Characterization of a neuraminidase from Corynebacterium aquaticum responsible for Th polyagglutination.
Th polyagglutinability is characterized by the agglutination of the red blood cells (RBC) by Arachis hypogaea, Medicago disciformis, Vicia cretica but, in contrast to the T phenomenon, not by Glycine max (Glycine soja). Because Th transformation of RBC has been obtained in vitro, the mechanism of Th polyagglutinability expression has been studied and reproduced experimentally. An enzyme with neuraminidase specificity has been isolated from the culture supernatant of Corynebacterium aquaticum, and further characterized (MW = 55,600 kDa, pH = 5.5, Km = 0.138 microM, Kcat = 0.22 micrograms). Reversely, Th transformation of RBC could be obtained by using other neuraminidases but in very mild conditions of hydrolysis. From our results, it can be concluded that by the release of less than 20 micrograms of sialic acid per 10(10) RBC, Th reactivity can be induced whereas hydrolysis of greater amounts of sialic acid (greater than 20 micrograms/10(10) RBC) give the classical T polyagglutinability.
Sondag-Thull
D
D
Laboratoire des Groupes Sanguins et de Transfusion, Université de Liège, Belgique.
Levene
N A
NA
Levene
C
C
Manny
N
N
Liew
Y W
YW
Bird
G W
GW
Schechter
Y
Y
François-Gérard
C
C
Huet
M
M
Blanchard
D
D
D001789:Blood Group Antigens / Q000502:physiology*; D003352:Corynebacterium / Q000201:enzymology*; D004903:Erythrocyte Aggregation / Q000187:drug effects*; D006801:Humans; D009439:Neuraminidase / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology
D001789:Blood Group Antigens; D009439:Neuraminidase