Abstract:
:Escherichia coli heat-labile enterotoxin B subunit (EtxB) has been proposed as a potential protein carrier for the delivery of heterologous peptides to target cells, particularly for the oral delivery of epitopes to the mucosal immune system. In this study, two extensions to the C-terminus of EtxB were genetically engineered that correspond to a well-characterized neutralising epitope of glycoprotein D from herpes simplex virus (EtxB-gD) and to the C-terminal nine amino acids from the 38 kDa subunit of HSV-encoded ribonucleotide reductase (EtxB-R2). Here we describe the extracellular secretion of the two hybrid EtxBs from a marine Vibrio harbouring a broad-host range inducible expression vector containing the hybrid genes. Large amounts of intact fusion proteins (15-20 mg per liter of culture) were secreted into the medium upon induction. These hybrid proteins maintained the receptor-binding activity of the native toxin as well as being cross-reactive with anti-EtxB and anti-heterologous peptide monoclonal antibodies.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Marcello A,Loregian A,Palù G,Hirst TRdoi
10.1111/j.1574-6968.1994.tb06741.xsubject
Has Abstractpub_date
1994-03-15 00:00:00pages
47-51issue
1eissn
0378-1097issn
1574-6968journal_volume
117pub_type
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