Glycosyl phosphatidylinositol-linked blood group antigens and paroxysmal nocturnal hemoglobinuria

1995 ◽  
Vol 2 (4) ◽  
pp. 277-290 ◽  
Author(s):  
M.J. Telen
Blood ◽  
1990 ◽  
Vol 75 (7) ◽  
pp. 1404-1407 ◽  
Author(s):  
MJ Telen ◽  
WF Rosse ◽  
CJ Parker ◽  
MK Moulds ◽  
JJ Moulds

Paroxysmal nocturnal hemoglobinuria (PNH) is an acquired disorder associated with absence of expression of phosphatidylinositol (PI)- linked membrane proteins from circulating hematopoietic cells of multiple lineages. Recent work demonstrated that decay accelerating factor, one such PI-linked protein, bears the Cromer-related blood group antigens. This study demonstrated that other high incidence antigens, including Cartwright (Yta/Ytb), Holley-Gregory (Hy/Gya), John Milton Hagen (JMH), and Dombrock (Doa/Dob), are absent from the complement-sensitive (PNH III) erythrocytes of patients with PNH. The relatively normal, complement-insensitive erythrocytes from the same patients express these antigens normally. Therefore, these antigens most likely reside on PI-linked proteins absent from PNH III, but not PNH I, erythrocytes.


Blood ◽  
1990 ◽  
Vol 75 (7) ◽  
pp. 1404-1407 ◽  
Author(s):  
MJ Telen ◽  
WF Rosse ◽  
CJ Parker ◽  
MK Moulds ◽  
JJ Moulds

Abstract Paroxysmal nocturnal hemoglobinuria (PNH) is an acquired disorder associated with absence of expression of phosphatidylinositol (PI)- linked membrane proteins from circulating hematopoietic cells of multiple lineages. Recent work demonstrated that decay accelerating factor, one such PI-linked protein, bears the Cromer-related blood group antigens. This study demonstrated that other high incidence antigens, including Cartwright (Yta/Ytb), Holley-Gregory (Hy/Gya), John Milton Hagen (JMH), and Dombrock (Doa/Dob), are absent from the complement-sensitive (PNH III) erythrocytes of patients with PNH. The relatively normal, complement-insensitive erythrocytes from the same patients express these antigens normally. Therefore, these antigens most likely reside on PI-linked proteins absent from PNH III, but not PNH I, erythrocytes.


1979 ◽  
Vol 254 (6) ◽  
pp. 2112-2119 ◽  
Author(s):  
J.E. Sadler ◽  
J.C. Paulson ◽  
R.L. Hill

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

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

1988 ◽  
Vol 32 (3) ◽  
pp. 130-138 ◽  
Author(s):  
M. Gerenčer ◽  
Z. Singer ◽  
S. Pfeifer ◽  
M. Tomaškovi ◽  
I. Humar ◽  
...  

Viruses ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 416
Author(s):  
Robert Creutznacher ◽  
Thorben Maass ◽  
Patrick Ogrissek ◽  
Georg Wallmann ◽  
Clara Feldmann ◽  
...  

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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