Navegando por Palavras-chave "picornavirus"

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    Poliovirus 3C proteinase inhibition by organotelluranes
    (Walter de Gruyter & Co, 2011-04-01) Gouvea, Iuri E. [UNIFESP]; Santos, Jorge A. N. [UNIFESP]; Burlandy, Fernanda M.; Tersariol, Ivarne L. S.; Silva, Edson E. da; Juliano, Maria A. [UNIFESP]; Juliano, Luiz [UNIFESP]; Cunha, Rodrigo L. O. R. [UNIFESP]; Universidade Federal de São Paulo (UNIFESP); Inst Oswaldo Cruz; Univ Mogi das Cruzes; Universidade Federal do ABC (UFABC)
    The 3C proteinase, essential for human poliovirus (PV) replication, has unique characteristics as its three-dimensional structure resembles chymotrypsin, but its catalytic nucleophile is a cysteine SH group rather than the OH group of serine. Here, we describe the use of tellurium compounds as inhibitors of PV3C proteinase. A rapid, stoichiometric and covalent inactivation of PV3C was observed with both a chloro-telluroxetane and a bis-vinylic organotellurane. These compounds also inhibit human cathepsins B, L, S, and K with second order rate constants higher than those obtained for PV3C. Chloro-telluroxetane inhibits replication of PV in human embryonic rhabdomyosarcoma cells in the low micromolar range and below the toxic level for the host cells. Bis-vinylic organotellurane is more effective as antiviral agent but reduces the cell viability by 20% at 10 mM, a concentration almost completely inhibiting virus growth. This is the first description of inhibition of viral 3C proteinase with antiviral property by this class of compounds.