scholarly journals A plate-based histo-blood group antigen binding assay for evaluation of human norovirus receptor binding ability

2017 ◽  
Vol 533 ◽  
pp. 56-59 ◽  
Author(s):  
Matthew D. Moore ◽  
Lee-Ann Jaykus
Keyword(s):  
Blood Group ◽  
Receptor Binding ◽  
Binding Assay ◽  
Blood Group Antigen ◽  
Antigen Binding ◽  
Human Norovirus ◽  
Binding Ability

scholarly journals The P Domain of Norovirus Capsid Protein Forms a Subviral Particle That Binds to Histo-Blood Group Antigen Receptors

2005 ◽  
Vol 79 (22) ◽  
pp. 14017-14030 ◽  
Author(s):  
Ming Tan ◽  
Xi Jiang
Keyword(s):  
Blood Group ◽  
Receptor Binding ◽  
Vaccine Development ◽  
Human Colon ◽  
Blood Group Antigen ◽  
Antigen Receptors ◽  
Human Colon Carcinoma Cell ◽  
Strong Binding ◽  
Internal Core ◽  
P Domain

ABSTRACT Norovirus is the most important cause of nonbacterial acute gastroenteritis. We have shown previously that the isolated P domain containing the hinge forms a dimer and binds to histo-blood group antigen (HBGA) receptors with a low affinity (M. Tan, R. S. Hegde, and X. Jiang, J. Virol. 78:6233-6242, 2004). Here, we reported that the P domain of VA387 without the hinge forms a small particle with a significantly increased receptor binding affinity. An end-linked oligopeptide containing one or more cysteines promoted P-particle formation by forming intermolecular disulfide bridges. The binding sensitivity of the P particle to HBGAs was enhanced >700-fold compared to the P dimer, which was comparable to that of virus-like particles. The binding specificity of the P particle was further confirmed by strong binding to the Caco-2 cells, a human colon carcinoma cell line. This binding enhancement was observed in the P particles of both norovirus GI and GII strains. The P particle is estimated to contain 12 P dimers, in which the P2 subdomain builds up the outer layer, while the P1 subdomain forms the internal core. Taken together, our data indicate that the P domain is involved not only in dimerization but also in polymerization of the protein during the capsid assembling. The enhanced receptor binding of the P particle reflects the intrinsic feature of the viral capsid. The easy production of the P particle and its strong binding to HBGAs suggest that the P particle is useful in studying pathogenesis and morphogenesis of norovirus and candidates for antiviral or vaccine development.

Blood group antigen-Binding Adhesion2 (BabA2) gene in gastric tissue biopsies as a diagnostic biomarker for Helicobacter pylori infection

2019 ◽  
Vol 27 (3) ◽  
pp. 193-199 ◽  
Author(s):  
Ashraf A. Hassan ◽  
Amany I. Youssef ◽  
Abeer A. Ghazal ◽  
Manal I. Sheta ◽  
Nabil L. Diwedar ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Blood Group ◽  
Blood Group Antigen ◽  
Helicobacter Pylori Infection ◽  
Antigen Binding ◽  
Gastric Tissue ◽  
Diagnostic Biomarker

Characterization of a Histo-Blood Group Antigen-like Substance in Romaine Lettuce That Contributes to Human Norovirus Attachment

2019 ◽  
Vol 68 (5) ◽  
pp. 1207-1212 ◽  
Author(s):  
Zilei Zhang ◽  
Danlei Liu ◽  
Qingping Wu ◽  
Yu Lu ◽  
Peng Tian ◽  
...  
Keyword(s):  
Blood Group ◽  
Blood Group Antigen ◽  
Romaine Lettuce ◽  
Human Norovirus

scholarly journals Structural Analysis of Determinants of Histo-Blood Group Antigen Binding Specificity in Genogroup I Noroviruses

2014 ◽  
Vol 88 (11) ◽  
pp. 6168-6180 ◽  
Author(s):  
S. Shanker ◽  
R. Czako ◽  
B. Sankaran ◽  
R. L. Atmar ◽  
M. K. Estes ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Blood Group ◽  
Binding Specificity ◽  
Blood Group Antigen ◽  
Antigen Binding

scholarly journals Histo-blood group antigen-binding specificities of human rotaviruses are associated with gastroenteritis but not with in vitro infection

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Laure Barbé ◽  
Béatrice Le Moullac-Vaidye ◽  
Klara Echasserieau ◽  
Karine Bernardeau ◽  
Thomas Carton ◽  
...  
Keyword(s):  
Blood Group ◽  
Blood Group Antigen ◽  
Antigen Binding

scholarly journals Helicobacter Pylori: How is Adhesin BabA, a Blood Group Antigen Binding Membrane Protein, Involved in Bacterial Adherence?

2009 ◽  
Vol 96 (3) ◽  
pp. 409a ◽  
Author(s):  
Katja Petzold ◽  
Annelie Olofsson ◽  
Anna Arnqvist ◽  
Thomas Boren ◽  
Gerhard Gröbner ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Membrane Protein ◽  
Blood Group ◽  
Blood Group Antigen ◽  
Bacterial Adherence ◽  
Antigen Binding

scholarly journals Comprehensive analysis of blood group antigen binding to classical and El Tor cholera toxin B-pentamers by NMR

Glycobiology ◽  
2014 ◽  
Vol 24 (8) ◽  
pp. 766-778 ◽  
Author(s):  
Francesca Vasile ◽  
José J Reina ◽  
Donatella Potenza ◽  
Julie E Heggelund ◽  
Alasdair Mackenzie ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
Blood Group ◽  
Comprehensive Analysis ◽  
Blood Group Antigen ◽  
Antigen Binding ◽  
Toxin B ◽  
Cholera Toxin B ◽  
El Tor

scholarly journals Human Norovirus Histo-Blood Group Antigen (HBGA) Binding Sites Mediate the Virus Specific Interactions with Lettuce Carbohydrates

Viruses ◽  
2019 ◽  
Vol 11 (9) ◽  
pp. 833
Author(s):  
Malak A. Esseili ◽  
Xiang Gao ◽  
Patricia Boley ◽  
Yixuan Hou ◽  
Linda J. Saif ◽  
...  
Keyword(s):  
Blood Group ◽  
Binding Sites ◽  
Specific Binding ◽  
Blood Group Antigen ◽  
Blood Group Antigens ◽  
Specific Interactions ◽  
Wild Type ◽  
Human Norovirus ◽  
Virus Like Particles ◽  
Foodborne Outbreaks

Lettuce is often implicated in human norovirus (HuNoV) foodborne outbreaks. We identified H-like histo-blood group antigens (HBGAs) on lettuce leaves as specific binding moieties for virus-like particles (VLPs) of HuNoV GII.4/HS194/2009 strain. The objective of this study was to determine whether HuNoV-lettuce binding is mediated through the virus HBGA binding sites (HBS). Toward this objective, VLPs of historical HuNoV GII.4 strains (1987, 1997, 2002, 2004 and 2006) with known natural mutations in their HBS, two newly generated VLP mutants of GII.4/HS194/2009 (D374A and G443A) and a VLP mutant (W375A) of GI.1/Norwalk/1968 along with its wild type VLPs, which displays distinct HBS, were investigated for their binding to lettuce. ELISA revealed that historical GII.4 strains binding to lettuce was dependent on their HBGAs profiles. The VLP mutants D374A and G443A lost binding to HBGAs and displayed no to minimal binding to lettuce, respectively. The VLPs of GI.1/Norwalk/1968 strain bound to lettuce through an H-like HBGA and the binding was inhibited by fucosidase digestion. Mutant W375A which was previously shown not to bind to HBGAs, displayed significantly reduced binding to lettuce. We conclude that the binding of HuNoV GII.4 and GI.1 strains to lettuce is mediated through the virus HBS.

scholarly journals Atomic force microscopy measurements reveal multiple bonds between Helicobacter pylori blood group antigen binding adhesin and Lewis b ligand

2014 ◽  
Vol 11 (101) ◽  
pp. 20141040 ◽  
Author(s):  
P. Parreira ◽  
Q. Shi ◽  
A. Magalhaes ◽  
C. A. Reis ◽  
J. Bugaytsova ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Helicobacter Pylori ◽  
Blood Group ◽  
Blood Group Antigen ◽  
Antigen Binding ◽  
Dynamic Force ◽  
Force Microscopy ◽  
Single Receptor ◽  
Atomic Force ◽  
Assembled Monolayers

The strength of binding between the Helicobacter pylori blood group antigen-binding adhesin (BabA) and its cognate glycan receptor, the Lewis b blood group antigen (Le b ), was measured by means of atomic force microscopy. High-resolution measurements of rupture forces between single receptor–ligand pairs were performed between the purified BabA and immobilized Le b structures on self-assembled monolayers. Dynamic force spectroscopy revealed two similar but statistically different bond populations. These findings suggest that the BabA may form different adhesive attachments to the gastric mucosa in ways that enhance the efficiency and stability of bacterial adhesion.

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