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Published on: June 25, 2018
N-glycosylation at noncanonical Asn-X-Cys sequences in plant cells
Takeshi Matsui1, Eiji Takita, Toshio Sato
1Advanced Technology Research Laboratories, Idemitsu Kosan Co., Ltd., 1280 Kamiizumi, Sodegaura-shi, Chiba 299-0293, Japan.
Abstract:
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 ≠ 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.
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