Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0267964 (PAA)
 2,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A comparative study of the hemagglutinin (HA) receptor binding site (RBS) of a number of H13 influenza viruses isolated from Laridae family of birds (gulls) and other influenza viruses obtained from the Anatidae family (ducks) was conducted. The affinity of all viruses to alpha N-acetylneuraminic acid (Neu5Ac alpha), 3'sialyllactose (3'SL), and sialylglycopolymers bearing 3'-sialyl(N-acetyllactosamine) (3'SLN-PAA), [Neu5Ac alpha(2-3)Gal beta(1-4)][-Fuc alpha(1-3)]GlcNAc beta (SLe(x)-PAA), and [Neu5Ac alpha(2-3)Gal beta(1-3)][-Fuc alpha(1-4)]GlcNAc beta (SLe(a)-PAA), was determined. The last three polymer glycoconjugates were synthesized for determining the contribution of carbohydrate chains after the galactose link to the binding with the receptor. The difference in affinity between 3'SL and Neu5Ac alpha in all studied H13 viruses is small, which indicates a less significant role of the galactose moiety in the binding to the receptor. The results of virus binding with polymer sialylglycoconjugates indicates that the method of linking, the third monosaccharide moiety, and the presence of an extra fucose substitute in this moiety may influence the binding considerably. For viruses isolated from ducks, the suitable polymer is SLe(a)-PAA (i.e., a 1-3 linkage between galactose and glucosamine is optimal). This finding is in accord with the data that H13 viruses isolated from the gulls differ based on their ability to interact with polymer sialylglycoconjugates. The affinity to all three polymers is uniform, and the presence of GlcNAc-linked fucose does not prevent the binding. A comparative analysis of six sequenced HA H13 viruses and other subtype viruses showed presence of substantial differences in the composition of amino acids of this region in H13 viruses.
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PMID:Differences between HA receptor-binding sites of avian influenza viruses isolated from Laridae and Anatidae. 1457 35

It has been shown that human blood contains a soluble 67 kDa enzyme, belonging by its donor-acceptor properties to trans-sialidases. The enzyme is capable of both cleaving and synthesizing alpha2-3 and alpha2-6 sialosides [Atherosclerosis2001, 159, 103]. In this work the study of donor-acceptor specificity of the new enzyme was extended. It has been demonstrated in vitro that trans-sialidase possesses the ability of transferring Neu5Ac residue to acceptor (asialofetuin) both from alpha2-3- (GM1, GM3, GD1a), and alpha2-8-sialylated gangliosides (GD3 and GD1b, but not GT1b and GQ1b). Transfer of radiolabeled Neu5Ac from fetuin to glycosphingolipids demonstrated that Lac-Cer>mono- and disialogangliosides>GT1b>GQ1b were acceptors for this enzyme. Two methods were used to reveal whether alpha2-8 bond can be formed between Neu5Ac residues during trans-sialylation, that is immunochemical detection using monoclonal antibodies specific to alpha2-8 di- and oligosialic acids, and fluorometric C7/C9 analysis. Both methods demonstrated the formation of Neu5Acalpha2-8Neu5Ac termination by trans-sialidase, for example, in case of the use 3'SL as sialic acid donor and Neu5Ac-PAA or LDL as acceptor. Thus, human trans-sialidase in vitro displays wide substrate specificity: the enzyme is capable of digesting as well as synthesizing alpha2-3, alpha2-6, and alpha2-8 sialosides.
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PMID:Specificity of human trans-sialidase as probed with gangliosides. 1538 Feb 19