tailieunhanh - Báo cáo y học: " Interaction of human dipeptidyl peptidase IV and human immunodeficiency virus type-1 transcription transactivator in Sf9 cells"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Interaction of human dipeptidyl peptidase IV and human immunodeficiency virus type-1 transcription transactivator in Sf9 cells | Tansi et al. Virology Journal 2010 7 267 http content 7 1 267 VIROLOGY JOURNAL RESEARCH Open Access Interaction of human dipeptidyl peptidase IV and human immunodeficiency virus type-1 transcription transactivator in Sf9 cells 1 2 2 2 11 Felista L Tansi Véronique Blanchard Markus Berger Rudolf Tauber Werner Reutter Hua Fan Abstract Background Dipeptidyl peptidase IV DPPIV also known as the T cell activation marker CD26 is a multifunctional protein which is involved in various biological processes. The association of human-DPPIV with components of the human immunodeficiency virus type-1 HIV1 is well documented and raised some discussions. Several reports implicated the interaction of human-DPPIV with the HIV1 transcription transactivator protein HIV1-Tat and the inhibition of the dipeptidyl peptidase activity of DPPIV by the HIV1-Tat protein. Furthermore enzyme kinetic data implied another binding site for the HIV1-Tat other than the active centre of DPPIV. However the biological significance of this interaction of the HIV1-Tat protein and human-DPPIV has not been studied yet. Therefore we focused on the interaction of HIV1-Tat protein with DPPIV and investigated the subsequent biological consequences of this interaction in Spodoptera frugiperda cells using the BAC-TO-BAC baculovirus system. Results The HIV1-Tat protein Tat-BRU co-localized and co-immunoprecipitated with human-DPPIV protein following co-expression in the baculovirus-driven Sf9 cell expression system. Furthermore tyrosine phosphorylation of DPPIV protein was up-regulated in Tat DPPIV-co-expressing cells after 72 h culturing and also in DPPIV-expressing Sf9 cells after application of purified recombinant Tat protein. As opposed to the expression of Tat alone serine phosphorylation of the Tat protein was decreased when co-expressed with human-DPPIV protein. Conclusions We show for the first time that human-DPPIV and HIV1-Tat co-immunoprecipitate. Furthermore our findings indicate that