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Article

Evolution of interleukin-15 for higher E. coli expression and solubility.

Protein engineering, design & selection : PEDS - 1 Mar 2011

Béhar Ghislaine, Solé Véronique, Defontaine Alain, Maillasson Mike, Quéméner Agnès, Jacques Yannick, Tellier Charles

Abstract excerpt

Directed evolution was used to generate IL-15 mutants with increased solubility and cytoplasmic over-expression in Escherichia coli. A protein solubility selection method was used in which the IL-15 gene was expressed as an N-terminal fusion to chloramphenicol acetyltransferase (CAT) as reporter protein. Clones that grew in the presence of high concentrations of chloramphenicol were then screened by ELISA to...

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Source

Identifiers

PMID: 21109548
DOI: 10.1093/protein/gzq107

Genes

CAT

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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