Provided is a neutralizing antibody employed in the study which immunoreacts with glycoprotein D of Herpes simplex virus. The antibody can be used in ELISA and Inhibition.
Figure 1 Neutralization of low-passage clinical isolates by human recombinant MAb HSV8.
These concentrations are comparable to those required for HSV8 neutralization of laboratory strains of HSV-1 and -2.
De Logu, A., Williamson, R. A., Rozenshteyn, R., Ramiro-Ibañez, F., Simpson, C. D., Burton, D. R., & Sanna, P. P. (1998). Characterization of a type-common human recombinant monoclonal antibody to herpes simplex virus with high therapeutic potential. Journal of Clinical Microbiology, 36(11), 3198-3204.
Figure 2 Syncytial inhibition as a function of HSV8 concentration.
At the higher concentrations tested (8 and 16 mg/ml), syncytium formation was completely prevented.
De Logu, A., Williamson, R. A., Rozenshteyn, R., Ramiro-Ibañez, F., Simpson, C. D., Burton, D. R., & Sanna, P. P. (1998). Characterization of a type-common human recombinant monoclonal antibody to herpes simplex virus with high therapeutic potential. Journal of Clinical Microbiology, 36(11), 3198-3204.
Figure 3 Inhibition of syncytium formation by human recombinant MAb HSV8.
HSV8 was effective in completely abolishing syncytium formation.
De Logu, A., Williamson, R. A., Rozenshteyn, R., Ramiro-Ibañez, F., Simpson, C. D., Burton, D. R., & Sanna, P. P. (1998). Characterization of a type-common human recombinant monoclonal antibody to herpes simplex virus with high therapeutic potential. Journal of Clinical Microbiology, 36(11), 3198-3204.
Figure 4 Epitope mapping of human recombinant MAb HSV8.
MAb H170, specific for the continuous group VII antigenic site, were used as controls.
De Logu, A., Williamson, R. A., Rozenshteyn, R., Ramiro-Ibañez, F., Simpson, C. D., Burton, D. R., & Sanna, P. P. (1998). Characterization of a type-common human recombinant monoclonal antibody to herpes simplex virus with high therapeutic potential. Journal of Clinical Microbiology, 36(11), 3198-3204.
Figure 5 Since human recombinant MAb HSV8 is directed to a discontinuous determinant, epitope mapping was carried out by competition with known antibodies in two ELISA configurations.
The y axis represents optical density (O.D.).
De Logu, A., Williamson, R. A., Rozenshteyn, R., Ramiro-Ibañez, F., Simpson, C. D., Burton, D. R., & Sanna, P. P. (1998). Characterization of a type-common human recombinant monoclonal antibody to herpes simplex virus with high therapeutic potential. Journal of Clinical Microbiology, 36(11), 3198-3204.
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