter infection in humans and animals. As well, antibodies which specifically bind these compounds may be provided. Such antibodies and vaccines may be used to prevent or neutralize campylobacter infections in livestock thereby preventing this pathogen from entering the human food chain. The glycan may be linked to one or more amino acids to form a glycopeptide. As well, a method for determining the glycan structure of an intact glycoprotein consists of subjecting a sample to high resolution magic angle spinning nuclear magnetic resonance (HR-MAS-NMR) spectroscopy.