Human RBCs blood group conversion from A to O using a novel α-N-acetylgalactosaminidase of high specific activity

Yu, ChengYu; Xu, Hua; Wang, LiSheng; Zhang, Jian-Geng; Zhang, Yang-Pei

doi:10.1007/s11434-008-0248-y

Cited by 7 publications

(7 citation statements)

References 19 publications

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“…Initial physicochemical substrate specificity of the enzyme with the reagent α -N-acetylgalactosamine was highly selective compared to eleven additional substrates. Similar specific activity was demonstrated by E. meningoseptica [19, 27] and C. perfringens [35] α -NAGA to α -N-acetylgalactosamine substrate. Optimal enzyme activity was demonstrated by S. linguale in the pH range of 6.0 - 8.0; well within the range RBCs are stored.…”

Section: Discussionsupporting

confidence: 73%

“…The α -NAGAs from S. linguale and E. meningoseptica have both demonstrated the capacity to convert Type A RBC to blood group O in this research and by two groups Liu et al [19] and Yu et al [27], respectively. The E. meningoseptica enzymes used [19, 27] had very similar steady state Michaelis-Menten kinetic parameters. An alignment of the protein sequences is identical with the exception of four amino acids at positions 160G>V, 174H>R, 426F>S, and 434V>A.…”

Section: Discussionmentioning

confidence: 54%

“…Using a phosphate buffer pH 7.0, as a base to relate the effect on enzyme activity, solutions composed of 50 mM acetate, 10 mM citrate, 10 mM tris, and 500 mM EDTA appeared to reduce relative enzyme activity. A glycine solution, used in studies by Liu et al [19] and Yu et al [27], appeared to reduce enzyme activity in vitro compared to the phosphate solution. Liu et al showed inhibition of E. meningosetica enzyme activity with several divalent metals, Cu 2+ , Ni 2+ , and Zn 2+ , at concentrations of 1 or 10 mM but EDTA did not impact enzyme activity at these concentrations [19].…”

Section: Discussionmentioning

confidence: 99%

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Enzymatic Conversion of RBCs by α-N-Acetylgalactosaminidase from Spirosoma linguale

Malinski

Singh

2019

Enzyme Research

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Spirosoma lingualeis a free-living nonpathogenic organism. Like many other bacteria,S. lingualeproduces a cell-associatedα-N-acetylgalactosaminidase. This work was undertaken to elucidate the nature of this activity. The recombinant enzyme was produced, purified, and examined for biochemical attributes. The purified enzyme was ~50 kDa active as a homodimer in solution. It catalyzed hydrolysis ofα-N-acetylgalactosamine at pH 7. CalculatedKMwas 1.1 mM withkcatof 173 s−1. The described enzyme belongs to the GH109 family.

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Section: Discussionsupporting

confidence: 73%

Section: Discussionmentioning

confidence: 54%

Section: Discussionmentioning

confidence: 99%

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Enzymatic Conversion of RBCs by α-N-Acetylgalactosaminidase from Spirosoma linguale

Malinski

Singh

2019

Enzyme Research

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“…The practical solution of the problem is hampered by the absence of economically advanta geous sources of the enzymes, which act effectively under conditions where erythrocytes retain viability (neutral pH, temperature of 20-25°C, and low ionic strength). Therefore, the search for new sources of specific, stable, and efficient enzymes for the large scale modification of A erythrocytes is topical.To date, α N acetylgalactosaminidases with the required properties were revealed in the anaerobic bacteria of terrestrial origin, Clostridium perfringens [6-9] and Ruminococcus torques [10,11] of the phy lum Firmicutes and Elisabethkingia meningoseptica of the phylum Bacteroidetes [12][13][14]. The evidence of α N acetylgalactosaminidases from marine bacteria is scarce.…”

mentioning

confidence: 99%

“…To date, α N acetylgalactosaminidases with the required properties were revealed in the anaerobic bacteria of terrestrial origin, Clostridium perfringens [6][7][8][9] and Ruminococcus torques [10,11] of the phy lum Firmicutes and Elisabethkingia meningoseptica of the phylum Bacteroidetes [12][13][14]. The evidence of α N acetylgalactosaminidases from marine bacteria is scarce.…”

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confidence: 99%

Distribution of α-N-acetylgalactosaminidases among marine bacteria of the phylum Bacteroidetes, epiphytes of marine algae of the Seas of Okhotsk and Japan

et al. 2012

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373α N Acetylgalactosaminidase (EC 3.2.1.49) cata lyzes the hydrolytic cleavage of the terminal α O gly coside bonded residues of N acetylgalactosamine from the nonreducing ends of various complex carbo hydrates and glycoconjugates. Glycolipids, glycopep tides, and glycoproteins containing the structures with the O glycoside core, oligosaccharides, and blood group A erythrocyte antigens are it's physiological substrates [1][2][3]. An increased interest in this enzyme was generated by the possibility of its use in biotech nology when the group 0 "universal blood" was obtained by enzymatic conversion of A and AB donor blood [4,5]. The practical solution of the problem is hampered by the absence of economically advanta geous sources of the enzymes, which act effectively under conditions where erythrocytes retain viability (neutral pH, temperature of 20-25°C, and low ionic strength). Therefore, the search for new sources of specific, stable, and efficient enzymes for the large scale modification of A erythrocytes is topical.To date, α N acetylgalactosaminidases with the required properties were revealed in the anaerobic bacteria of terrestrial origin, Clostridium perfringens [6-9] and Ruminococcus torques [10,11] of the phy lum Firmicutes and Elisabethkingia meningoseptica of the phylum Bacteroidetes [12][13][14]. The evidence of α N acetylgalactosaminidases from marine bacteria is scarce.Earlier, we investigated the distribution of these enzymes in the inhabitants of various ecotopes of the World Ocean and Lake Baikal [15,16]. As result of thorough screening of over 800 strains, α N acetylga lactosaminidase, which inactivated the serological activity of A erythrocytes at neutral pH, was isolated from the biomass of the obligate marine bacterium Arenibacter latericius KMM 426 T of the phylum Bacteroidetes and studied [17]. No Bacteroidetes epi phytic bacterial strains isolated from the algoplane of marine algae were among the isolates tested.Abstract-Occurrence of α N acetylgalactosaminidases among 177 strains of marine bacteria of the phylum Bacteroidetes, epiphytes of marine algae growing on the littoral of the Seas of Okhotsk and Japan, was studied. About 36% of the isolates studied contained α N acetylgalactosaminidase. All of the bacteria of the genus Arenibacter (species A. latericius, A. certesii, and A. palladensis), irrespective of the source of isolation, syn thesized this enzyme. The greatest number of α N acetylgalactosaminidase producers was found among the isolates from the algae Neosiphonia japonica, Acrosiphonia sonderi, and Ulva fenestrata sampled in the Cove of Trinity, Posyet Bay, the Sea of Japan. These were mainly bacteria of the genera Zobellia (50%) and Mari bacter (58%). Among the epibionts studied, the bacteria Arenibacter latericius KMM 3523, an epiphyte of the brown alga Chorda filum from the Sea of Okhotsk, and Cellulophaga sp. KMM 6488, an epiphyte of the green alga Acrosiphonia sonderi from the Sea of Japan, were marked as the most promising sources of the enzyme. The results of this stu...

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Production of Universal Group O Red Blood Cells by Alpha-N-Acetylgalactosaminidase Enzyme Expressed in Pichia pastoris

Molafilabi

Shahabi

Rafatpanah

et al. 2018

Indian J Hematol Blood Transfus

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Enzymatic removal of blood groups antigens A and B is an efficient method for production of universal red blood cells. In this research, an a-N-acetylgalactosaminidase (NAGA) enzyme was expressed in Pichia pastoris for digestion of the A blood antigen. DNA sequence of the gene NAGA, originally expressed in Elizabethkingia meningosepticum (NAGA-EM), was ordered for optimization and synthesis. It was then expressed in P. pastoris (KM71H and GS115 strains). Expression of the recombinant NAGA was evaluated by dot blot, SDS-PAGE, and Western blotting. The activity of the enzyme was measured using a synthetic substrate in addition to the conversion of group A red blood cells to the O cells. Expression of NAGA-EM with an apparent molecular mass of 55 kDa was verified by dot blot, SDS-PAGE and Western blot analysis. The maximum enzyme activity in the supernatant of KM71H was higher than that in the GS115 (250 vs. 200 U/ml). Treated group A RBCs did not react with the anti-A antiserum or with the sera from individuals with blood groups B and O. The results of this study indicated that NAGA-EM is an efficient enzyme for production of universal O blood cells.

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Human RBCs blood group conversion from A to O using a novel α-N-acetylgalactosaminidase of high specific activity

Cited by 7 publications

References 19 publications

Enzymatic Conversion of RBCs by α-N-Acetylgalactosaminidase from Spirosoma linguale

Enzymatic Conversion of RBCs by α-N-Acetylgalactosaminidase from Spirosoma linguale

Distribution of α-N-acetylgalactosaminidases among marine bacteria of the phylum Bacteroidetes, epiphytes of marine algae of the Seas of Okhotsk and Japan

Production of Universal Group O Red Blood Cells by Alpha-N-Acetylgalactosaminidase Enzyme Expressed in Pichia pastoris

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