Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: The effects of N-terminal insertion into VSV-G of an scFv peptide | Virology Journal BioMed Central Research The effects of N-terminal insertion into VSV-G of an scFv peptide Hanna Dreja and Marc Piechaczyk Open Access Address Institut de Génétique Moléculaire de Montpellier UMR 5535 IFR122 CNRS France Email Hanna Dreja - dreja@ Marc Piechaczyk - piechaczyk@ Corresponding author Published 02 September 2006 Received 21 June 2006 Accepted 02 September 2006 Virology journal 2006 3 69 doi l743-422X-3-69 This article is available from http content 3 1 69 2006 Dreja and Piechaczyk licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Recombinant retroviruses including lentiviruses are the most widely used vectors for both in vitro and in vivo stable gene transfer. However the inability to selectively deliver transgenes into cells of interest limits the use of this technology. Due to its wide tropism stability and ability to pseudotype a range of viral vectors vesicular stomatitis virus G protein VSV-G is the most commonly used pseudotyping protein. Here we attempted to engineer this protein for targeting purposes. Chimaeric VSV-G proteins were constructed by linking a cell-directing single-chain antibody scFv to its N-terminal. We show that the chimaeric VSV-G molecules can integrate into retroviral and lentiviral particles. HIV- 1 particles pseudotyped with VSV-G linked to an scFv against human Major Histocompatibility Complex class I MHC-I bind strongly and specifically to human cells. Also this novel molecule preferentially drives lentiviral transduction of human cells although the titre is considerably lower that viruses pseudotyped with VSV-G. This is likely due to the inefficient fusion activity of the modified protein. To our knowledge .
