A knottin scaffold directs the CXC-chemokine–binding specificity of tick evasins

Volume: 294, Issue: 29, Pages: 11199 - 11212
Published: Jul 1, 2019
Abstract
Tick evasins (EVAs) bind either CC- or CXC-chemokines by a poorly understood promiscuous or "one-to-many" mechanism to neutralize inflammation. Because EVAs potently inhibit inflammation in many preclinical models, highlighting their potential as biological therapeutics for inflammatory diseases, we sought to further unravel the CXC-chemokine-EVA interactions. Using yeast surface display, we identified and characterized 27 novel...
Paper Details
Title
A knottin scaffold directs the CXC-chemokine–binding specificity of tick evasins
Published Date
Jul 1, 2019
Volume
294
Issue
29
Pages
11199 - 11212
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