Structure-function analysis of CCL28 in the development of post-viral asthma

Monica A. Thomas, Becky J. Buelow, Amanda M. Nevins, Stephanie E. Jones, Francis C. Peterson, Rebekah L. Gundry, Mitchell H. Grayson, Brian F. Volkman

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

Background: CCL28 is associated with the pathogenesis of acute post-viral asthma. Results: In the absence of viral infection, natively folded CCL28 can induce asthma pathology, whereas unfolded CCL28 cannot. Conclusion: The structure of CCL28 is critical for its role in asthma pathogenesis. Significance: Inhibition of CCL28 presents a novel therapeutic option for the prevention of post-viral asthma.

Original languageEnglish (US)
Pages (from-to)4528-4536
Number of pages9
JournalJournal of Biological Chemistry
Volume290
Issue number7
DOIs
StatePublished - Feb 13 2015

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Structure-function analysis of CCL28 in the development of post-viral asthma'. Together they form a unique fingerprint.

  • Cite this

    Thomas, M. A., Buelow, B. J., Nevins, A. M., Jones, S. E., Peterson, F. C., Gundry, R. L., Grayson, M. H., & Volkman, B. F. (2015). Structure-function analysis of CCL28 in the development of post-viral asthma. Journal of Biological Chemistry, 290(7), 4528-4536. https://doi.org/10.1074/jbc.M114.627786