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Structure-function analysis of two variants of mumps virus hemagglutinin-neuraminidase protein BJID
Santos-López,Gerardo; Scior,Thomas; Borraz-Argüello,María del Tránsito; Vallejo-Ruiz,Verónica; Herrera-Camacho,Irma; Tapia-Ramírez,José; Reyes-Leyva,Julio.
A point mutation from guanine (G) to adenine (A) at nucleotide position 1081 in the hemagglutinin-neuraminidase (HN) gene has been associated with neurovirulence of Urabe AM9 mumps virus vaccine. This mutation corresponds to a glutamic acid (E) to lysine (K) change at position 335 in the HN glycoprotein. We have experimentally demonstrated that two variants of Urabe AM9 strain (HN-A1081 and HN-G1081) differ in neurotropism, sialic acidbinding affinity and neuraminidase activity. In the present study, we performed a structure-function analysis of that amino acid substitution; the structures of HN protein of both Urabe AM9 strain variants were predicted. Based on our analysis, the E/K mutation changes the protein surface properties and to a lesser extent...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Hemagglutinin-neuraminidasa; Mumps virus; Paramyxovirus; 3D structure prediction; Sialic acid.
Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1413-86702009000100007
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