Characterization of a Neuraminidase fromCorynebacterium AquaticumResponsible for Th Polyagglutination

Publisher Website
Google Scholar
Abstract
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 μM, Kcat = 0.22 μg). 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 μg of sialic acid per 1010 RBC, Th reactivity can be induced whereas hydrolysis of greater amounts of sialic acid (>20 μg/1010 RBC) give the classical T polyagglutinability.