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Biological properties of N-acyl and N-haloacetyl neuraminic acids: processing by enzymes of sialic acid metabolism, and interaction with influenza virus

Biological properties of N-acyl and N-haloacetyl neuraminic acids: processing by enzymes of sialic acid metabolism, and interaction with influenza virus
Biological properties of N-acyl and N-haloacetyl neuraminic acids: processing by enzymes of sialic acid metabolism, and interaction with influenza virus
Several unnatural N-acyl neuraminic acids (N-propionyl, N-hexanoyl, N-benzoyl, N-trifluoroacetyl, N-chloroacetyl, N-difluoroacetyl) were prepared enzymatically using immobilised sialic acid aldolase. N-Trifluoroacetyl- N-chloroacetyl- and N-difluoroacetyl neuraminic acids were shown to enhance up to 10-fold the rate of association of influenza virus A to a sialoglycolipid neomembrane by surface plasmon resonance, and were found to act as weak inhibitors (K-iapp 0.45-2.0 mM) of influenza virus neuraminidase. The N-propionyl, N-chloroacetyl- and N-difluoroacetyl neuraminic acids were found to be substrates for recombinant Escherichia coli CMP sialate synthase, to give the corresponding CMP-N-acyl-neuraminic acids. CMP-N-propionyl neuraminic acid was found not to be a substrate for CMP-N-acetyl neuraminic acid hydroxylase from pig submandibular gland.
surface-plasmon resonance, acetylneuraminic acid, glycolylneuraminic acid, hydroxylase, analogs, oligosaccharides, purification, inhibitors, synthetase, aldolase
0968-0896
3175-3185
Humphrey, Andrew J.
c42295de-2151-4f72-85c0-0214ea4f0539
Fremann, Claire
92326b0a-a282-46af-9400-86274872afcc
Critchley, Peter
4e556699-ed72-440b-8053-6842b9ec3734
Malykh, Yanina
e37bbdf8-f906-42bf-80cc-8cbaa0d3ba57
Schauer, Roland
b5373e14-823e-4d13-85ca-509a465ce950
Bugg, Timothy D.H.
300f9ac5-0185-438a-a930-9bf22c08ddd5
Humphrey, Andrew J.
c42295de-2151-4f72-85c0-0214ea4f0539
Fremann, Claire
92326b0a-a282-46af-9400-86274872afcc
Critchley, Peter
4e556699-ed72-440b-8053-6842b9ec3734
Malykh, Yanina
e37bbdf8-f906-42bf-80cc-8cbaa0d3ba57
Schauer, Roland
b5373e14-823e-4d13-85ca-509a465ce950
Bugg, Timothy D.H.
300f9ac5-0185-438a-a930-9bf22c08ddd5

Humphrey, Andrew J., Fremann, Claire, Critchley, Peter, Malykh, Yanina, Schauer, Roland and Bugg, Timothy D.H. (2002) Biological properties of N-acyl and N-haloacetyl neuraminic acids: processing by enzymes of sialic acid metabolism, and interaction with influenza virus. Bioorganic & Medicinal Chemistry, 10 (10), 3175-3185. (doi:10.1016/S0968-0896(02)00213-4).

Record type: Article

Abstract

Several unnatural N-acyl neuraminic acids (N-propionyl, N-hexanoyl, N-benzoyl, N-trifluoroacetyl, N-chloroacetyl, N-difluoroacetyl) were prepared enzymatically using immobilised sialic acid aldolase. N-Trifluoroacetyl- N-chloroacetyl- and N-difluoroacetyl neuraminic acids were shown to enhance up to 10-fold the rate of association of influenza virus A to a sialoglycolipid neomembrane by surface plasmon resonance, and were found to act as weak inhibitors (K-iapp 0.45-2.0 mM) of influenza virus neuraminidase. The N-propionyl, N-chloroacetyl- and N-difluoroacetyl neuraminic acids were found to be substrates for recombinant Escherichia coli CMP sialate synthase, to give the corresponding CMP-N-acyl-neuraminic acids. CMP-N-propionyl neuraminic acid was found not to be a substrate for CMP-N-acetyl neuraminic acid hydroxylase from pig submandibular gland.

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More information

Published date: 2002
Keywords: surface-plasmon resonance, acetylneuraminic acid, glycolylneuraminic acid, hydroxylase, analogs, oligosaccharides, purification, inhibitors, synthetase, aldolase

Identifiers

Local EPrints ID: 19782
URI: http://eprints.soton.ac.uk/id/eprint/19782
ISSN: 0968-0896
PURE UUID: 2e2c63b7-044d-4c6b-a015-7635467bbcd0

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Date deposited: 20 Feb 2006
Last modified: 08 Jan 2022 09:51

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Contributors

Author: Andrew J. Humphrey
Author: Claire Fremann
Author: Peter Critchley
Author: Yanina Malykh
Author: Roland Schauer
Author: Timothy D.H. Bugg

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