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A Requirement for Metamorphic Interconversion in the Antimicrobial Activity of Chemokine XCL1. Biochemistry 2016 07 12;55(27):3784-93



Pubmed ID


Pubmed Central ID




Scopus ID

2-s2.0-84978370474   5 Citations


Chemokines make up a superfamily of ∼50 small secreted proteins (8-12 kDa) involved in a host of physiological processes and disease states, with several previously shown to have direct antimicrobial activity comparable to that of defensins in efficacy. XCL1 is a unique metamorphic protein that interconverts between the canonical chemokine fold and a novel all-β-sheet dimer. Phylogenetic analysis suggests that, within the chemokine family, XCL1 is most closely related to CCL20, which exhibits antibacterial activity. The in vitro antimicrobial activity of WT-XCL1 and structural variants was quantified using a radial diffusion assay (RDA) and in solution bactericidal assays against Gram-positive and Gram-negative species of bacteria. Comparisons of WT-XCL1 with variants that limit metamorphic interconversion showed a loss of antimicrobial activity when restricted to the conserved chemokine fold. These results suggest that metamorphic folding of XCL1 is required for potent antimicrobial activity.

Author List

Nevins AM, Subramanian A, Tapia JL, Delgado DP, Tyler RC, Jensen DR, Ouellette AJ, Volkman BF


Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Anti-Bacterial Agents
Chemokines, C
Protein Binding
Protein Folding
Sequence Homology, Amino Acid
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