Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Vaccine based on a ubiquitous cysteinyl protease and streptococcal pyrogenic exotoxin A protects against Streptococcus pyogenes sepsis and toxic shock. | Journal of Immune Based Therapies and Vaccines BioMed Central Original research Vaccine based on a ubiquitous cysteinyl protease and streptococcal pyrogenic exotoxin A protects against Streptococcus pyogenes sepsis and toxic shock Robert G Ulrich Open Access Address Laboratory of Molecular Immunology Army Medical Research Institute of Infectious Diseases 1425 Porter Street Frederick Maryland 21702 USA Email Robert G Ulrich - rulrich@ Published 31 October 2008 Received 7 June 2008 Journal of Immune Based Therapies and Vaccines 2008 6 8 doi l 476-8518-6-8 Accepted 31 October 2008 This article is available from http content 6 l 8 2008 Ulrich 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 The gram-positive bacterium Streptococcus pyogenes is a common pathogen of humans that causes invasive infections toxic-shock syndrome rheumatic fever necrotizing fasciitis and other diseases. Detection of antibiotic resistance in clinical isolates has renewed interest in development of new vaccine approaches for control S. pyogenes sepsis. In the study presented a novel protein vaccine was examined. The vaccine was based on a recombinant protein fusion between streptococcal pyrogenic exotoxin B SpeB a cysteinyl protease expressed by all clinical isolates and streptococcal pyrogenic exotoxin A SpeA a superantigen produced by a large subset of isolates. Results A novel protein was produced by mutating the catalytic site of SpeB and the receptor binding surface of SpeA in a fusion of the two polypeptides. Vaccination of HLA-DQ8 transgenic mice with the SpeA-SpeB fusion protein protected against a .
