Synthesis of complex α2-3 sialooligosaccharides, including sulfated and fucosylated ones, using Neu5Acα2-3Gal as a building block

Pazynina, Galina V.; Sablina, Marina A.; Tuzikov, Alexander; Chinarev, Alexander; Bovin, Nicolai V.

doi:10.1070/mc2003v013n06abeh001845

Cited by 24 publications

(9 citation statements)

References 12 publications

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“…The use of an aminoreactive NHS-activated microglass surface allows covalent attachment of glycans containing a terminal amine by forming an amide bond under aqueous conditions at room temperature. The compound library of 200 glycoconjugates comprises diverse and biologically relevant structures representing terminal sequences of glycoprotein and glycolipid glycans (see Methods and Supporting Methods) l (22)(23)(24)(25)(26)35). Glycan structures detected by GBPs analyzed in this article are listed in Fig.…”

Section: Resultsmentioning

confidence: 99%

Printed covalent glycan array for ligand profiling of diverse glycan binding proteins

Blixt

Head

Mondala

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

1,031

970

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Here we describe a glycan microarray constructed by using standard robotic microarray printing technology to couple amine functionalized glycans to an amino-reactive glass slide. The array comprises 200 synthetic and natural glycan sequences representing major glycan structures of glycoproteins and glycolipids. The array has remarkable utility for profiling the specificity of a diverse range of glycan binding proteins, including C-type lectins, siglecs, galectins, anticarbohydrate antibodies, lectins from plants and microbes, and intact viruses.carbohydrate ͉ lectin ͉ microarray ͉ glycoprotein ͉ glycolipid

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Section: Resultsmentioning

confidence: 99%

Printed covalent glycan array for ligand profiling of diverse glycan binding proteins

Blixt

Head

Mondala

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

1,031

970

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“…#2595) were purchased from Corning. Synthesis of 4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diazas-indacene-3-propionic acid (BODIPY)-labeled and polyacrylamide-coupled oligosaccharides was described earlier [18,20,21,27].…”

Section: Methodsmentioning

confidence: 99%

Adjustment of receptor-binding and neuraminidase substrate specificties in avian–human reassortant influenza viruses

et al. 2008

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Balanced action of hemagglutinin (HA) and neuraminidase (NA) is an important condition of influenza virus efficient replication, but a role of HA and NA specificities at oligosaccharide level in maintaining such a balance remains poorly studied. Avian virus HA binds exclusively and NA digests efficiently alpha2-3-sialylated carbohydrate chains, while human virus HA interacts with alpha2-6 chains and low-active NA cleaves both alpha2-3- and alpha2-6-sialosides. Reassortment between viruses leading to appearance of avian virus HA and human virus NA on the virion surface often resulted in decreasing the replicative potential of the formed variants because of disturbance of a functional balance between "alien" HA and NA. A restoration of the reassortant productivity happened due to the appearance of amino acid substitutions in HA and, sometimes, NA. Here, a role of NA and HA oligosaccharide specificities in a restoration of HA-NA functional balance in high-yield passage variants was studied. Postreassortment changes in HA receptor-binding and NA substrate specificities for three reassortant/passage variant virus pairs towards 3'SiaLac, 3'SiaLacNAc, SiaLe(c), SiaLe(a), SiaLe(x), 6'SiaLac, and 6'SiaLacNAc were determined. Selection of the high-yield variants of the human-avian reassortants led either to twofold decrease in the affinity of HA for most alpha2-3-sialosides and the appearance of affinity for alpha2-6-sialosides (H3N2 reassortant), or to decreasing the HA affinity for SiaLe(c) and SiaLe(a) (H3N1 reassortant), or to enhancing the ability of NA to discriminate between alpha2-3/2-6 substrates (H4N1 reassortant). Thus, all postreassortment changes in oligosaccharide specificities of "alien" HA and NA were directed towards their adjustment to each other, but by different manner.

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“…High-molecular-mass (ϳ1,000 kDa) biotinylated sialylglycopolymers (SGPs), which are analogs of natural influenza virus receptors (43,44), and SGPs with -aminoglycoside spacers and boron-dipyrromethene (BODIPY)-labeled SGPs were synthesized as described previously (45,46,47,48). The structures and designations of their oligosaccharide moieties are presented in Fig.…”

Section: Methodsmentioning

confidence: 99%

Alterations in Hemagglutinin Receptor-Binding Specificity Accompany the Emergence of Highly Pathogenic Avian Influenza Viruses

Heider

Mochalova

Harder

et al. 2015

J Virol

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Highly pathogenic avian influenza viruses (HPAIVs) of hemagglutinin H5 and H7 subtypes emerge after introduction of lowpathogenic avian influenza viruses (LPAIVs) from wild birds into poultry flocks, followed by subsequent circulation and evolution. The acquisition of multiple basic amino acids at the endoproteolytical cleavage site of the hemagglutinin (HA) is a molecular indicator for high pathogenicity, at least for infections of gallinaceous poultry. Apart from the well-studied significance of the multibasic HA cleavage site, there is only limited knowledge on other alterations in the HA and neuraminidase (NA) molecules associated with changes in tropism during the emergence of HPAIVs from LPAIVs. We hypothesized that changes in tropism may require alterations of the sialyloligosaccharide specificities of HA and NA. To test this hypothesis, we compared a number of LPAIVs and HPAIVs for their HA-mediated binding and NA-mediated desialylation of a set of synthetic receptor analogs, namely, ␣2-3-sialylated oligosaccharides. NA substrate specificity correlated with structural groups of NAs and did not correlate with pathogenic potential of the virus. In contrast, all HPAIVs differed from LPAIVs by a higher HA receptor-binding affinity toward the trisaccharides Neu5Ac␣2-3Gal␤1-4GlcNAc␤ (3=SLN) and Neu5Ac␣2-3Gal␤1-3GlcNAc␤ (SiaLe c ) and by the ability to discriminate between the nonfucosylated and fucosylated sialyloligosaccharides 3=SLN and Neu5Ac␣2-3Gal␤1-4(Fuc␣1-3)GlcNAc␤ (SiaLe x ), respectively. These results suggest that alteration of the receptor-binding specificity accompanies emergence of the HPAIVs from their low-pathogenic precursors. A vian influenza is a highly contagious infection with influenza A viruses, with a worldwide occurrence in aquatic wild bird populations which represent the major natural hosts of these viruses. Influenza A viruses are classified into subtypes according to their surface glycoproteins: 18 hemagglutinin (HA) and 11 neuraminidase (NA) antigenic subtypes have been identified (1, 2, 3). Avian influenza viruses (AIVs) are subdivided into groups of high and low pathogenicity. The presence of multiple basic amino acids at the endoproteolytical cleavage site of the HA is a molecular indicator for high pathogenicity, at least for infections of gallinaceous poultry (4,5,6,7,8). Influenza viruses of HA subtypes H5, H7, and H9 are commonly identified in terrestrial gallinaceous poultry (9, 10). Only low-pathogenic AIVs (LPAIVs) of subtypes H5 and H7 naturally evolve into highly pathogenic AIVs (HPAIVs), which cause severe infections with high rates of mortality in poultry (11,12,13,14) and can also be transmitted from birds to humans (15,16,17,18).The two viral glycoproteins, HA and NA, expressed on the surface of influenza virions play an important role in determining the pathogenic properties of the virus. Influenza virus infection is initiated by interactions between the viral HA and sialic acid-containing oligosaccharides on target cells. The NA cleaves off the terminal si...

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Synthesis of complex α2-3 sialooligosaccharides, including sulfated and fucosylated ones, using Neu5Acα2-3Gal as a building block

Cited by 24 publications

References 12 publications

Printed covalent glycan array for ligand profiling of diverse glycan binding proteins

Printed covalent glycan array for ligand profiling of diverse glycan binding proteins

Adjustment of receptor-binding and neuraminidase substrate specificties in avian–human reassortant influenza viruses

Alterations in Hemagglutinin Receptor-Binding Specificity Accompany the Emergence of Highly Pathogenic Avian Influenza Viruses

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