scholarly journals Norovirus GII.17 Virus-Like Particles Bind to Different Histo-Blood Group Antigens and Cross-React with Genogroup II-Specific Mouse Sera

2018 ◽  
Vol 31 (10) ◽  
pp. 649-657 ◽  
Author(s):  
Maria Malm ◽  
Kirsi Tamminen ◽  
Timo Vesikari ◽  
Vesna Blazevic
Keyword(s):  
Blood Group ◽  
Blood Group Antigens ◽  
Virus Like Particles ◽  
Norovirus Gii

The surface-exposed loop region of norovirus GII.3 VP1 plays an essential role in binding histo-blood group antigens

2019 ◽  
Vol 164 (6) ◽  
pp. 1629-1638 ◽  
Author(s):  
Gaobo Zhang ◽  
Jia Wang ◽  
Jinjin Liu ◽  
Lijun Zheng ◽  
Wenhui Wang ◽  
...  
Keyword(s):  
Blood Group ◽  
Essential Role ◽  
Blood Group Antigens ◽  
Loop Region ◽  
Norovirus Gii

scholarly journals Free Chlorine and Peroxynitrite Alter the Capsid Structure of Human Norovirus GII.4 and Its Capacity to Bind Histo-Blood Group Antigens

2021 ◽  
Vol 12 ◽  
Author(s):  
Manon Chassaing ◽  
Guillaume Bastin ◽  
Maëlle Robin ◽  
Didier Majou ◽  
Gaël Belliot ◽  
...  
Keyword(s):  
Blood Group ◽  
Major Capsid Protein ◽  
Free Chlorine ◽  
Blood Group Antigens ◽  
Cross Links ◽  
Two Oxidants ◽  
Capsid Protein Vp1 ◽  
Norovirus Gii ◽  
The Impact ◽  
Natural Life

Human noroviruses (HuNoVs) are one of the leading causes of acute gastroenteritis worldwide. HuNoVs are frequently detected in water and foodstuffs. Free chlorine and peroxynitrite (ONOO−) are two oxidants commonly encountered by HuNoVs in humans or in the environment during their natural life cycle. In this study, we defined the effects of these two oxidants on GII.4 HuNoVs and GII.4 virus-like particles (VLPs). The impact on the capsid structure, the major capsid protein VP1 and the ability of the viral capsid to bind to histo-blood group antigens (HBGAs) following oxidative treatments were analyzed. HBGAs are attachment factors that promote HuNoV infection in human hosts. Overall, our results indicate that free chlorine acts on regions involved in the stabilization of VP1 dimers in VLPs and affects their ability to bind to HBGAs. These effects were confirmed in purified HuNoVs. Some VP1 cross-links also take place after free chlorine treatment, albeit to a lesser extent. Not only ONOO− mainly produced VP1 cross-links but can also dissociate VLPs depending on the concentration applied. Nevertheless, ONOO− has less effect on HuNoV particles.

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.

Enzymatic cleavage promotes disassembly of GII.3 norovirus virus like particles and its binding to salivary histo-blood group antigens

2017 ◽  
Vol 240 ◽  
pp. 18-24 ◽  
Author(s):  
Yuqi Huo ◽  
Wenhui Wang ◽  
Lijun Zheng ◽  
Xuhui Chen ◽  
Shuo Shen ◽  
...  
Keyword(s):  
Blood Group ◽  
Blood Group Antigens ◽  
Enzymatic Cleavage ◽  
Virus Like Particles

scholarly journals The effect of proteolytic enzymes and pH on GII.4 norovirus, during both interactions and non-interaction with Histo-Blood Group Antigens

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Manon Chassaing ◽  
Maëlle Robin ◽  
Julie Loutreul ◽  
Didier Majou ◽  
Gaël Belliot ◽  
...  
Keyword(s):  
Blood Group ◽  
Acute Gastroenteritis ◽  
Digestive System ◽  
Proteolytic Enzymes ◽  
Blood Groups ◽  
Blood Group Antigens ◽  
Human Noroviruses ◽  
Virus Like Particles ◽  
Acid Ph ◽  
Human Digestive System

Abstract Human noroviruses (HuNoVs) are the leading cause of acute gastroenteritis worldwide. Histo-Blood Groups Antigens (HBGAs) have been described as attachment factors, promoting HuNoV infection. However, their role has not yet been elucidated. This study aims to evaluate the ability of HBGAs to protect HuNoVs against various factors naturally found in the human digestive system. The effects of acid pH and proteolytic enzymes (pepsin, trypsin, and chymotrypsin) on GII.4 virus-like particles (VLPs) and GII.4 HuNoVs were studied, both during interactions and non-interaction with HBGAs. The results showed that GII.4 VLPs and GII.4 HuNoVs behaved differently following the treatments. GII.4 VLPs were disrupted at a pH of less than 2.0 and in the presence of proteolytic enzymes (1,500 units/mL pepsin, 100 mg/mL trypsin, and 100 mg/mL chymotrypsin). VLPs were also partially damaged by lower concentrations of trypsin and chymotrypsin (0.1 mg/mL). Conversely, the capsids of GII.4 HuNoVs were not compromised by such treatments, since their genomes were not accessible to RNase. HBGAs were found to offer GII.4 VLPs no protection against an acid pH or proteolytic enzymes.

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

2002 ◽  
Vol 76 (23) ◽  
pp. 12335-12343 ◽  
Author(s):  
Patrick R. Harrington ◽  
Lisa Lindesmith ◽  
Boyd Yount ◽  
Christine L. Moe ◽  
Ralph S. Baric
Keyword(s):  
Blood Group ◽  
Human Saliva ◽  
Blood Group Antigens ◽  
Norwalk Virus ◽  
Venezuelan Equine Encephalitis ◽  
Virus Like Particles ◽  
Equine Encephalitis Virus ◽  
Human Volunteers ◽  
Type 3

ABSTRACT Attachment of Norwalk (NV), Snow Mountain (SMV), and Hawaii (HV) virus-like particles (VLPs) to specific ABH histo-blood group antigens was investigated by using human saliva and synthetic biotinylated carbohydrates. The three distinct Norwalk-like viruses (NLVs) have various capacities for binding ABH histo-blood group antigens, suggesting that different mechanisms for NLV attachment likely exist. Importantly, 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 VLPs to bind synthetic H type 1, Leb, and H type 3, suggesting a potential mechanism for antibody-mediated neutralization of NV.

scholarly journals The role of sialic acid in the expression of human MN blood group antigens.

1979 ◽  
Vol 254 (6) ◽  
pp. 2112-2119 ◽  
Author(s):  
J.E. Sadler ◽  
J.C. Paulson ◽  
R.L. Hill
Keyword(s):  
Sialic Acid ◽  
Blood Group ◽  
Blood Group Antigens ◽  
Mn Blood Group
Sign in / Sign up

Export Citation Format

Share Document