The N-linking glycosylation system from Actinobacillus pleuropneumoniae is required for adhesion and has potential use in glycoengineering.

Jon Cuccui, Vanessa S Terra, Janine T Bossé, Andreas Naegeli, Sherif Abouelhadid, Yanwen Li, Chia-Wei Lin, Prerna Vohra, Alexander Tucker, Andrew N Rycroft, Duncan Maskell, Markus Aebi, Paul R Langford, Brendan W Wren & BRaDP1T Consortium
Actinobacillus pleuropneumoniae is a mucosal respiratory pathogen causing contagious porcine pleuropneumonia. Pathogenesis studies have demonstrated a major role for the capsule, exotoxins and outer membrane proteins. Actinobacillus pleuropneumoniae can also glycosylate proteins, using a cytoplasmic N-linked glycosylating enzyme designated NGT, but its transcriptional arrangement and role in virulence remains unknown. We investigated the NGT locus and demonstrated that the putative transcriptional unit consists of rimO, ngt and a glycosyltransferase termed agt. From this information we...

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