<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Quintero D</submitter><funding>NIGMS NIH HHS</funding><pagination>2079-2094</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6883771</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>28(12)</volume><pubmed_abstract>Sunflower trypsin inhibitor (SFTI) is a 14-amino-acid bicyclic peptide that contains a single internal disulfide bond. We initially constructed chimeras of SFTI with N-terminal secretion signals from the &lt;i>Escherichia coli&lt;/i> OmpA and &lt;i>Pseudomonas aeruginosa&lt;/i> ToxA, but only detected small amounts of protease inhibition resulting from these constructs. A substantially higher degree of protease inhibition was detected from a C-terminal SFTI fusion with &lt;i>E. coli&lt;/i> YebF, which radiated more than a centimeter from an individual colony of &lt;i>E. coli&lt;/i> using a culture-based inhibitor assay. Inhibitory activity was further improved in YebF-SFTI fusions by the addition of a trypsin cleavage signal immediately upstream of SFTI, and resulted in production of a 14-amino-acid, disulfide-bo</pubmed_abstract><journal>Journal of microbiology and biotechnology</journal><pubmed_title>Co-Expression of a Chimeric Protease Inhibitor Secreted by a Tumor-Targeted &lt;i>Salmonella&lt;/i> Protects Therapeutic Proteins from Proteolytic Degradation.</pubmed_title><pmcid>PMC6883771</pmcid><funding_grant_id>SC3 GM098207</funding_grant_id><funding_grant_id>R25 GM063787</funding_grant_id><pubmed_authors>Vincent L</pubmed_authors><pubmed_authors>Quintero D</pubmed_authors><pubmed_authors>Carrafa J</pubmed_authors><pubmed_authors>Wohlschlegel J</pubmed_authors><pubmed_authors>Lee HJ</pubmed_authors><pubmed_authors>Bermudes D</pubmed_authors></additional><is_claimable>false</is_claimable><name>Co-Expression of a Chimeric Protease Inhibitor Secreted by a Tumor-Targeted &lt;i>Salmonella&lt;/i> Protects Therapeutic Proteins from Proteolytic Degradation.</name><description>Sunflower trypsin inhibitor (SFTI) is a 14-amino-acid bicyclic peptide that contains a single internal disulfide bond. We initially constructed chimeras of SFTI with N-terminal secretion signals from the &lt;i>Escherichia coli&lt;/i> OmpA and &lt;i>Pseudomonas aeruginosa&lt;/i> ToxA, but only detected small amounts of protease inhibition resulting from these constructs. A substantially higher degree of protease inhibition was detected from a C-terminal SFTI fusion with &lt;i>E. coli&lt;/i> YebF, which radiated more than a centimeter from an individual colony of &lt;i>E. coli&lt;/i> using a culture-based inhibitor assay. Inhibitory activity was further improved in YebF-SFTI fusions by the addition of a trypsin cleavage signal immediately upstream of SFTI, and resulted in production of a 14-amino-acid, disulfide-bo</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Dec</publication><modification>2026-05-03T14:48:21.199Z</modification><creation>2020-10-29T12:19:41Z</creation></dates><accession>S-EPMC6883771</accession><cross_references><pubmed>30661346</pubmed><doi>10.4014/jmb.1807.08036</doi><doi>10.4014/jmb.1808.08036</doi></cross_references></HashMap>