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: Recombinant norovirus-specific scFv inhibit virus-like particle binding to cellular ligands | Virology Journal BioMed Central Research Recombinant norovirus-specific scFv inhibit virus-like particle binding to cellular ligands Khalil Ettayebi and Michele E Hardy Address Veterinary Molecular Biology Montana State University Bozeman MT 59717 USA Email Khalil Ettayebi - kettayeb@ Michele E Hardy - mhardy@ Corresponding author Open Access Published 31 January 2008 Received 30 November 2007 Accepted 31 January 2008 Virology Journal 2008 5 21 doi l 743-422X-5-2I This article is available from http content 5 1 21 2008 Ettayebi and Hardy 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 Background Noroviruses cause epidemic outbreaks of gastrointestinal illness in all age-groups. The rapid onset and ease of person-to-person transmission suggest that inhibitors of the initial steps of virus binding to susceptible cells have value in limiting spread and outbreak persistence. We previously generated a monoclonal antibody mAb that blocks binding of recombinant norovirus-like particles VLP to Caco-2 intestinal cells and inhibits VLP-mediated hemagglutination. In this study we engineered the antigen binding domains of mAb into a single chain variable fragment scFv and tested whether these scFv could function as cell binding inhibitors similar to the parent mAb. Results The construct was engineered to encode the light VL and heavy VH variable domains of mAb separated by a flexible peptide linker and this recombinant protein was expressed in Pichia pastoris. Purified recognized native VLPs by immunoblot inhibited VLP-mediated hemagglutination and blocked VLP binding to H carbohydrate antigen expressed on the surface of a CHO cell line stably .
