Abstract:
:Chimeric proteins composed of ricin toxin A chain (RTA) and staphylococcal protein A (PA) have been produced in E. coli. Constructs consisting of N-terminal RTA and C-terminal PA (RTA-PA) or N-terminal PA and C-terminal (PA-RTA) were capable of binding to immunoglobulin G (via PA) and of specifically depurinating 28 S ribosomal RNA (via RTA). However, neither fusion protein was cytotoxic to antigen-bearing target cells in the presence of an appropriate monoclonal antibody presumably because the RTA could not be released from the PA within the cytosol where the ribosomal substrate of RTA is located. The overcome this, a short amino acid sequence from diphtheria toxin was engineered between the RTA and PA to produce a disulfide-linked loop containing a trypsin sensitive cleavage site. Cleavage of this fusion protein with trypsin converted the RTA-DT-PA to the two chain form consisting of RTA linked by a disulfide bond to PA. The cleaved fusion protein was highly toxic to Daudi cells coated with anti-immunoglobulin antibody suggesting that the RTA could be released from the PA by reduction within the cytosol.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
O'Hare M,Brown AN,Hussain K,Gebhardt A,Watson G,Roberts LM,Vitetta ES,Thorpe PE,Lord JMdoi
10.1016/0014-5793(90)81084-2subject
Has Abstractpub_date
1990-10-29 00:00:00pages
200-4issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(90)81084-2journal_volume
273pub_type
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