<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>3(1)</volume><submitter>Tomisawa S</submitter><pubmed_abstract>Antibacterial factor 2 (ABF-2) is a 67-residue antimicrobial peptide derived from the nematode Caenorhabditis elegans. Although it has been reported that ABF-2 exerts in vitro microbicidal activity against a range of bacteria and fungi, the structure of ABF-2 has not yet been solved. To enable structural studies of ABF-2 by NMR spectroscopy, a large amount of isotopically labeled ABF-2 is essential. However, the direct expression of ABF-2 in Escherichia coli is difficult to achieve due to its instability. Therefore, we applied a coexpression method to the production of ABF-2 in order to enhance the inclusion body formation of ABF-2. The inclusion body formation of ABF-2 was vastly enhanced by coexpression of aggregation-prone proteins (partner proteins). By using this method, we succeeded </pubmed_abstract><journal>AMB Express</journal><pagination>45</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3751704</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Overexpression of an antimicrobial peptide derived from C. elegans using an aggregation-prone protein coexpression system.</pubmed_title><pmcid>PMC3751704</pmcid><pubmed_authors>Kato Y</pubmed_authors><pubmed_authors>Kawano K</pubmed_authors><pubmed_authors>Kikukawa T</pubmed_authors><pubmed_authors>Demura M</pubmed_authors><pubmed_authors>Kumaki Y</pubmed_authors><pubmed_authors>Ohki S</pubmed_authors><pubmed_authors>Mizuguchi M</pubmed_authors><pubmed_authors>Miyazawa M</pubmed_authors><pubmed_authors>Kamiya M</pubmed_authors><pubmed_authors>Aizawa T</pubmed_authors><pubmed_authors>Hojo E</pubmed_authors><pubmed_authors>Tomisawa S</pubmed_authors><pubmed_authors>Umetsu Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>Overexpression of an antimicrobial peptide derived from C. elegans using an aggregation-prone protein coexpression system.</name><description>Antibacterial factor 2 (ABF-2) is a 67-residue antimicrobial peptide derived from the nematode Caenorhabditis elegans. Although it has been reported that ABF-2 exerts in vitro microbicidal activity against a range of bacteria and fungi, the structure of ABF-2 has not yet been solved. To enable structural studies of ABF-2 by NMR spectroscopy, a large amount of isotopically labeled ABF-2 is essential. However, the direct expression of ABF-2 in Escherichia coli is difficult to achieve due to its instability. Therefore, we applied a coexpression method to the production of ABF-2 in order to enhance the inclusion body formation of ABF-2. The inclusion body formation of ABF-2 was vastly enhanced by coexpression of aggregation-prone proteins (partner proteins). By using this method, we succeeded </description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Aug</publication><modification>2025-04-18T15:10:39.37Z</modification><creation>2019-03-27T01:14:58Z</creation></dates><accession>S-EPMC3751704</accession><cross_references><pubmed>23945047</pubmed><doi>10.1186/2191-0855-3-45</doi></cross_references></HashMap>