N-glycosylation at noncanonical Asn-X-Cys sequences in plant cells

作者:Matsui Takeshi; Takita Eiji; Sato Toshio; Kinjo Satoko; Aizawa Michie; Sugiura Yukie; Hamabata Takashi; Sawada Kazutoshi; Kato Ko*
来源:Glycobiology, 2011, 21(8): 994-999.
DOI:10.1093/glycob/cwq198

摘要

The vesicular transport pathway in plant cells is often used for higher accumulation of recombinant proteins. In the endoplasmic reticulum, which acts as a gateway to the vesicular transport pathway, N-glycosylation occurs on specific Asn residues. This N-glycosylation in recombinant proteins must be carefully regulated as it can impact their enzymatic activity, half lives in serum when injected, structural stability, etc. In eukaryotic cells, including plant cells, N-glycans were found to be attached to Asn residues in Asn-X-Ser/Thr (X not equal Pro) sequences. However, recently, N-glycosylations at noncanonical Asn-X-Cys sequences have been found in mammals and yeast. Our laboratory has discovered that N-glycans are attached to Asn residues at Asn-Thr-Cys sequences of double-repeated B subunit of Shiga toxin 2e produced in plant cells, the first reported case of N-glycosylation at a noncanonical Asn-X-Cys sequence in plant cells.

  • 出版日期2011-8