High molecular weight neoglycoconjugates for solid phase assays

Шилова, Н. В.; Galanina, Oxana; Pochechueva, Tatiana; Chinarev, Alexander; Kadykov, Vasily A.; Tuzikov, Alexander; Bovin, Nicolai V.

doi:10.1007/s10719-005-0280-y

Cited by 26 publications

(25 citation statements)

References 16 publications

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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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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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“…Thirty-kilodalton label-free and biotinylated conjugates were obtained as described previously (Bovin et al, 1993) by coupling aminopropyl glycosides to poly(4-nitrophenyl acrylate) followed by quenching of the polymer active groups with ethanolamine. The 2000-kDa polymers were obtained similarly starting from poly(4-N-hydroxysuccinimidyl acrylate) (Shilova et al, 2005). Spacerarmed tetrasaccharides 6Ј-sulfo-sLe x , sLe x , and 3Ј-sulfo-sLe x were synthesized as described previously (Zemlyanukhina et al, 1995;Pazynina et al, 2003; G. V. Pazynina, V. Severov, M. L. Maisel, I. M. Belyanchikov, and N. V. Bovin, submitted for publication).…”

Section: Methodsmentioning

confidence: 99%

Eosinophil-Selective Binding and Proapoptotic Effect in Vitro of a Synthetic Siglec-8 Ligand, Polymeric 6′-Sulfated Sialyl Lewis X

Hudson¹,

Bovin²,

Schnaar³

et al. 2009

J Pharmacol Exp Ther

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“…Biotinylated low-molecular-mass (30 kDa) sialoside-polyacrylamide (PAA) conjugates bearing Neu5Ac␣2-3[6-SO 4 ]Gal␤1-4[Fuc␣1-3]GlcNAc (6Ј-sulfo-sLe X ) or 9-biphenylcarbonyl (BPC)-Neu5Ac␣2-6Gal␤1-4GlcNAc were synthesized by coupling spacered oligosaccharides and spacered biotin to poly (4-nitrophenyl acrylate) as described previously (16) Biotinylated high-molecular-mass (1,000 kDa) PAA conjugates were synthesized by coupling spacered oligosaccharides and spacered biotin to poly (N-oxysuccinimide acrylate) as described previously (67); the 1,000-kDa lactose conjugate was obtained from The Consortium for Functional Glycomics.…”

Section: Methodsmentioning

confidence: 99%

Distinct Endocytic Mechanisms of CD22 (Siglec-2) and Siglec-F Reflect Roles in Cell Signaling and Innate Immunity

Tateno

Schur

et al. 2007

Molecular and Cellular Biology

116

109

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Sialic acid-binding immunoglobulin-like lectins (siglecs) are predominately expressed on immune cells. They are best known as regulators of cell signaling mediated by cytoplasmic tyrosine motifs and are increasingly recognized as receptors for pathogens that bear sialic acid-containing glycans. Most siglec proteins undergo endocytosis, an activity tied to their roles in cell signaling and innate immunity. Here, we investigate the endocytic pathways of two siglec proteins, CD22 (Siglec-2), a regulator of B-cell signaling, and mouse eosinophil Siglec-F, a member of the rapidly evolving CD33-related siglec subfamily that are expressed on cells of the innate immune system. CD22 exhibits hallmarks of clathrin-mediated endocytosis and traffics to recycling compartments, consistent with previous reports demonstrating its localization to clathrin domains. Like CD22, Siglec-F mediates endocytosis of anti-Siglec-F and sialoside ligands, a function requiring intact tyrosinebased motifs. In contrast, however, we find that Siglec-F endocytosis is clathrin and dynamin independent, requires ADP ribosylation factor 6, and traffics to lysosomes. The results suggest that these two siglec proteins have evolved distinct endocytic mechanisms consistent with roles in cell signaling and innate immunity.The siglec (sialic-acid binding immunoglobulin [Ig]-like lectins) proteins are subset of the Ig superfamily of cell recognition molecules that bind to sialic acid-containing glycans of cell surface glycoconjugates as ligands (27,78). Of the 13 human and 9 murine siglec proteins, 4 are highly conserved in mammalian species: sialoadhesin (Sn)/Siglec-1, CD22/Siglec-2, myelin-associated glycoprotein (MAG)/Siglec-4, and Siglec-15. The others comprise a rapidly evolving subfamily homologous to CD33/Siglec-4, known as the CD33-related siglec proteins. With two exceptions (MAG and Siglec-6) the siglec proteins are predominantly expressed in various white blood cells of the immune system (25,43,78,85). All contain a N-terminal V-set sugar-binding Ig domain, a variable number of additional C-set Ig domains, a transmembrane domain, and a cytoplasmic domain that typically contains tyrosine-based motifs implicated in regulation of cell signaling and endocytosis.Many of the siglec proteins contain one or more immunoreceptor tyrosine-based inhibitory motifs (ITIMs), (I/L/V)XYXX (L/V), suggesting that they play important roles as inhibitory receptors of cell signaling (25, 78), as exemplified by CD22, which is well documented as a regulator of B-cell receptor (BCR) signaling. Upon antigen binding to the BCR, the ITIMs of CD22 are quickly tyrosine phosphorylated and recruit protein tyrosine phosphatase SHP-1, which dephosphorylates the BCR and dampens the B-cell response, setting a threshold for B-cell activation (27,73).CD22 is also known to undergo endocytosis following ligation by anti-CD22 antibody (38, 64) or high-affinity multivalent-sialoside ligands (22). The tyrosine-based ITIMs of CD22 also fit the sorting signal YXXØ (where Ø is a hydrophobic...

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High molecular weight neoglycoconjugates for solid phase assays

Cited by 26 publications

References 16 publications

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

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

Eosinophil-Selective Binding and Proapoptotic Effect in Vitro of a Synthetic Siglec-8 Ligand, Polymeric 6′-Sulfated Sialyl Lewis X

Distinct Endocytic Mechanisms of CD22 (Siglec-2) and Siglec-F Reflect Roles in Cell Signaling and Innate Immunity

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