Structural analysis of the RH-like blood group gene products in nonhuman primates

1995 ◽  
Vol 41 (5) ◽  
pp. 271-281 ◽  
Author(s):  
I. Salvignol ◽  
P. Calvas ◽  
W. W. Socha ◽  
Y. Colin ◽  
C. Le Van Kim ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Blood Group ◽  
Nonhuman Primates ◽  
Gene Products

Structural analysis of hexa- to octa-saccharide fractions isolated from sheep gastric-glycoproteins having blood-group I and i activities

1981 ◽  
Vol 90 (2) ◽  
pp. 283-307 ◽  
Author(s):  
Elizabeth F. Hounsell ◽  
Edwin Wood ◽  
Ten Feizi ◽  
Minoru Fukuda ◽  
Mark E. Powell ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Blood Group ◽  
Group I

Primary structural analysis of the Tla region gene products, QA-2 and TL

1982 ◽  
Vol 19 (9) ◽  
pp. 1193-1197 ◽  
Author(s):  
Mark J. Soloski ◽  
Katherine R. McIntyre ◽  
Jonathan W. Uhr ◽  
Ellen S. Vitetta
Keyword(s):  
Structural Analysis ◽  
Gene Products ◽  
Region Gene

scholarly journals Structural analysis of the Ss sialoglycoprotein specific for Henshaw blood group from human erythrocyte membranes

1984 ◽  
Vol 141 (1) ◽  
pp. 51-55 ◽  
Author(s):  
Wolfgang DAHR ◽  
Maria KORDOWICZ ◽  
W. John JUDD ◽  
John MOULDS ◽  
Konrad BEYREUTHER ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Blood Group ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes

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

2014 ◽  
Vol 16 ◽  
Author(s):  
Ming Tan ◽  
Xi Jiang
Keyword(s):  
Helicobacter Pylori ◽  
Structural Analysis ◽  
Blood Group ◽  
Bacterial Pathogen ◽  
Binding Pocket ◽  
Lewis Antigens ◽  
Blood Group Antigens ◽  
Exploratory Research ◽  
Binding Interfaces ◽  
Selection Of

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.

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
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