| Literature DB >> 23100780 |
Majid Alipour1, Seyed Latif Mousavi Gargari, Iraj Rasooli.
Abstract
The gene coding for ferric enterobactin binding protein from E. coli O157:H7 was amplifi ed. This gene was cloned and expressed as C-terminal His (6)-tagged protein. The SDS-PAGE analysis of the total protein revealed only two distinct bands, with molecular masses of 31kDa and 34kDa. The Ni-NTA chromatography purifi ed FepB and the osmotically shocked periplasmic fraction of IPTG induced cells showed only a single band of 31 kDa. Polyclonal mouse antibody was raised against the recombinant protein during 4 weeks after immunization. Western blot analysis of the recombinant FepB with mouse antiserum revealeda single band of 31 kDa. Identification and purification of FepB helped reveal its appropriate molecular mass. Polyclonal antibody raised against the recombinant protein reacted with bacterial FepB. The recombinant protein FepB could have a protective effect against E. coli O157:H7 and might be useful as an effective vaccine.Entities:
Keywords: E. coli; FepB; Ferric enterobactin; Periplasmic binding protein
Year: 2009 PMID: 23100780 PMCID: PMC3450013 DOI: 10.1007/s12088-009-0044-7
Source DB: PubMed Journal: Indian J Microbiol ISSN: 0046-8991 Impact factor: 2.461