Abstract
Plants are attractive hosts for the production of recombinant glycoproteins for therapeutic use. Recent advances in glyco-engineering facilitate the elimination of nonmammalian-type glycosylation and introduction of missing pathways for customized N-glycan formation. However, some therapeutically relevant recombinant glycoproteins exhibit unwanted truncated (paucimannosidic) N-glycans that lack GlcNAc residues at the nonreducing terminal end. These paucimannosidic N-glycans increase product heterogeneity and may affect the biological function of the recombinant drugs. Here, we identified two enzymes, β-hexosaminidases (HEXOs) that account for the formation of paucimannosidic N-glycans in Nicotiana benthamiana, a widely used expression host for recombinant proteins. Subcellular localization studies showed that HEXO1 is a vacuolar protein and HEXO3 is mainly located at the plasma membrane in N. benthamiana leaf epidermal cells. Both enzymes are functional and can complement the corresponding HEXO-deficient Arabidopsis thaliana mutants. In planta expression of HEXO3 demonstrated that core α1,3-fucose enhances the trimming of GlcNAc residues from the Fc domain of human IgG. Finally, using RNA interference, we show that suppression of HEXO3 expression can be applied to increase the amounts of complex N-glycans on plant-produced human α1-antitrypsin.
Abstract from the paper’s OpenAlex record; open copy licensed cc-by. Read at the source ↗
The text the model read, with the source record’s inline markup (italics, sub- and superscripts) rendered and its character entities decoded; quote offsets refer to the raw text.
Claims 6
Claim · model-written summary
Two β-hexosaminidases account for paucimannosidic N-glycan formation in Nicotiana benthamiana.
- Taxon
- Nicotiana benthamiana
Nicotiana benthamianae0 - Gene
- β-hexosaminidases (HEXOs)e0
- Outcome
- formation of paucimannosidic N-glycanse0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“we identified two enzymes, β-hexosaminidases (HEXOs) that account for the formation of paucimannosidic N-glycans in Nicotiana benthamiana”
Claim · model-written summary
HEXO1 localized to the vacuole.
- Taxon
- Nicotiana benthamianaNicotiana benthamianat0
- Gene
- HEXO1e0
- Outcome
- vacuolar proteine0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“HEXO1 is a vacuolar protein”
t0“Nicotiana benthamiana”
Claim · model-written summary
HEXO3 localized mainly to the plasma membrane in leaf epidermal cells.
- Taxon
- N. benthamianaNicotiana benthamianae0
- Organ / stage
- leaf epidermal cellse0
- Gene
- HEXO3e0
- Outcome
- mainly located at the plasma membranee0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“HEXO3 is mainly located at the plasma membrane in N. benthamiana leaf epidermal cells”
Claim · model-written summary
Both enzymes complemented corresponding HEXO-deficient Arabidopsis mutants.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianae0 - Treatment
- Both enzymese0
- Outcome
- complemente0
- Comparator
- HEXO-deficient Arabidopsis thaliana mutantse0
Not reportedGeneDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Both enzymes are functional and can complement the corresponding HEXO-deficient Arabidopsis thaliana mutants.”
Claim · model-written summary
Core α1,3-fucose enhanced GlcNAc trimming from human IgG Fc in planta.
- Taxon
- Nicotiana benthamianaNicotiana benthamianat0
- Gene
- HEXO3e0
- Compound
- core α1,3-fucosee0
- Outcome
- trimming of GlcNAc residues from the Fc domain of human IgGe0
- Direction
- enhancese0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“In planta expression of HEXO3 demonstrated that core α1,3-fucose enhances the trimming of GlcNAc residues from the Fc domain of human IgG.”
t0“Nicotiana benthamiana”
Claim · model-written summary
RNA interference suppression of HEXO3 increased complex N-glycans on plant-produced human α1-antitrypsin.
- Taxon
- Nicotiana benthamianaNicotiana benthamianat0
- Treatment
- suppression of HEXO3 expressione0
- Gene
- HEXO3e0
- Outcome
- amounts of complex N-glycans on plant-produced human α1-antitrypsine0
- Direction
- increasee0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“using RNA interference, we show that suppression of HEXO3 expression can be applied to increase the amounts of complex N-glycans on plant-produced human α1-antitrypsin”
t0“Nicotiana benthamiana”
The same questions in other papers
loss of function · molecular: metabolites · Nicotiana benthamianaPositive and negative results
9 papers in the same direction as this paper · 25 in the opposite direction
- negative
- negative
- no effect
31 papers more in this group
See all 35 papers →Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.