Sialidase, receptor-binding and fusion-promotion activities of Newcastle disease virus haemagglutinin-neuraminidase glycoprotein: a mutational and kinetic study

The Journal of General Virology
Laura FerreiraEnrique Villar

Abstract

Mutations were generated in residues at the putative catalytic site of the haemagglutinin-neuraminidase (HN) protein of Newcastle disease virus Clone 30 strain (Arg498, Glu258, Tyr262, Tyr317 and Ser418) and their effects on its three associated activities were studied. Expression of the mutant proteins at the surface of HeLa cells was similar to that of the wild-type. Sialidase, receptor-binding and fusion-promotion activities were affected to different degrees for all mutants studied. Mutant Arg498Lys lost most of its sialidase activity, although it retained most of the receptor-binding activity, suggesting that, for the former activity, besides the presence of a basic residue, the proximity to the substrate molecule is also important, as Lys is shorter than Arg. Proximity also seems to be important in substrate recognition, since Tyr262Phe retained most of its sialidase activity while Tyr262Ser lost most of it. Also, Ser418Ala displayed most of the wild-type sialidase activity. However, a kinetic and thermodynamic study of the sialidase activity of the Tyr262Ser and Ser418Ala mutants was performed and revealed that the hydroxyl group of these residues also plays an important role in catalysis, since such activity was much le...Continue Reading

References

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Jan 20, 2004·European Journal of Biochemistry·Laura FerreiraIsabel Muñoz-Barroso

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Citations

Apr 1, 2006·Glycoconjugate Journal·Enrique Villar, Isabel Muñoz Barroso
Aug 8, 2012·Glycoconjugate Journal·Lorena Sánchez-FelipeIsabel Muñoz-Barroso
May 11, 2021·Reviews in Medical Virology·Aziz Ul-RahmanMuhammad Zubair Shabbir

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