Plant members of the α1→3/4‐fucosyltransferase gene family encode an α1→4‐fucosyltransferase, potentially involved in Lewis<sup>a</sup> biosynthesis, and two core α1→3‐fucosyltransferases<sup>1</sup>

Bakker, Hans; Schijlen, Elio; Vries, Theodora de; Schiphorst, Wietske E. C. M.; Jordi, W.; Lommen, Arjen; Bosch, Dirk; Die, Irma van

doi:10.1016/s0014-5793(01)02999-4

Cited by 54 publications

(28 citation statements)

References 47 publications

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“…Alternatively, although this occurs at a very low frequency, the terminal GlcNAc residues of secreted proteins may be extended by b1,3-galactose and a1,4-fucose residues by the respective glycosyltransferases. These structures are called Lewis A epitopes and can also be found on glycoconjugates in mammals [18,19]. Since any of the above-described processing reactions may not go to completion, N-glycan structures, even on a single type of glycoprotein, can be heterogeneous and may include complex glycans as well as various intermediate high-mannose structures [20,21].…”

Section: N-glycosylation: Differences Between Plants and Mammalsmentioning

confidence: 99%

Plant glycans: friend or foe in vaccine development?

Bosch

Schots

2010

Expert Review of Vaccines

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Section: N-glycosylation: Differences Between Plants and Mammalsmentioning

confidence: 99%

Plant glycans: friend or foe in vaccine development?

Bosch

Schots

2010

Expert Review of Vaccines

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“…To date, FucT enzymes that display ␣1,4 activity have also been found in the chimpanzee (48), Rhesus macaque (Old World Monkey) (49), and plants (50,51). According to sequence alignment, all of these FucTs contain a tryptophan residue within the N-terminal hypervariable stem region, which was found to be essential for conferring ␣1,4 activity in mammalian FucTs (18).…”

Section: Ua948mentioning

confidence: 99%

C-terminal Amino Acids of Helicobacter pylori α1,3/4 Fucosyltransferases Determine Type I and Type II Transfer

Wang

Palcic

et al. 2003

Journal of Biological Chemistry

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The ␣1,3/4 fucosyltransferase (FucT) enzyme from Helicobacter pylori catalyzes fucose transfer from donor GDP-␤-L-fucose to the GlcNAc group of two series of acceptor substrates in H. pylori lipopolysaccharide: ␤Gal1,3␤GlcNAc (Type I) or ␤Gal1,4␤GlcNAc (Type II). Fucose is added either in ␣1,3 linkage of Type II acceptor to produce Lewis X or in ␣1,4 linkage of Type I acceptor to produce Lewis A, respectively. H. pylori FucTs from different strains have distinct Type I or Type II substrate specificities. FucT in H. pylori strain NCTC11639 has an exclusive ␣1,3 activity because it recognizes only Type II substrates, whereas FucT in H. pylori strain UA948 can utilize both Type II and Type I acceptors; thus it has both ␣1,3 and ␣1,4 activity, respectively. To identify elements conferring substrate specificity, 12 chimeric FucTs were constructed by domain swapping between 11639FucT and UA948FucT and characterized for their ability to transfer fucose to Type I and Type II acceptors. Our results indicate that the C-terminal region of H. pylori FucTs controls Type I and Type II acceptor specificity. In particular, the highly divergent C-terminal portion, seven amino acids DNP-FIFC at positions 347-353 in 11639FucT, and the corresponding 10 amino acids CNDAHYSALH at positions 345-354 in UA948FucT, controls the Type I and Type II acceptor recognition. This is the opposite of mammalian FucTs where acceptor preference is determined primarily by the N-terminal residues in the hypervariable stem domain.

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“…FUT13 has been cloned from several plant species, and its enzymatic activity has been characterized. FUT13 has a strict acceptor substrate specificity for type 1 chain-based glycan structures, whereas type 2 chains (Galb1-4GlcNAc), which are typical for mammalian N-linked glycans, are not used (Bakker et al, 2001a;Wilson, 2001a;Palma et al, 2001;Lé onard et al, 2002Lé onard et al, , 2005a. However, the b1,3-galactosyltransferase involved in Le a biosynthesis has not been characterized so far.…”

Section: Introductionmentioning

confidence: 99%

A Unique β1,3-Galactosyltransferase Is Indispensable for the Biosynthesis of N-Glycans Containing Lewis a Structures in Arabidopsis thaliana

et al. 2007

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In plants, the only known outer-chain elongation of complex N-glycans is the formation of Lewis a [Fuca1-4(Galb1-3) GlcNAc-R] structures. This process involves the sequential attachment of b1,3-galactose and a1,4-fucose residues by b1,3-galactosyltransferase and a1,4-fucosyltransferase. However, the exact mechanism underlying the formation of Lewis a epitopes in plants is poorly understood, largely because one of the involved enzymes, b1,3-galactosyltransferase, has not yet been identified and characterized. Here, we report the identification of an Arabidopsis thaliana b1,3-galactosyltransferase involved in the biosynthesis of the Lewis a epitope using an expression cloning strategy. Overexpression of various candidates led to the identification of a single gene (named GALACTOSYLTRANSFERASE1 [GALT1]) that increased the originally very low Lewis a epitope levels in planta. Recombinant GALT1 protein produced in insect cells was capable of transferring b1,3-linked galactose residues to various N-glycan acceptor substrates, and subsequent treatment of the reaction products with a1,4-fucosyltransferase resulted in the generation of Lewis a structures. Furthermore, transgenic Arabidopsis plants lacking a functional GALT1 mRNA did not show any detectable amounts of Lewis a epitopes on endogenous glycoproteins. Taken together, our results demonstrate that GALT1 is both sufficient and essential for the addition of b1,3-linked galactose residues to N-glycans and thus is required for the biosynthesis of Lewis a structures in Arabidopsis. Moreover, cell biological characterization of a transiently expressed GALT1-fluorescent protein fusion using confocal laser scanning microscopy revealed the exclusive location of GALT1 within the Golgi apparatus, which is in good agreement with the proposed physiological action of the enzyme.

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Plant members of the α1→3/4‐fucosyltransferase gene family encode an α1→4‐fucosyltransferase, potentially involved in Lewis^a biosynthesis, and two core α1→3‐fucosyltransferases¹

Cited by 54 publications

References 47 publications

Plant glycans: friend or foe in vaccine development?

Plant glycans: friend or foe in vaccine development?

C-terminal Amino Acids of Helicobacter pylori α1,3/4 Fucosyltransferases Determine Type I and Type II Transfer

A Unique β1,3-Galactosyltransferase Is Indispensable for the Biosynthesis of N-Glycans Containing Lewis a Structures in Arabidopsis thaliana

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Plant members of the α1→3/4‐fucosyltransferase gene family encode an α1→4‐fucosyltransferase, potentially involved in Lewisa biosynthesis, and two core α1→3‐fucosyltransferases1

Cited by 54 publications

References 47 publications

Plant glycans: friend or foe in vaccine development?

Plant glycans: friend or foe in vaccine development?

C-terminal Amino Acids of Helicobacter pylori α1,3/4 Fucosyltransferases Determine Type I and Type II Transfer

A Unique β1,3-Galactosyltransferase Is Indispensable for the Biosynthesis of N-Glycans Containing Lewis a Structures in Arabidopsis thaliana

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Plant members of the α1→3/4‐fucosyltransferase gene family encode an α1→4‐fucosyltransferase, potentially involved in Lewis^a biosynthesis, and two core α1→3‐fucosyltransferases¹