Histo-blood group antigens: a common niche for norovirus and rotavirus

Author(s):  
Ming Tan ◽  
Xi Jiang

Noroviruses (NoVs) and rotaviruses (RVs), the two most important causes of viral acute gastroenteritis, are found to recognise histo-blood group antigens (HBGAs) as receptors or ligands for attachment. Human HBGAs are highly polymorphic containing ABO, secretor and Lewis antigens. In addition, both NoVs and RVs are highly diverse in how they recognise these HBGAs. Structural analysis of the HBGA-binding interfaces of NoVs revealed a conserved central binding pocket (CBP) interacting with a common major binding saccharide (MaBS) of HBGAs and a variable surrounding region interacting with additional minor binding saccharides. The conserved CBP indicates a strong selection of NoVs by the host HBGAs, whereas the variable surrounding region explains the diverse recognition patterns of different HBGAs by NoVs and RVs as functional adaptations of the viruses to human HBGAs. Diverse recognition of HBGAs has also been found in bacterial pathogenHelicobacter pylori. Thus, exploratory research into whether such diverse recognitions also occur for other viral and bacterial pathogens that recognise HBGAs is warranted.

2012 ◽  
Vol 86 (18) ◽  
pp. 9899-9910 ◽  
Author(s):  
Yang Liu ◽  
Pengwei Huang ◽  
Ming Tan ◽  
Yiliu Liu ◽  
Jacek Biesiada ◽  
...  

The distal portion of rotavirus (RV) VP4 spike protein (VP8*) is implicated in binding to cellular receptors, thereby facilitating viral attachment and entry. While VP8* of some animal RVs engage sialic acid, human RVs often attach to and enter cells in a sialic acid-independent manner. A recent study demonstrated that the major human RVs (P[4], P[6], and P[8]) recognize human histo-blood group antigens (HBGAs). In this study, we performed a phylogenetic analysis of RVs and showed further variations of RV interaction with HBGAs. On the basis of the VP8* sequences, RVs are grouped into five P genogroups (P[I] to P[V]), of which P[I], P[IV], and P[V] mainly infect animals, P[II] infects humans, and P[III] infects both animals and humans. The sialic acid-dependent RVs (P[1], P[2], P[3], and P[7]) form a subcluster within P[I], while all three major P genotypes of human RVs (P[4], P[6], and P[8]) are clustered in P[II]. We then characterized three human RVs (P[9], P[14], and P[25]) in P[III] and observed a new pattern of binding to the type A antigen which is distinct from that of the P[II] RVs. The binding was demonstrated by hemagglutination and saliva binding assay using recombinant VP8* and native RVs. Homology modeling and mutagenesis study showed that the locations of the carbohydrate binding interfaces are shared with the sialic acid-dependent RVs, although different amino acids are involved. The P[III] VP8* proteins also bind the A antigens of the porcine and bovine mucins, suggesting the A antigen as a possible factor for cross-species transmission of RVs. Our study suggests that HBGAs play an important role in RV infection and evolution.


1996 ◽  
Vol 64 (6) ◽  
pp. 2031-2040 ◽  
Author(s):  
B J Appelmelk ◽  
I Simoons-Smit ◽  
R Negrini ◽  
A P Moran ◽  
G O Aspinall ◽  
...  

Helicobacter ◽  
2004 ◽  
Vol 9 (4) ◽  
pp. 324-329 ◽  
Author(s):  
Dietrich Rothenbacher ◽  
Maria Weyermann ◽  
Gunter Bode ◽  
Murrat Kulaksiz ◽  
Bernd Stahl ◽  
...  

2005 ◽  
Vol 79 (11) ◽  
pp. 6714-6722 ◽  
Author(s):  
Pengwei Huang ◽  
Tibor Farkas ◽  
Weiming Zhong ◽  
Ming Tan ◽  
Scott Thornton ◽  
...  

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.


2005 ◽  
Vol 83 (5) ◽  
pp. 589-596 ◽  
Author(s):  
Eleonora Altman ◽  
Blair A Harrison ◽  
Tomoko Hirama ◽  
Vandana Chandan ◽  
Rebecca To ◽  
...  

The cell envelope of Helicobacter pylori contains lipopolysaccharide (LPS), the O-chain of which expresses type 2 Lexand Leyblood group antigens, which mimic human gastric mucosal cell-surface glycoconjugates and may contribute to the survival of H. pylori in gastric mucosa. Here we describe the generation of monoclonal antibodies specific for Lexand Leyblood group determinants and the characterization of their binding properties using purified, structurally defined H. pylori LPS, synthetic glycoconjugates, and H. pylori cells. Analysis of oligosaccharide binding by SPR provided a rapid and reliable means for characterization of antibody affinities. One of the antibodies, anti-Lex, was of IgG3 subclass and had superior binding characteristics as compared with the commercially available anti-LexIgM. These antibodies could have potential in the immunodiagnosis of certain types of cancer, in serotyping of H. pylori isolates, and in structure–function studies.Key words: Helicobacter pylori, lipopolysaccharide, monoclonal antibodies, Lewis determinants, immunodiagnosis.


Glycobiology ◽  
2000 ◽  
Vol 10 (7) ◽  
pp. 701-713 ◽  
Author(s):  
M. A. Monteiro ◽  
P.-y. Zheng ◽  
B. Ho ◽  
S.-i. Yokota ◽  
K.-i. Amano ◽  
...  

2000 ◽  
Vol 68 (2) ◽  
pp. 937-941 ◽  
Author(s):  
Michael A. Heneghan ◽  
Ciaran F. McCarthy ◽  
Anthony P. Moran

ABSTRACT As Lewis a (Lea) and Lewis b (Leb) blood group antigens are isoforms of Lewis x (Lex) and Lewis y (Ley) and are expressed in the gastric mucosa, we evaluated whether the patterns of expression of Lex and Ley on Helicobacter pylorilipopolysaccharides reflected those of host expression of Lea and Leb. When 79 patients (secretors and nonsecretors) were examined for concordance between bacterial and host Le expression, no association was found (χ2 = 5.734, 3 df, P = 0.125), nor was there a significant difference between the amount of Lex or Ley expressed on isolates from ulcer and chronic gastritis patients (P > 0.05). Also, the effect of host and bacterial expression of Le antigens on bacterial colonization and the observed inflammatory response was assessed. In ulcer patients, Lex expression was significantly related to neutrophil infiltration (r s = 0.481,P = 0.024), whereas in chronic gastritis patients significant relationships were found between Lexexpression and H. pylori colonization density (r s = 0.296, P = 0.03), neutrophil infiltrate (r s = 0.409,P = 0.001), and lymphocyte infiltrate (r s = 0.389, P = 0.002). Furthermore, bacterial Ley expression was related to neutrophil (r s = 0.271, P= 0.033) and lymphocyte (r s = 0.277,P = 0.029) infiltrates. Thus, although no evidence of concordance was found between bacterial and host expression of Le determinants, these antigens may be crucial for bacterial colonization, and the ensuing inflammatory response appears, at least in part, to be influenced by Le antigens.


2011 ◽  
Vol 83 (16) ◽  
pp. 6336-6341 ◽  
Author(s):  
Y. Y. Fei ◽  
A. Schmidt ◽  
G. Bylund ◽  
D. X. Johansson ◽  
S. Henriksson ◽  
...  

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