NDLI: Proteolysis Triggers Self-Assembly and Unmasks Innate Immune Function of a Human α-Defensin Peptide

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Proteolysis Triggers Self-Assembly and Unmasks Innate Immune Function of a Human α-Defensin Peptide

Content Provider	PubMed Central
Author	Chairatana, Phoom Chu, Hiutung Castillo, Patricia A. Shen, Bo Bevins, Charles L. Nolan, Elizabeth M.
Abstract	Human α-defensin 6 (HD6) is a unique peptide of the defensin family that provides innate immunity in the intestine by self-assembling to form high-order oligomers that entrap bacteria and prevent host cell invasion. Here, we report critical steps in the self-assembly pathway of HD6. We demonstrate that HD6 is localized in secretory granules of small intestinal Paneth cells. HD6 is stored in these granules as an 81-residue propeptide (proHD6), and is recovered from ileal lumen as a 32-residue mature peptide. The propeptide neither forms higher-order oligomers, nor agglutinates bacteria, nor prevents Listeria monocytogenes invasion into epithelial cells. The Paneth cell granules also contain the protease trypsin, and trypsin-catalyzed hydrolysis of proHD6 liberates mature HD6, unmasking its latent activities. This work illustrates a remarkable example of how nature utilizes a propeptide strategy to spatially and temporally control peptide self-assembly, and thereby initiates innate immune function in the human intestine.
Related Links	http://dx.doi.org/10.1039/C5SC04194E
Ending Page	1752
Page Count	15
Starting Page	1738
File Format	PDF
ISSN	20416539
e-ISSN	20416539
Journal	Chemical science (Royal Society of Chemistry : 2010)
Issue Number	3
Volume Number	7
Language	English
Publisher Date	2016-03-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Chemistry

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