Human noroviruses recognize sialyl Lewis x neoglycoprotein.

  title={Human noroviruses recognize sialyl Lewis x neoglycoprotein.},
  author={Gustaf E. Rydell and Jonas Nilsson and J{\'e}sus Rodr{\'i}guez-D{\'i}az and Nathalie Ruvoën-Clouet and Lennart Svensson and Jacques Le Pendu and G{\"o}ran Larson},
  volume={19 3},
The carbohydrate binding characteristics of a norovirus GII.3 (Chron1) and a GII.4 (Dijon) strain were investigated using virus-like particles (VLPs) and saliva samples from 81 individuals genotyped for FUT2 (secretor) and FUT3 (Lewis) and phenotyped for ABO and Lewis blood groups. The two VLPs showed a typical secretor-gene-dependent binding and bound significantly stronger to saliva from A, B, and AB than from O individuals (P < 0.0001 and P < 0.001) but did not bind to any samples from… 

Lewis histo-blood group α1,3/α1,4 fucose residues may both mediate binding to GII.4 noroviruses.

This study investigated the possibilities of the Lewis α1,3/α1,4 fucoses as mediators of binding of GII.4 noroviruses to Lewis antigens and suggested the possibility of two receptor binding modes for Lewis HBGAs: the "Secretor pose" and the "Lewis pose".

Crystallography of a Lewis-Binding Norovirus, Elucidation of Strain-Specificity to the Polymorphic Human Histo-Blood Group Antigens

The results elucidate for the first time the genetic and structural basis of strain-specificity by a direct comparison of two genetically related noroviruses in their interaction with different HBGAs and highlight the role of human HBGA as a critical factor in norovirus evolution.

Tulane virus recognizes sialic acids as cellular receptors

Tulane virus (TV), a cultivable primate calicivirus, also recognizes SAs in addition to the previously known TV-HBGA interactions, and Maackia amurensis leukoagglutinin (MAL), a lectin that recognizes the α-2,3 linked SAs, is found, by which MAL promoted TV infectivity in cell culture.

Norovirus, causative agent of winter vomiting disease, exploits several histo-blood group glycans for adhesion

A wide variety of histo-blood group glycoconjugates recognized by human noroviruses are described, suggesting novel approaches for design of glycomimetics for norovirus anti-adhesion therapy.

Norwalk virus-like particles bind specifically to A, H and difucosylated Lewis but not to B histo-blood group active glycosphingolipids

For the first time specific binding of Norwalk virus VLPs to type 1 and type 2 chain glycosphingolipids (GSLs) carrying ABH and Lewis antigens is demonstrated.

Noroviruses and histo‐blood groups: the impact of common host genetic polymorphisms on virus transmission and evolution

Studies of NoV–HBGA interactions together with phylogenetic analyses and the epidemiologic survey of strains indicate that NoV transmission and evolution depend on both the establishment of herd immunity and the genetic resistance of many individuals, which confers herd innate protection by restricting NoV circulation.

Alternative attachment factors and internalization pathways for GIII.2 bovine noroviruses.

Results show that, in addition to a galactosyl residue, sialic acid could also be involved in binding to susceptible cells, and increase the knowledge on bovine norovirus cell interactions.

Glycan Recognition in Human Norovirus Infections

The discovery of HBGAs are described as genetic susceptibility factors for HuNoV infection and the potential for using the HIE model to answer unresolved questions on viral interactions with HBG as well as other glycans is discussed.



Norwalk Virus-Like Particle Hemagglutination by Binding to H Histo-Blood Group Antigens

The discovery that recombinant Norwalk virus virus-like particles (rNV VLPs) agglutinate red blood cells (RBCs) indicates that carbohydrate antigens in the gut are a previously unrecognized factor in NV pathogenesis.

Norwalk virus binds to histo-blood group antigens present on gastroduodenal epithelial cells of secretor individuals☆☆☆

Abstract Background & Aims: Norwalk Virus (NV) is a member of the Caliciviridae family, which causes acute epidemic gastroenteritis in humans of all ages and its cellular receptors have not

Genogroup II Noroviruses Efficiently Bind to Heparan Sulfate Proteoglycan Associated with the Cellular Membrane

The present study found that virus-like particles (VLPs) derived from genogroup II (GII) NV were bound to cell surface heparan sulfate proteoglycan, suggesting that GII NV has two separate binding sites.

Norovirus Capture with Histo-Blood Group Antigens Reveals Novel Virus-Ligand Interactions

Histo-blood group antigen attachment properties of various norovirus strains obtained from clinical stool specimens are characterized, providing the first known observation that one or more components of human feces could promote and enhance norov virus attachment to histo- blood group antigens.

Characterization of sialosylated Lewisx as a new tumor-associated antigen.

Results indicate that the CSLEX1 epitope has the following structure: These results indicate that this structure had not previously been known to be tumor associated.

Alpha2,6-linked sialic acid acts as a receptor for Feline calicivirus.

Using various proteases and metabolic inhibitors, it was shown that alpha2,6-linked sialic acid recognized by FCV is present on an N-linked glycoprotein.

Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity.

Results suggest that the saccharides that MG2 carries could specify some of its important functions, which may include mediating leukocyte interactions in the oral cavity.

Binding of Norwalk Virus-Like Particles to ABH Histo-Blood Group Antigens Is Blocked by Antisera from Infected Human Volunteers or Experimentally Vaccinated Mice

Antisera from NV-infected human volunteers, as well as from mice inoculated with packaged Venezuelan equine encephalitis virus replicons expressing NV VLPs, blocked the ability of NV V LPs to bind synthetic H type 1, Leb, and H type 3, suggesting a potential mechanism for antibody-mediated neutralization of NV.

Functional Adaptation of BabA, the H. pylori ABO Blood Group Antigen Binding Adhesin

It is proposed that cycles of selection for increased and decreased bacterial adherence contribute to babA diversity and that these cycles have led to gradual replacement of generalist binding by specialist binding in blood group O–dominant human populations.

Junctional Adhesion Molecule 1 Is a Functional Receptor for Feline Calicivirus

It is demonstrated that feline JAM-1 is a functional receptor for FCV, simian Jam-1 also functions as a receptor for some strains of FCv, and the interaction between FCV and JAM -1 molecules may be a determinant of viral tropism.