Creation of a biologically active interleukin-5 monomer

Richard R. Dickason, David P. Huston

Research output: Contribution to journalArticlepeer-review

55 Scopus citations


Interleukin-5 (IL-5) specifically induces the differentiation of eosinophils, which are important in host defence and the pathogenesis of allergies and asthma. Structurally, IL-5 is a unique member of the short-chain helical-bundle subfamily of cytokines whose canonical motif contains four helices (A-D) arranged in an up-up-down-down topology. In contrast to other subfamily members, which fold unimolecularly into a single helical bundle, IL-5 forms a pair of helical bundles by the interdigitation of two identical monomers that contribute a D helix to the other's A-C helices. We predicted that the lack of bioactivity by an IL-5 monomer was due to a short loop between helices C and D which physically prevents unimolecular folding of helix D into a functionally obligate structural motif. Here we report that, by lengthening this loop, we have engineered an insertional mutant of IL-5 that was expressed as a monomer with biological activity similar to that of native IL-5. These studies demonstrate that all of the structural features necessary for IL-5 to function are contained within a single helical bundle.

Original languageEnglish (US)
Pages (from-to)652-655
Number of pages4
Issue number6566
StatePublished - Feb 15 1996

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Creation of a biologically active interleukin-5 monomer'. Together they form a unique fingerprint.

Cite this