The intestinal tract is the shared locus of intestinal epithelial cells, immune cells, nutrient digestion and absorption, and microbial survival. The gut in animals faces continuous challenges in communicating with the external environment. Threats from endogenous imbalance and exogenous feeds, especially pathogens, could trigger a disorder of homeostasis, leading to intestinal disease and even systematic disease risk. As a part of the intestinal protective barrier, endogenous host defense peptides (HDPs) play multiple beneficial physiological roles in the gut mucosa. Moreover, enhancing endogenous HDPs is being developed as a new strategy for resisting pathogens and commensal microbes, and to maintain intestinal health and reduce antibiotic use. In recent years, multiple nutrients such as branched-chain amino acids, SCFAs, lactose, zinc, and cholecalciferol (vitamin D3) have been reported to significantly increase HDP expression. Nutritional intervention has received more attention and is viewed as a promising means to defend against pathogenic infections and intestinal inflammation. The present review focuses on current discoveries surrounding HDP expression and nutritional regulation of mechanisms in the gut. Our aim is to provide a comprehensive overview, referable tactics, and novel opinions.
Bibliographical noteFunding Information:
Supported by National Key R&D Program of China grants 2018YFD0500601 and 2017YFD0500501 (both to XM), National Natural Science Foundation of China grants 31829004 and 31722054(to XM), College of Animal Science and Technology “Young Talents Program”at China Agricultural University grant 2017DKA001, Beijing Nova Programme Interdisciplinary Cooperation Project grant xxjc201804, 111 Project grant B16044, and the Developmental Fund for Animal Science by Shenzhen Jinxinnong Feed Co., Ltd. Author disclosures: JW, NM, LJJ, and XM, no conflicts of interest. Address correspondence to XM (e-mail: firstname.lastname@example.org). Abbreviations used: AMP, antimicrobial peptide; AvBD9, avianβ-defensin 9; BCAA, branched-chain amino acid; CAMP, cathelicidin antimicrobial peptides; C/EBPε, CCAAT/enhancer binding protein ε; ERK, extracellular signal regulated protein kinase; FFAR, free fatty acid receptor; GPCR, G protein–coupled receptor; HAT, histone acetyltransferase; hBD, humanβ-defensin; HDAC, histone deacetylase; HDP, host defense peptide; JNK, c-Jun N-terminal kinase; LCFA, long-chain fatty acid; LL-37, cathelicidin antimicrobial peptide LL-37; LYZ, lysozyme; MAPK, mitogen-activated protein kinase; MCFA, medium-chain fatty acid; MEK, mitogen-activated protein kinase kinase; mTOR, mammalian target of rapamycin; NOD, nucleotide-binding oligomerization domain protein; pBD, porcineβ-defensin; PR-39, cathelicidin proline-arginine-rich-39; TLR, Toll-like receptor; VDR, vitamin D receptor; 1,25(OH)2-D3, 1,25-dihydroxycholecalciferol.
Copyright © American Society for Nutrition 2019.
Copyright 2020 Elsevier B.V., All rights reserved.
- antibiotic alternative
- host defense peptides
PubMed: MeSH publication types
- Journal Article
- Research Support, Non-U.S. Gov't