Presence and Distribution of Histo-Blood Group Antigens in Pacific Oysters and the Effects of Exposure to Noroviruses GI.3 and GII.4 on Their Expression

2018 ◽  
Vol 81 (11) ◽  
pp. 1783-1790
Author(s):  
LAIJIN SU ◽  
LIPING MA ◽  
HUI LIU ◽  
FENG ZHAO ◽  
ZHIWEI SU ◽  
...  
Keyword(s):  
Blood Group ◽  
Blood Group Antigens ◽  
Genotype 3 ◽  
Lewis X ◽  
Viral Pathogens ◽  
Genotype 4 ◽  
Republic Of China ◽  
Reverse Transcription Pcr ◽  
Pacific Oysters ◽  
Different Tissues

ABSTRACT Noroviruses (NoVs) are one of the most important foodborne viral pathogens worldwide. Oysters are common carriers of NoVs and are responsible for their transmission. NoVs recognize human histo-blood group antigens (HBGAs) as receptors. Recent studies indicate that HBGA-like molecules also exist in oyster tissues and that they may play a key role in the binding of NoVs. However, the mechanism by which different genotypes of NoV accumulate in different oyster tissues is unknown. In this study, the presence and distribution of different types of HBGA-like molecules were evaluated in 240 oysters collected from the Shandong Peninsula of People's Republic of China for 1 year. The HBGA-like molecules were detected at various rates and expressed at different levels in different tissues. Immunohistochemistry confirmed the diversity of HBGA-like molecules in four oyster tissues. Eight types of HBGA-like molecules (types A, B, H1, Lewis x, Lewis y, Lewis a, Lewis b, and precursor) were assessed in different tissues. Of these, the type A HBGA-like molecule was consistently expressed in the gills, digestive tissue, and mantle, while types H1 and Lewis b HBGA-like molecules were expressed in the digestive tissues. The expression of HBGA-like molecules in response to the NoV challenge was investigated. The levels of types A, H1, and Lewis x increased significantly in specific oyster tissues after exposure to genogroup II, genotype 4 (GII.4) or genogroup I, genotype 3 (GI.3) NoV. The real-time reverse transcription PCR assays indicated that GI.3 NoV mainly accumulated in the digestive tissues of oysters, whereas GII.4 NoV accumulated in the gills, mantle, and digestive tissues. These results provide new insights into the mechanism of NoV bioaccumulation in oysters and suggest that NoV accumulation in oysters may be related to the expression of HBGA-like molecules.

Seasonal Tracking of Histo-Blood Group Antigen Expression and Norovirus Binding in Oyster Gastrointestinal Cells

2008 ◽  
Vol 71 (8) ◽  
pp. 1696-1700 ◽  
Author(s):  
PENG TIAN ◽  
ANNA L. ENGELBREKTSON ◽  
ROBERT E. MANDRELL
Keyword(s):  
Blood Group ◽  
Seasonal Pattern ◽  
Antigen Expression ◽  
Blood Group Antigen ◽  
Viral Gastroenteritis ◽  
Blood Group Antigens ◽  
Pacific Oysters ◽  
Crassostrea Sikamea ◽  
Highly Correlated ◽  
Viral Receptors

Noroviruses (NORs) are the most common cause of viral gastroenteritis outbreaks. Outbreaks are often associated with the consumption of contaminated oysters and generally occur between the months of November and March, when oysters produce the highest levels of glycogen. Oyster glycogen has been proposed as playing a role in NOR accumulation. Recent research indicates that histo-blood group antigens (HBGAs) function as viral receptors on human gastrointestinal cells. In this study, oyster glycogen was tested to determine whether it contains HBGA-like molecules and whether it plays a role in NOR binding. The correlation between the amount of HBGA expression and NOR binding also was measured. We also tested whether seasonal changes affected HBGA expression and binding of recombinant NORs. The results indicate that recombinant NOR binding is highly correlated with HBGA expression in Virginica (Crassostrea virginica), Pacific (Crassostrea gigas), and Kumamato (Crassostrea sikamea) oysters, but the association does not have a seasonal pattern. No obvious trend in either HBGA expression or recombinant NOR binding by month was noted. A significant increase in recombinant NOR binding was observed in Virginica and Pacific oysters in a season not generally associated with NOR gastroenteritis outbreaks. A significant increase in HBGA expression also was observed for Pacific and Virginica oysters in the same season. Paradoxically, HBGA expression and NOR binding both were higher in oysters produced in the non–NOR gastroenteritis season (April through October) than in those produced in the NOR gastroenteritis season (November through March), suggesting that seasonal NOR gastroenteritis outbreaks are not associated with high levels of HBGA expression or NOR binding.

scholarly journals Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens

mSphere ◽  
2016 ◽  
Vol 1 (2) ◽  
Author(s):  
Bishal K. Singh ◽  
Mila M. Leuthold ◽  
Grant S. Hansman
Keyword(s):  
Aspartic Acid ◽  
Blood Group ◽  
Blood Group Antigens ◽  
Structural Constraints ◽  
Human Norovirus ◽  
Genotype 4 ◽  
Human Noroviruses ◽  
X Ray ◽  
X Ray Crystallography ◽  
New Findings

ABSTRACT Human norovirus interacts with the polymorphic human histo-blood group antigens (HBGAs), and this interaction is thought to be important for infection. The genogroup II genotype 4 (GII.4) noroviruses are the dominant cluster, evolve every other year, and are thought to modify their binding interactions with different HBGA types. Most human noroviruses bind HBGAs, while some strains were found to have minimal or no HBGA interactions. Here, we explain some possible structural constraints for several noroviruses that were found to bind poorly to HBGAs by using X-ray crystallography. We showed that one aspartic acid was flexible or positioned away from the fucose moiety of the HBGAs and this likely hindered binding, although other fucose-interacting residues were perfectly oriented. Interestingly, a neighboring loop also appeared to influence the loop hosting the aspartic acid. These new findings might explain why some human noroviruses bound HBGAs poorly, although further studies are required.

Synthesis of 5-thio-l-fucose-containing blood group antigens H-type 2 and Lewis X (Lex)

1996 ◽  
Vol 37 (11) ◽  
pp. 1809-1812 ◽  
Author(s):  
Masayuki Izumi ◽  
Osamu Tsuruta ◽  
Hironobu Hashimoto ◽  
Shin Yazawa
Keyword(s):  
Blood Group ◽  
Blood Group Antigens ◽  
Lewis X

scholarly journals Two-Log Increase in Sensitivity for Detection of Norovirus in Complex Samples by Concentration with Porcine Gastric Mucin Conjugated to Magnetic Beads

2008 ◽  
Vol 74 (14) ◽  
pp. 4271-4276 ◽  
Author(s):  
Peng Tian ◽  
Anna Engelbrektson ◽  
Robert Mandrell
Keyword(s):  
Blood Group ◽  
Magnetic Beads ◽  
Rna Extraction ◽  
Extraction Procedure ◽  
Food Samples ◽  
Gastric Mucin ◽  
Blood Group Antigens ◽  
Reverse Transcription Pcr ◽  
Porcine Gastric Mucin ◽  
Multiple Strains

ABSTRACT Human histo-blood group antigens (HBGA) have been identified previously as candidate receptors for human norovirus (NOR). Type A, type H1, and Lewis HBGA in humans have been identified as major HBGA for NOR binding. We have found that pig stomach (gastric) mucin (PGM) contains blood group A, H1, and Lewis b HBGA and binds to multiple strains of NOR more broadly than do specific antibodies to NOR. Both genogroup I (GGI) and GGII NOR strains were recovered by PGM-conjugated magnetic beads. A fecal sample containing GGII NOR was detected at a dilution of 1:1,000,000 by the standard RNA extraction procedure, whereas NOR in a 1:100,000,000 dilution could be concentrated by PGM-conjugated magnetic beads and NOR in spiked food samples (e.g., oyster extract, strawberry, raspberry, and lettuce) was captured by PGM, thus minimizing the reverse transcription-PCR inhibitors in food and increasing sensitivity.

scholarly journals Histo–Blood Group Antigens and Susceptibility to Infection with Norovirus Genogroup II Genotype 4

2008 ◽  
Vol 198 (6) ◽  
pp. 940-940 ◽  
Author(s):  
Martin C. W. Chan ◽  
Y. P. Wong ◽  
Joseph J. Y. Sung ◽  
Wai K. Leung
Keyword(s):  
Blood Group ◽  
Blood Group Antigens ◽  
Genotype 4 ◽  
Susceptibility To Infection

scholarly journals Recognition of Histo-Blood Group Antigen-Like Carbohydrates in Lettuce by Human GII.4 Norovirus

2016 ◽  
Vol 82 (10) ◽  
pp. 2966-2974 ◽  
Author(s):  
Xiang Gao ◽  
Malak A. Esseili ◽  
Zhongyan Lu ◽  
Linda J. Saif ◽  
Qiuhong Wang
Keyword(s):  
Cell Wall ◽  
Blood Group ◽  
The United States ◽  
Blood Group Antigens ◽  
Cell Wall Degrading Enzymes ◽  
Human Norovirus ◽  
Genotype 4 ◽  
Binding Characteristics ◽  
Contaminated Food ◽  
Potential Inhibitors

ABSTRACTHuman norovirus (HuNoV) genogroup II genotype 4 (GII.4) strains account for about 80% of the gastroenteritis outbreaks in the United States. Contaminated food is a major transmission vehicle for this virus. In humans, pigs, and oysters, histo-blood group antigens (HBGAs) act as attachment factors for HuNoVs. In lettuce, although the virus-like particles (VLPs) of a GII.4 HuNoV were found to bind to cell wall carbohydrates, the exact binding site has not been investigated. Here, we show the presence of HBGA-like carbohydrates in the cell wall of lettuce. The digestion of lettuce leaves with cell wall-degrading enzymes exposed more binding sites and significantly increased the level of binding of GII.4 HuNoV VLPs. Competition assays showed that both the HBGA monoclonal antibody, recognizing the H type, and plant lectins, recognizing α-l-fucose in the H type, effectively inhibited VLP binding to lettuce tissues. Lettuce cell wall components were isolated and their NoV VLP binding characteristics were tested by enzyme-linked immunosorbent assays. The binding was inhibited by pretreatment of the lettuce cell wall materials with α-1,2-fucosidase. Collectively, our results indicate that H-type HBGA-like carbohydrates exist in lettuce tissues and that GII.4 HuNoV VLPs can bind the exposed fucose moiety, possibly in the hemicellulose component of the cell wall.IMPORTANCESalad crops and fruits are increasingly recognized as vehicles for human norovirus (HuNoV) transmission. A recent study showed that HuNoVs specifically bind to the carbohydrates of the lettuce cell wall. Histo-blood group antigens (HBGAs) are carbohydrates and are known as the attachment factors for HuNoV infection in humans. In this study, we show the presence of HBGA-like carbohydrates in lettuce, to which HuNoVs specifically bind. These results suggest that specifically bound HuNoVs cannot be removed by simple washing, which may allow viral transmission to consumers. Our findings provide new information needed for developing potential inhibitors to block binding and prevent contamination.

scholarly journals Bat Caliciviruses and Human Noroviruses Are Antigenically Similar and Have Overlapping Histo-Blood Group Antigen Binding Profiles

mBio ◽  
2018 ◽  
Vol 9 (3) ◽  
Author(s):  
Jacob F. Kocher ◽  
Lisa C. Lindesmith ◽  
Kari Debbink ◽  
Anne Beall ◽  
Michael L. Mallory ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Homology Modeling ◽  
Blood Group ◽  
Receptor Binding ◽  
Wild Animal ◽  
Blood Group Antigens ◽  
Viral Pathogens ◽  
Human Noroviruses ◽  
Animal Populations ◽  
Antigenic Epitopes

ABSTRACTEmerging zoonotic viral diseases remain a challenge to global public health. Recent surveillance studies have implicated bats as potential reservoirs for a number of viral pathogens, including coronaviruses and Ebola viruses.Caliciviridaerepresent a major viral family contributing to emerging diseases in both human and animal populations and have been recently identified in bats. In this study, we blended metagenomics, phylogenetics, homology modeling, andin vitroassays to characterize two novel bat calicivirus (BtCalV) capsid sequences, corresponding to strain BtCalV/A10/USA/2009, identified inPerimyotis subflavusnear Little Orleans, MD, and bat norovirus. We observed that bat norovirus formed virus-like particles and had epitopes and receptor-binding patterns similar to those of human noroviruses. To determine whether these observations stretch across multiple bat caliciviruses, we characterized a novel bat calicivirus, BtCalV/A10/USA/2009. Phylogenetic analysis revealed that BtCalV/A10/USA/2009 likely represents a novelCaliciviridaegenus and is most closely related to "recoviruses." Homology modeling revealed that the capsid sequences of BtCalV/A10/USA/2009 and bat norovirus resembled human norovirus capsid sequences and retained host ligand binding within the receptor-binding domains similar to that seen with human noroviruses. Both caliciviruses bound histo-blood group antigens in patterns that overlapped those seen with human and animal noroviruses. Taken together, our results indicate the potential for bat caliciviruses to bind histo-blood group antigens and overcome a significant barrier to cross-species transmission. Additionally, we have shown that bat norovirus maintains antigenic epitopes similar to those seen with human noroviruses, providing further evidence of evolutionary descent. Our results reiterate the importance of surveillance of wild-animal populations, especially of bats, for novel viral pathogens.IMPORTANCECaliciviruses are rapidly evolving viruses that cause pandemic outbreaks associated with significant morbidity and mortality globally. The animal reservoirs for human caliciviruses are unknown; bats represent critical reservoir species for several emerging and zoonotic diseases. Recent reports have identified several bat caliciviruses but have not characterized biological functions associated with disease risk, including their potential emergence in other mammalian populations. In this report, we identified a novel bat calicivirus that is most closely related to nonhuman primate caliciviruses. Using this new bat calicivirus and a second norovirus-like bat calicivirus capsid gene sequence, we generated virus-like particles that have host carbohydrate ligand binding patterns similar to those of human and animal noroviruses and that share antigens with human noroviruses. The similarities to human noroviruses with respect to binding patterns and antigenic epitopes illustrate the potential for bat caliciviruses to emerge in other species and the importance of pathogen surveillance in wild-animal populations.

Sign in / Sign up

Export Citation Format

Share Document