H2N2V1, Main, Exploration, bibRecord, 001D70

A Sialic Acid-derived Phosphonate Analog Inhibits Different Strains of Influenza Virus Neuraminidase with Different Efficiencies

Identifieur interne : 001D70 ( Main/Exploration ); précédent : 001D69; suivant : 001D71

A Sialic Acid-derived Phosphonate Analog Inhibits Different Strains of Influenza Virus Neuraminidase with Different Efficiencies

Auteurs : Clinton L. White [Suisse] ; Musiri N. Janakiraman [Suisse] ; Graeme W. Laver [Suisse] ; Cédric Philippon [Suisse] ; Andrea Vasella [Suisse] ; Gillian M. Air [Suisse] ; Ming Luo [Suisse]

Source :

Journal of Molecular Biology [ 0022-2836 ] ; 1995.

RBID : ISTEX:EDDD86A22A2967C9BE79FD4458B509E24B839D38

English descriptors

Abstract

Abstract: A phosphonate analog ofN-acetyl neuraminic acid (PANA) has been designed as a potential neuraminidase (NA) inhibitor and synthesized as both the α (ePANA) anomers. Inhibition of type A (N2) and type B NA activity by ePANA was approximately a 100-fold better than by sialic acid, but inhibition of type A (N9) NA was only ten-fold better than by sialic acid. The aPANA compound was not a strong inhibitor for any of the NA strains tested. The crystal structures at 2.4 Å resolution of ePANA complexed to type A (N2) NA, type A (N9) NA and type B NA and aPANA complexed to type A (N2) NA showed that neither of the PANA compounds distorted the NA active site upon binding. No significant differences in the NA-ePANA complex structures were found to explain the anomalous inhibition of N9 neuraminidase by ePANA. We put forward the hypothesis that an increase in the ePANA inhibition compared to that caused bysialic acid is due to (1) a stronger electrostatic interaction between the inhibitor phosphonyl group and the active site arginine pocket and (2) a lower distortion energy requirement for binding of ePANA.

Url:

https://api.istex.fr/ark:/67375/6H6-B7S4KXHB-1/fulltext.pdf

DOI: 10.1006/jmbi.1994.0051

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>PANA</term>
<term>X-ray structure</term>
<term>antiviral</term>
<term>neuraminyl phosphonic acid</term>
<term>structure-based drug design</term>
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<keywords scheme="Teeft" xml:lang="en"><term>Acetamido</term>
<term>Active site</term>
<term>Active site arginine pocket</term>
<term>Active site backbone atoms</term>
<term>Active site backbone atoms group</term>
<term>Active site residues</term>
<term>Active site structure</term>
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<term>Arginine</term>
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<term>Assay</term>
<term>Axial phosphonate</term>
<term>Carboxyl</term>
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<term>Complex table</term>
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<term>Fcalc</term>
<term>Glycerol</term>
<term>Hydroxyl</term>
<term>Hydroxyl group</term>
<term>Inhibition</term>
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<term>Inhibitor acid group</term>
<term>Inhibitor acidic group</term>
<term>Inhibitor binding</term>
<term>Inhibitor complexes</term>
<term>Inhibitor ring</term>
<term>Inhibitory activity</term>
<term>Itzstein</term>
<term>Janakiraman</term>
<term>Laver</term>
<term>Modeling</term>
<term>Nana</term>
<term>Native coordinates</term>
<term>Neuraminic acid</term>
<term>Neuraminidase</term>
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<term>Pana</term>
<term>Pana inhibitors</term>
<term>Phosphonate</term>
<term>Phosphonate analog</term>
<term>Phosphonate group</term>
<term>Phosphonoyl</term>
<term>Phosphonoyl group</term>
<term>Polyethylene glycol</term>
<term>Pyranosidic</term>
<term>Pyranosidic ring</term>
<term>Ring atoms</term>
<term>Ring conformation</term>
<term>Room temperature</term>
<term>Sialic</term>
<term>Sialic acid</term>
<term>Strong interaction</term>
<term>Structure factors</term>
<term>Sugar ring</term>
<term>Superposition</term>
<term>Uorometric assay</term>
<term>Varghese</term>
<term>Vasella</term>
<term>Viral</term>
<term>Virus neuraminidase</term>
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<front><div type="abstract" xml:lang="en">Abstract: A phosphonate analog ofN-acetyl neuraminic acid (PANA) has been designed as a potential neuraminidase (NA) inhibitor and synthesized as both the α (ePANA) anomers. Inhibition of type A (N2) and type B NA activity by ePANA was approximately a 100-fold better than by sialic acid, but inhibition of type A (N9) NA was only ten-fold better than by sialic acid. The aPANA compound was not a strong inhibitor for any of the NA strains tested. The crystal structures at 2.4 Å resolution of ePANA complexed to type A (N2) NA, type A (N9) NA and type B NA and aPANA complexed to type A (N2) NA showed that neither of the PANA compounds distorted the NA active site upon binding. No significant differences in the NA-ePANA complex structures were found to explain the anomalous inhibition of N9 neuraminidase by ePANA. We put forward the hypothesis that an increase in the ePANA inhibition compared to that caused bysialic acid is due to (1) a stronger electrostatic interaction between the inhibitor phosphonyl group and the active site arginine pocket and (2) a lower distortion energy requirement for binding of ePANA.</div>
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A Sialic Acid-derived Phosphonate Analog Inhibits Different Strains of Influenza Virus Neuraminidase with Different Efficiencies

A Sialic Acid-derived Phosphonate Analog Inhibits Different Strains of Influenza Virus Neuraminidase with Different Efficiencies

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Abstract

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