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  • EDEVAG, G, et al. (författare)
  • Enzyme-linked immunosorbent assay-based inhibition test for neutralizing antibodies to polioviruses as an alternative to the neutralization test in tissue culture
  • 1995
  • Ingår i: Journal of clinical microbiology. - : American Society for Microbiology. - 0095-1137 .- 1098-660X. ; 33:11, s. 2927-2930
  • Tidskriftsartikel (refereegranskat)abstract
    • A poliovirus-binding inhibition test (PoBI test) was established for the quantitative determination of antibodies to polioviruses and was evaluated in comparison with the conventional neutralization test (NT). The first step of the PoBI test is an incubation of serial dilutions of test samples with inactivated poliovirus followed by the detection of free viral epitopes by a double antibody sandwich enzyme-linked immunosorbent assay with type-specific capture polyclonal antisera and type-specific neutralizing monoclonal indicator antibodies. A comparison of the PoBI test with the conventional NT for antibodies to all three types in 100 human serum samples showed excellent correlations (r > 0.95) over a wide range of antibody concentrations. The PoBI test, not necessitating live virus and tissue culture facilities, could be a simple alternative to the NT, and the principle of the assay is potentially applicable to other microbial systems.
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  • Mirazimi, A, et al. (författare)
  • Free thiol groups are essential for infectivity of human cytomegalovirus
  • 1999
  • Ingår i: The Journal of general virology. - : Microbiology Society. - 0022-1317 .- 1465-2099. ; 8080 ( Pt 11), s. 2861-2865
  • Tidskriftsartikel (refereegranskat)abstract
    • The membrane-impermeable thiol blocker 5′5-dithiobis 2- nitrobenzoic acid (DTNB) blocked infectivity of human cytomegalovirus (CMV) although the virus still bound to cells. DTNB-treated CMV regained 65% of its infectivity after incubation with the disulfide bond-reducing agent dithiothreitol. These observations suggest that free thiol groups on CMV are required for infectivity and may participate in disulfide bond formation during virus entry.
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