Cryptantigenic N_Vg Receptor in Mucoids from Mu/Mu Cells

Abstract

Résumé Les mucoïdes obtenus à partir des erythrocytes Mu/Mu qui dans leur forme originale (non traités) ne possèdent pas les récepteurs “N‐like” (Nvg) comme les mucoïdes des erythrocytes MU/MU, ont été trouvés comme ayant un effet inhibiteur sur la phythémagglutinine anti‐N obtenue à partir des semences de Vicia graminea si l'acide neuraminique était séparé à la suite d'un traitement par la neuraminidase (RDE). Zusammenfassung Mukoide von Mu/Mu‐Zellen, die im Gegensatz zu Mukoiden von MU/MU‐Zellen keine “N‐like” (Nvg)‐Rezeptoren aufweisen, vermochten das pflanzliche Anti‐N‐Agglutinin von Vicia graminea zu hemmen, sofern an ihnen mit RDE die Neuraminsäure abgespalten worden war.

Possible Genetical Pathways in the MNSsUu System

“…This is in contrast to the hypothesis of Uhlenbruck and Krüpe [44], who postulated in this case a maximal utilisation of the precursor by the N genes and subsequently the development of the maximum number of N receptors. Therefore we are left with the possibility, that the u gene also produces a special serological product and that the corresponding anti-u will be found one day.…”

“…Another problem is that the MNSs active mucoids from red cells exhibit no U activity [Uhlenbruck and Krüpe,44] as should be expected on the basis of the proposed scheme in fig. 1.…”

Glycosyltransferases and their Use in Assessing Oligosaccharide Structure and Structure‐Function Relationships

“…The removal of sialic acid has been proposed to change the conformation of the MN antigens, making them either inaccessible or unrecognizable to antibody (434,438,447). However, the oligosaccharide chains of sialidase-treated erythrocytes are exposed sufficiently to be recognized by anti-TF antibodies (448) and a variety of lectins (447), and to be substrates for either galactose oxidase (449), P-galactosidase (41 5 ) , or three different sialyltransferases (444). Thus removal of sialic acid probably does not sterically prevent access to the MN-specific region of glycophorin, although the molecular structure required for recognition of the MN antigens by most antibodies is clearly destroyed by sialidase.…”

Biochemical Genetics of MN

“…This phenotype has been in terpreted by Prokop and Uhlenbruck [14] as due to complete conversion of precursor N to M (presumably by a hyperactive trans ferase). From this, Uhlenbruck and Kriipe [20] suggested that the M antigen of MU cells 'should have more M receptors'. Our data do not support this contention.…”