Association between circulating rotavirus genotypes and histo‐blood group antigens in the children hospitalized with acute gastroenteritis in Iran

2021 ◽  
Author(s):  
Mohammad Farahmand ◽  
Somayeh Jalilvand ◽  
Arash Arashkia ◽  
Shohreh Shahmahmoodi ◽  
Atefeh Afchangi ◽  
...  
Keyword(s):  
Blood Group ◽  
Acute Gastroenteritis ◽  
Blood Group Antigens

scholarly journals Norovirus and Histo-Blood Group Antigens: Demonstration of a Wide Spectrum of Strain Specificities and Classification of Two Major Binding Groups among Multiple Binding Patterns

2005 ◽  
Vol 79 (11) ◽  
pp. 6714-6722 ◽  
Author(s):  
Pengwei Huang ◽  
Tibor Farkas ◽  
Weiming Zhong ◽  
Ming Tan ◽  
Scott Thornton ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Blood Group ◽  
Acute Gastroenteritis ◽  
Specific Binding ◽  
Wide Spectrum ◽  
Phylogenetic Analyses ◽  
Lewis Antigens ◽  
Blood Group Antigens ◽  
Multiple Binding

ABSTRACT Noroviruses, an important cause of acute gastroenteritis, have been found to recognize human histo-blood group antigens (HBGAs) as receptors. Four strain-specific binding patterns to HBGAs have been described in our previous report. In this study, we have extended the binding patterns to seven based on 14 noroviruses examined. The oligosaccharide-based assays revealed additional epitopes that were not detected by the saliva-based assays. The seven patterns have been classified into two groups according to their interactions with three major epitopes (A/B, H, and Lewis) of human HBGAs: the A/B-binding group and the Lewis-binding group. Strains in the A/B binding group recognize the A and/or B and H antigens, but not the Lewis antigens, while strains in the Lewis-binding group react only to the Lewis and/or H antigens. This classification also resulted in a model of the norovirus/HBGA interaction. Phylogenetic analyses showed that strains with identical or closely related binding patterns tend to be clustered, but strains in both binding group can be found in both genogroups I and II. Our results suggest that noroviruses have a wide spectrum of host range and that human HBGAs play an important role in norovirus evolution. The high polymorphism of the human HBGA system, the involvement of multiple epitopes, and the typical protein/carbohydrate interaction between norovirus VLPs and HBGAs provide an explanation for the virus-ligand binding diversities.

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 Bovine Nebovirus Interacts with a Wide Spectrum of Histo-Blood Group Antigens

2018 ◽  
Vol 92 (9) ◽  
Author(s):  
Eun-Hyo Cho ◽  
Mahmoud Soliman ◽  
Mia Madel Alfajaro ◽  
Ji-Yun Kim ◽  
Ja-Young Seo ◽  
...  
Keyword(s):  
Cell Surface ◽  
Blood Group ◽  
Host Species ◽  
Acute Gastroenteritis ◽  
Wide Spectrum ◽  
Human Saliva ◽  
Mammalian Host ◽  
Blood Group Antigens ◽  
Cell Surface Carbohydrate ◽  
Enteric Caliciviruses

ABSTRACTSome viruses within theCaliciviridaefamily initiate their replication cycle by attachment to cell surface carbohydrate moieties, histo-blood group antigens (HBGAs), and/or terminal sialic acids (SAs). Although bovine nebovirus (BNeV), one of the enteric caliciviruses, is an important causative agent of acute gastroenteritis in cattle, its attachment factors and possibly other cellular receptors remain unknown. Using a comprehensive series of protein-ligand biochemical assays, we sought to determine whether BNeV recognizes cell surface HBGAs and/or SAs as attachment factors. It was found that BNeV virus-like particles (VLPs) bound to A type/H type 2/LeyHBGAs expressed in the bovine digestive tract and are related to HBGAs expressed in humans and other host species, suggesting a wide spectrum of HBGA recognition by BNeV. BNeV VLPs also bound to a large variety of different bovine and human saliva samples of all ABH and Lewis types, supporting previously obtained results and suggesting a zoonotic potential of BNeV transmission. Removal of α1,2-linked fucose and α1,3/4-linked fucose epitopes of target HBGAs by confirmation-specific enzymes reduced the binding of BNeV VLPs to synthetic HBGAs, bovine and human saliva, cultured cell lines, and bovine small intestine mucosa, further supporting a wide HBGA binding spectrum of BNeV through recognition of α1,2-linked fucose and α1,3/4-linked fucose epitopes of targeted HBGAs. However, removal of terminal α2,3- and α2,6-linked SAs by their specific enzyme had no inhibitory effects on binding of BNeV VLPs, indicating that BNeV does not use terminal SAs as attachment factors. Further details of the binding specificity of BNeV remain to be explored.IMPORTANCEEnteric caliciviruses such as noroviruses, sapoviruses, and recoviruses are the most important etiological agents of severe acute gastroenteritis in humans and many other mammalian host species. They initiate infection by attachment to cell surface carbohydrate moieties, HBGAs, and/or terminal SAs. However, the attachment factor(s) for BNeV, a recently classified enteric calicivirus genus/type species, remains unexplored. Here, we demonstrate that BNeV VLPs have a wide spectrum of binding to synthetic HBGAs, bovine and human saliva samples, and bovine duodenal sections. We further discovered that α1,2-linked fucose and α1,3/4-linked fucose epitopes are essential for binding of BNeV VLPs. However, BNeV VLPs do not bind to terminal SAs on cell carbohydrates. Continued investigation regarding the proteinaceous receptor(s) will be necessary for better understanding of the tropism, pathogenesis, and host range of this important viral genus.

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

Primate genes for glycophorins carrying MN blood group antigens

1993 ◽  
Vol 22 (1) ◽  
pp. 7-12
Author(s):  
Shinichi Kudo ◽  
Masaaki Onda ◽  
Ann Rearden ◽  
Minoru Fukuda
Keyword(s):  
Blood Group ◽  
Blood Group Antigens ◽  
Mn Blood Group

Depressed blood group antigens on red cells from a Mexican donor

Transfusion ◽  
1983 ◽  
Vol 23 (1) ◽  
pp. 65-66 ◽  
Author(s):  
V Biro ◽  
G Garratty ◽  
CL Johnson ◽  
WL Marsh
Keyword(s):  
Blood Group ◽  
Red Cells ◽  
Blood Group Antigens

HLA and red blood group antigens in pregnancy disorders

1988 ◽  
Vol 32 (3) ◽  
pp. 130-138 ◽  
Author(s):  
M. Gerenčer ◽  
Z. Singer ◽  
S. Pfeifer ◽  
M. Tomaškovi ◽  
I. Humar ◽  
...  
Keyword(s):  
Blood Group ◽  
Blood Group Antigens ◽  
In Pregnancy ◽  
Pregnancy Disorders
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