RESUMO
A panel of murine monoclonal antibodies (MAbs) to the human immunodeficiency virus type 1 trans-activator tat protein were characterized. The anti-tat MAbs were mapped to the different domains of the tat protein by Western blot (immunoblot) and Pepscan analyses. One-half of the MAbs tested mapped to the amino-terminal proline-rich region, and one-third of the MAbs tested mapped to the lysine-arginine-rich region of tat. The individual MAbs were tested for inhibition of tat-mediated trans activation, using a cell-based in vitro assay system. MAbs which mapped to the amino-terminal region of the tat protein demonstrated the highest degree of inhibition, whereas MAbs reactive to other portions of the molecule exhibited a less pronounced effect on tat function.
Assuntos
Anticorpos Monoclonais , Produtos do Gene tat/imunologia , HIV-1/imunologia , Transativadores/imunologia , Sequência de Aminoácidos , Western Blotting , Epitopos/análise , Produtos do Gene tat/genética , HIV-1/genética , Dados de Sequência Molecular , Oligopeptídeos/imunologia , Produtos do Gene tat do Vírus da Imunodeficiência HumanaRESUMO
Treponema pallidum can only be cultured in living animal tissue, such as rabbit testes. However, the extract of these organisms from the testicular material leaves the T. pallidum contaminated with tissue debris. This paper describes the separation of T. pallidum from the debris by continuous-particle electrophoresis. The importance of equilibration time before electrophoresis is discussed.
