期刊
GLYCOBIOLOGY
卷 26, 期 4, 页码 398-409出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwv111
关键词
bacterial glycobiology; deep-sea vent bacteria; glycoengineering; N-linked glycosylation
资金
- Wellcome Trust [102978/Z/13/Z]
- Biotechnology and Biological Sciences Research Council [BB/H017437/1]
- Biotechnology and Biological Sciences Research Council [BB/H017437/1, BB/H017542/1, BB/F009321/1, E20372] Funding Source: researchfish
- Wellcome Trust [102979/Z/13/Z] Funding Source: researchfish
- BBSRC [BB/F009321/1, BB/H017437/1, BB/H017542/1] Funding Source: UKRI
- Wellcome Trust [102978/Z/13/Z, 102979/Z/13/Z] Funding Source: Wellcome Trust
Bacterial N-linking oligosaccharyl transferases (OTase enzymes) transfer lipid-linked glycans to selected proteins in the periplasm and were first described in the intestinal pathogen Campylobacter jejuni, a member of the epsilon-proteobacteria-subdivision of bacteria. More recently, orthologues from other epsilon-proteobacterial Campylobacter and Helicobacter species and a delta-proteobacterium, Desulfovibrio desulfuricans, have been described, suggesting that these two subdivisions of bacteria may be a source of further N-linked protein glycosylation systems. Whole-genome sequencing of both epsilon- and delta-proteobacteria from deep-sea vent habitats, a rich source of species from these subdivisions, revealed putative ORFs encoding OTase enzymes and associated adjacent glycosyltransferases similar to the C. jejuni N-linked glycosylation locus. We expressed putative OTase ORFs from the deep-sea vent species Nitratiruptor tergarcus, Sulfurovum lithotrophicum and Deferribacter desulfuricans in Escherichia coli and showed that they were able to functionally complement the C. jejuni OTase, CjPglB. The enzymes were shown to possess relaxed glycan specificity, transferring diverse glycan structures and demonstrated different glycosylation sequon specificities. Additionally, a permissive D. desulfuricans acceptor protein was identified, and we provide evidence that the N-linked glycan synthesized by N. tergarcus and S. lithotrophicum contains an acetylated sugar at the reducing end. This work demonstrates that deep-sea vent bacteria encode functional N-glycosylation machineries and are a potential source of biotechnologically important OTase enzymes.
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