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: Avermectin aglycones are glycosylated by fermentation in a medium of a non-producing mutant of Streptomyces avermitilis MA-6078. The glycosylation produces the monosaccharide and disaccharide derivatives while leaving the remainder of the molecule intact. The microorganism glycosylates with the .alpha.-L-oleandrose moiety.

Abstract: Certain isolated fractions, extracted from allergy-causing molds, have been found to be antigenic but non-allergenic, and are able to decrease substantially or prevent the susceptibility to mold allergens of allergic individuals. The antigenic non-allergenic fractions contain protein and carbohydrate and have molecular weights which have been found to vary with the mold source. Increased polyvalent protection can be realized by combining fractions from different molds, e.g. Alternaria with Hormodendrum or Helminthosporium. The extracts are administered parenterally, preferably subcutaneously in isotonic saline.