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Structural basis for Streptococcus pneumoniae NanA inhibition by influenza antivirals zanamivir and oseltamivir carboxylate.

Gut H, Xu G, Taylor GL, Walsh MA
J Mol Biol 409 496-503 (2011)
Related entries: 2ya4, 2ya5, 2ya6, 2ya7

Cited: 29 times
EuropePMC logo PMID: 21514303

Abstract

The human pathogen Streptococcus pneumoniae is the major cause of bacterial meningitis, respiratory tract infection, septicemia, and otitis media. The bacterium expresses neuraminidase (NA) proteins that contribute to pathogenesis by cleaving sialic acids from host glycoconjugates, thereby enhancing biofilm formation and colonization. Recent in vivo experiments have shown that antiviral compounds, widely used in clinics and designed to inhibit influenza NA, significantly reduce biofilm formation and nasopharyngeal colonization of S. pneumoniae in mice. Here, we present the structural basis for the beneficial effect of these compounds against pneumococcal infection. Crystal structures of pneumococcal NanA in complex with zanamivir and oseltamivir carboxylate are discussed, correlated with measured inhibitory constants K(i), and compared with the binding modes of the inhibitors in the viral enzyme. Inhibitor structures show for the first time how clinically approved anti-influenza compounds interact with an NA of the human pathogen S. pneumoniae and give a rational explanation for their antibacterial effects.

Articles - 2ya8 mentioned but not cited (1)

  1. Sequence diversity of NanA manifests in distinct enzyme kinetics and inhibitor susceptibility. Xu Z, von Grafenstein S, Walther E, Fuchs JE, Liedl KR, Sauerbrei A, Schmidtke M. Sci Rep 6 25169 (2016)


Reviews citing this publication (6)

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Articles citing this publication (22)

  1. Discovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation. Tailford LE, Owen CD, Walshaw J, Crost EH, Hardy-Goddard J, Le Gall G, de Vos WM, Taylor GL, Juge N. Nat Commun 6 7624 (2015)
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  15. The elusive crystal structure of the neuraminidase inhibitor Tamiflu (oseltamivir phosphate): molecular details of action. Naumov P, Yasuda N, Rabeh WM, Bernstein J. Chem. Commun. (Camb.) 49 1948-1950 (2013)
  16. An easy, rapid, and sensitive method for detection of drug-resistant influenza virus by using a sialidase fluorescent imaging probe, BTP3-Neu5Ac. Kato D, Kurebayashi Y, Takahashi T, Otsubo T, Otake H, Yamazaki M, Tamoto C, Minami A, Ikeda K, Suzuki T. PLoS ONE 13 e0200761 (2018)
  17. Exploration of Binding Mechanism of a Potential Streptococcus pneumoniae Neuraminidase Inhibitor from Herbaceous Plants by Molecular Simulation. Guan S, Zhu K, Dong Y, Li H, Yang S, Wang S, Shan Y. Int J Mol Sci 21 (2020)
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