Molecular genetic basis for the variable expression of Lewis Y antigen in <i>Helicobacter pylori</i> : analysis of the α(1,2) fucosyltransferase gene

Wang, Ge; Rasko, David A.; Sherburne, Richard; Taylor, Diane E.

doi:10.1046/j.1365-2958.1999.01268.x

Cited by 127 publications

(140 citation statements)

References 32 publications

(44 reference statements)

Supporting

Mentioning

135

Contrasting

Order By: Relevance

“…Recently, a gene encoding α1,3-FucT in H. pylori was identified and characterized (Ge et al, 1997 ;Martin et al, 1997), and the whole genome sequences (Alm et al, 1999 ;Tomb et al, 1997) (Wang et al, 1999). Here we report the development of a sensitive assay system for detection of Hp α1,2-FucT enzyme activity, and the characterization of its properties and functions in the synthesis of Lewis antigens.…”

Section: Fig 1 Structural Relationship Between Lewis Antigens (A) Amentioning

confidence: 89%

“…2a, pGEMB3). In vitro expression of this gene has demonstrated that the full-length protein (equivalent to that of prototype UA802 α1,2-FucT) can be produced from this gene, most probably by a mechanism of translational frameshifting (the frequency was around 50 %) (Wang et al, 1999). In this study, the plasmid pGEMB3 carrying the 26695 fucT2 gene was transferred into E. coli CLM4(pGP1-2), and the gene was expressed in the same way as described above.…”

Section: Pylori Strain 26695mentioning

confidence: 91%

“…DNA sequence analysis predicted the Hp α1,2-FucT to be a hydrophilic protein (Wang et al, 1999), and the same is true for Hp α1,3-FucT (Ge et al, 1997). However, the determination of Hp α1,3-FucT activity from the overexpressed proteins demonstrated that the majority of the activity was present in the membrane fraction (Ge et al, 1997 using Le X or type 1 as acceptors (Table 2).…”

Section: Hp α12-fuct Is a Soluble Proteinmentioning

confidence: 93%

“…Here we report the development of a sensitive assay system for detection of Hp α1,2-FucT enzyme activity, and the characterization of its properties and functions in the synthesis of Lewis antigens. Different H. pylori strains express different types of fucT2 genes in which a frameshift mutation at the DNA level and ribosomal frameshifting at the translation level may be involved (Wang et al, 1999). We have proceeded to examine an enzyme encoded by a variant of the fucT2 gene.…”

Section: Fig 1 Structural Relationship Between Lewis Antigens (A) Amentioning

confidence: 99%

“…The disruption of this gene in the bacterium resulted in no Le Y production, suggesting that its gene product is involved in Le Y synthesis (Wang et al, 1999). Initially, we quantified the α1,2-FucT activity by using LacNAc and Le X as acceptors, the two potential substrates of α1,2-FucT for the synthesis of Le Y (Fig.…”

Section: Acceptor Specificity Of Hp α12-fuctmentioning

confidence: 99%

See 4 more Smart Citations

Novel Helicobacter pylori α1,2-fucosyltransferase, a key enzyme in the synthesis of Lewis antigens

et al. 1999

Self Cite

View full text Add to dashboard Cite

Section: Fig 1 Structural Relationship Between Lewis Antigens (A) Amentioning

confidence: 89%

Section: Pylori Strain 26695mentioning

confidence: 91%

Section: Hp α12-fuct Is a Soluble Proteinmentioning

confidence: 93%

Section: Fig 1 Structural Relationship Between Lewis Antigens (A) Amentioning

confidence: 99%

Section: Acceptor Specificity Of Hp α12-fuctmentioning

confidence: 99%

See 3 more Smart Citations

Novel Helicobacter pylori α1,2-fucosyltransferase, a key enzyme in the synthesis of Lewis antigens

et al. 1999

Self Cite

View full text Add to dashboard Cite

One‐Pot Multienzyme Synthesis of Lewis x and Sialyl Lewis x Antigens

Lau

et al. 2012

CP Chemical Biology

View full text Add to dashboard Cite

L‐Fucose has been found abundantly in human milk oligosaccharides, bacterial lipopolysaccharides, glycolipids, and many N‐ and O‐linked glycans produced by mammalian cells. Fucose‐containing carbohydrates have important biological functions. Alterations in the expression of fucosylated oligosaccharides have been observed in several pathological processes such as cancer and atherosclerosis. Chemical formation of fucosidic bonds is challenging due to its acid lability. Enzymatic construction of fucosidic bonds by fucosyltransferases is highly efficient and selective but requires the expensive sugar nucleotide donor guanosine 5′‐diphosphate‐L‐fucose (GDP‐Fuc). Here, we describe a protocol for applying a one‐pot three‐enzyme system in synthesizing structurally defined fucose‐containing oligosaccharides from free L‐fucose. In this system, GDP‐Fuc is generated from L‐fucose, adenosine 5′‐triphosphate (ATP), and guanosine 5′‐triphosphate (GTP) by a bifunctional L‐fucokinase/GDP‐fucose pyrophosphorylase (FKP). An inorganic pyrophosphatase (PpA) is used to degrade the by‐product pyrophosphate (PPi) to drive the reaction towards the formation of GDP‐Fuc. In situ generated GDP‐Fuc is then used by a suitable fucosyltransferase for the formation of fucosides. The three‐enzyme reactions are carried out in one pot without the need for high‐cost sugar nucleotide or isolation of intermediates. The time for the synthesis is 4 to 24 hr. Purification and characterization of products can be completed in 2 to 3 days. Curr. Protoc. Chem. Biol. 4:233‐247 © 2012 by John Wiley & Sons, Inc.

show abstract

Hydrolysis and Formation of Glycosidic Bonds

Monti

Riva

2012

Enzyme Catalysis in Organic Synthesis

View full text Add to dashboard Cite

Carbohydrates play an important role in many biological events, such as cellular communication and physiological responses. In fact, oligosaccharides and various glycoconjugates have been shown to modulate different molecular recognition processes, including viral and bacterial pathogens recognition [1][2][3][4][5], tumor-associated cell adhesion and metastasis events [6-8], immune response [9], fertilization [10], and neuronal development [11]. This significant role, together with advances in the glycomics field and the recent developments of new synthetic methodologies, for example, the glycorandomization of biologically active natural products [12,13], makes glycoconjugates extremely attractive therapeutic targets nowadays [14][15][16][17].However, the presence of multiple functional groups and stereocenters in carbohydrates makes them challenging targets for organic chemists. Time-consuming protecting group manipulations and complex synthetic schemes are often required to suitably discriminate among hydroxyl groups with similar reactivities and/or to obtain the desired glycosidic linkage by using specifically activated donors and acceptors. Both regioselectivity and stereospecificity need to be strictly controlled and, as the number of different monosaccharide units as well as of glycan structures of interest is very large, a general methodology for oligosaccharide synthesis is still far from being reached. Moreover, despite recent progress in the solid-phase synthesis of oligosaccharides [14,16,18], an automated oligosaccharide synthesizer for all purposes is not yet commercially available and not all the common glycosidic linkages are accessible. Even the structural characterization of the saccharidic part of novel glycoconjugates from natural sources is still a demanding task -no automated sequencing techniques are fully developed, unlike the case of nucleic acids and peptides.Finally, the natural complexity of glycoconjugates is amplified by the extreme variety of aglycon structures coupled to the glycan chains, which can range from Enzyme Catalysis in Organic Synthesis, Third Edition. Edited

show abstract

Molecular genetic basis for the variable expression of Lewis Y antigen in Helicobacter pylori : analysis of the α(1,2) fucosyltransferase gene

Cited by 127 publications

References 32 publications

Novel Helicobacter pylori α1,2-fucosyltransferase, a key enzyme in the synthesis of Lewis antigens

Novel Helicobacter pylori α1,2-fucosyltransferase, a key enzyme in the synthesis of Lewis antigens

One‐Pot Multienzyme Synthesis of Lewis x and Sialyl Lewis x Antigens

Hydrolysis and Formation of Glycosidic Bonds

Contact Info

Product

Resources

About