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. 2021 Mar 9;12:635962. doi: 10.3389/fpls.2021.635962

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Copyright © 2021 Kaulfürst-Soboll, Mertens-Beer, Brehler, Albert and von Schaewen.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Analysis of glycoprotein stability in N. benthamiana GNTI- and MANII-RNAi plants. (A) N. benthamiana wild-type (wt), GNTI-RNAi (#10), and MANII-RNAi (#4) T3 plants prior to agroinfiltration. (B) Immunoblot analysis of indicated leaf extracts (membrane fractions) developed with anti-complex glycan antiserum (α-cgly = α-PHA-L). The Ponceau S-stained blot (protein) is shown as the loading reference. Apparent molecular masses are indicated in kDa (PageRuler Prestained Protein Ladder, Fermentas). (C) Confocal laser scanning microscopy (CLSM) images of KOR1-GFP expression in N. benthamiana wild-type and the indicated RNAi lines. Merging of GFP (green) and chlorophyll autofluorescence (blue) with bright field. Bars = 10 μM. (D) Immunoblot analysis of leaf extracts (membrane fractions) upon agroinfiltration and development with anti-GFP antiserum (α-GFP). Tunicamycin (Tunica, 10 μM) treatment results in the accumulation of non-glycosylated KOR1-GFP (band shift). The fading top bands indicate decay due to protein turnover. 19K, co-expressed Agrobacterium silencing suppressor strain (negative control). The Ponceau S-stained blots are shown as the protein loading reference. Molecular masses are indicated in kDa (PageRuler Prestained Protein Ladder, Fermentas).