NCBI PubMed ID:16697990 Publication DOI:10.1016/j.carres.2006.04.031 Journal NLM ID:0043535 Publisher: Elsevier Correspondence: yukitoriken.jp Institutions: RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan, Graduate School of Science and Engineering, Saitama University, Sakura-ku, Saitama 338-8570, Japan, CREST, Japan Science and Technology Agency (JST), Kawaguchi, Saitama 332-1102, Japan
Various types of protein glycosylation have been identified from prokaryotes. Recent investigations have revealed the presence of N-linked glycoproteins in the pathogenic bacterium, Campylobacter jejuni. The structure of this glycan is unique, consisting of 5 GalNAc and 1 Glc, in addition to 2,4-diacetamido-2,4,6-trideoxy-d-glucopyranose (bacillosamine; Bac), which is N-glycosidically linked to the side chain of asparagine (Asn). We synthesized Bac from a 2-azido-2-deoxy-d-galactose derivative, which was further converted to the Asn-linked form.