Synthesis of p-nitrophenyl 5-acetamido-3,5-dideoxy-α-d-glycero-d-galacto-2-nonulopyranosidonic acid, a chromogenic substrate for sialidases
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With methylumbelliferyl-N-acetyl-neuraminic acid (MU-NANA) as substrate, acid sialidase was determined in intestinal biopsies of children. The enzyme has an acid pH optimum, a K(m) value of 4 mmol/1 and a pronounced thermal lability which can be partially prevented by the addition of albumin. N-acetyl-neuraminic acid (NANA) and derivatives as well as other glycoprotein and oligosaccharide sialidase substrates inhibit sialidase whereas gangliosides have no effect. This could be an indication that intestinal MU-NANA sialidase is different from ganglioside sialidase as has been reported for many other tissues.
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Neuraminidase-treated erythrocytes coated with a variety of neuraminic acid-containing glycoproteins adsorbed influenza virus and neuraminidase-free hemagglutinins, but not purified neuraminidase. The results indicate that neuraminic acid is the binding site on the glycoprotein and that the rest of the molecule does not play a specific role in the reaction.
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Abstract Sialic acid has been detected on the erythrocyte surface of a number of different species of animals. The objective of this investigation was to determine the physiological significance of these sialyl residues to the viability of erythrocytes in circulation. Methods have been described for the determination of total sialic acid on red blood cells and the conditions under which it may be released with sialidase. Chicken, dog, goat, and rabbit were chosen for these studies because of the differences in the amount (3 × 10 6 ‐72 × 10 6 residues per erythrocyte), and type (N‐acetyl‐ or N‐glycolyl‐neuraminic acids) of sialic acid found on the surface of their erythrocytes. Radioactive tagging with Na 2 51 CrO 4 was used to monitor the effect of sialidase on the viability of erythrocytes upon autologous transfusion. By the two criteria used to assess the viability of erythrocytes — the percentage of erythrocytes surviving 24 hr after the autologous transfusion, and the half‐life of those red blood cells in circulation that survive the first 24 hr — it is apparent that the presence of sialic acid on the cell surface is crucial for the survival of nonnucleated mammalian erythrocytes. The loss of viability of dog erythrocytes can be elicited by the removal of approximately 10% of the total sialic acid. In marked contrast to the behavior of mammalian erythrocytes, sialidase‐treated chicken erythrocytes appear to retain their viability in circulation.
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Abstract: The demand for novel anti-influenza drugs persists, which is highlighted by the recent pandemics of influenza affecting thousands of people across the globe. One of the approaches to block the virus spreading is inhibiting viral sialidase (neuraminidase). This enzyme cleaves the sialic acid link between the newly formed virions and the host cell surface liberating the virions from the cell and maintaining the cycle of infection. Viral neuraminidases appear therefore as attractive therapeutic targets for preventing further spread of influenza infection. Compared to ion channel blockers that were the first approved anti-influenza drugs, neuraminidase inhibitors are well tolerated and target both influenza A and B viruses. Moreover, neuraminidase/sialidase inhibitors may be useful for managing some other human pathologies, such as cancer. In this review, we discuss the available knowledge on neuraminidase or sialidase inhibitors, their design, clinical application, and the current challenges. Keywords: sialidase, neuraminidase, neuraminidase inhibitor, influenza, drug design
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