An investigation of human antibodies to blood group antigens for the management of haemolytic disease of the fetus and newborn

2021 ◽  
Author(s):  
◽  
Eunike McGowan
Keyword(s):  
Blood Group ◽  
Blood Group Antigens ◽  
Haemolytic Disease ◽  
Human Antibodies

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

scholarly journals NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins

Viruses ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 416
Author(s):  
Robert Creutznacher ◽  
Thorben Maass ◽  
Patrick Ogrissek ◽  
Georg Wallmann ◽  
Clara Feldmann ◽  
...  
Keyword(s):  
Blood Group ◽  
Protein Interactions ◽  
Capsid Proteins ◽  
Blood Group Antigens ◽  
Biological Processes ◽  
Murine Norovirus ◽  
Human Norovirus ◽  
Head Groups ◽  
Significant Difference

Glycan–protein interactions are highly specific yet transient, rendering glycans ideal recognition signals in a variety of biological processes. In human norovirus (HuNoV) infection, histo-blood group antigens (HBGAs) play an essential but poorly understood role. For murine norovirus infection (MNV), sialylated glycolipids or glycoproteins appear to be important. It has also been suggested that HuNoV capsid proteins bind to sialylated ganglioside head groups. Here, we study the binding of HBGAs and sialoglycans to HuNoV and MNV capsid proteins using NMR experiments. Surprisingly, the experiments show that none of the norovirus P-domains bind to sialoglycans. Notably, MNV P-domains do not bind to any of the glycans studied, and MNV-1 infection of cells deficient in surface sialoglycans shows no significant difference compared to cells expressing respective glycans. These findings redefine glycan recognition by noroviruses, challenging present models of infection.

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