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Glycoside hydrolases of marine bacteria are promising tools in haemotherapy

Authors:
Larissa Balabanova
Irina Bakunina
Galina Likhatskaya
Tatyana Zvyagintseva
Valery Rasskazov

Keywords: marine bacteria, glycosidase, alpha-N-acetylgalactosaminidase, homology model, blood group conversion, erythrocytes

Abstract:
Universal donor blood of group O is widely used on an emergency basis when it is impossible to define for some reasons a blood type of the recipient, for pediatric transfusions, and, especially, in cases when the blood of unusual or rare phenotypes. For today in transfusion medicine, still there is a problem of production of a qualitative donor blood in necessary quantity. Despite occurrence of techniques of enzymatic production of a donor blood, it cannot widely be applied in clinical practice because the enzymes being used for blood groups conversion are isolated from pathogenic microbial strains or/and produce up to 70 % injuring erythrocytes. Herein, alpha-N-acetylgalactosaminidase and α-galactosidase of marine bacteria, operating at neutral values of рН, have been suggested for conversion of erythrocytes of blood group A, B and АВ to O in biotechnological production of universal donor blood. Alpha-N-acetylgalactosaminidase isolated from marine bacterium Arenibacter latericius has found to be uncommon enzyme. It shows the maximum activity at рН 7.0-8.0 and remains stable up to 50°С. The enzyme does not cause nonspecific agglutination of erythrocytes and their hemolysis and unlike known analogs modifies erythrocytes of blood subgroup А2 and А1 into erythrocytes of blood group O. Characterization of the sequences encoding glycoside hydrolases of marine bacteria revealed that they shared about 20-40% overall amino acid identity with their terrestrial counterparts. For further comparison of A. latericius alpha-N-acetylgalactosaminidase gene family, the gene sequence was isolated and characterized. It has a single open-reading frame consisting of 1287 base pairs, and the deduced amino acid sequence revealed that the mature enzyme consisted of 428 amino acid residues. The enzyme was estimated to be a homodimer with a molecular mass of subunit 48.2 kDa. The Arenibacter enzyme has a conserved common gene structure with a new glycoside hydrolases family 109. The structure of the putative binding sites of A. latericius alpha-N-acetylgalactosaminidase with NAD+ and blood group A antigen was predicted by molecular docking.

Pages: 47 to 50

Copyright: Copyright (c) IARIA, 2011

Publication date: May 22, 2011

Published in: conference

ISSN: 2308-4154

ISBN: 978-1-61208-138-0

Location: Venice/Mestre, Italy

Dates: from May 22, 2011 to May 27, 2011