黏膜层蛋白质糖基化修饰调控畜禽肠道健康的作用机制研究进展

doi:10.3864/j.issn.0578-1752.2026.10.014

Abstract

Abstract:

Since the implementation of the "antibiotic ban order" for feed in China in 2020, the livestock and poultry breeding industry has faced numerous challenges, including impaired animal growth and development, reduced feed conversion efficiency, and decreased disease resistance. Among these, the intestinal tract, as the core organ for nutrient absorption and immune defense in the body, has increasingly prominent health issues, manifested as damaged intestinal barriers, frequent inflammatory responses, and imbalances in microbial communities. The health of the intestinal tract is crucial for overall production performance, and the intestinal mucosal barrier, as the first line of defense against pathogens and toxins, maintains homeostasis through multiple mechanisms, such as mucus layer, tight junctions, immune regulation, and microbial interactions. In this process, protein O-glycosylation modification plays a key role, as it determines the structural and functional diversity of mucin proteins and directly affects barrier integrity. In recent years, with the rapid development of glycomics technology, the complex structure of glycosylation modifications can be more accurately analyzed, laying the foundation for its application in nutritional intervention and disease prevention. This article systematically summarized the main types of protein glycosylation modifications and their structural characteristics, and focused on the regional distribution differences and functional characteristics of mucin O-glycosylation modifications in the intestinal mucus layer. The article thoroughly analyzed the mechanisms of action of three important O-glycosylation subtypes (sialylation, sulfation, and fucosylation) in the intestinal mucosal barrier: Sialylation enhanced the negative charge of the mucus layer, inhibited pathogen adhesion, and regulated the function of immunoglobulins; Sulfation modification improved the stability and anti-degradation ability of the mucus layer and affected microbial recognition and colonization; Fucosylation provided carbon sources for symbiotic bacteria and activates immune axes (such as AHR/IL-22) to participate in host defense. In addition, this article systematically reviewed the latest research progress of O-glycosylation in regulating the immune response and microbial interactions in livestock and poultry, such as in models of necrotic enteritis and Salmonella infection, O-glycosylation abnormalities could lead to impaired intestinal barrier function, and supplementing specific monosaccharides (mannose, and fucosamine) could alleviate inflammation by repairing the glycan chain structure. Although significant progress has been made in related research, the precise analysis of the glycosylation modification structure and the targeted regulation of key glycosyltransferases (Fut2, St3gal, etc.) through nutritional strategies still face challenges. In the future, it is necessary to further integrate multi-omics technologies, artificial intelligence models, and synthetic biology approaches to deeply reveal the molecular mechanism of glycosylation modification in the occurrence and development of intestinal diseases in livestock and poultry, providing new ideas for the precise prevention and control of issues, such as diarrhea after antibiotic ban, and ultimately helping to improve the intestinal health level and breeding efficiency of livestock.

Key words: protein glycosylation, intestinal barrier, O-glycosylation, gut microbiota, immune response

WANG YuXuan, GU Jiong, XIA Bing. Research Progress on the Mechanism of Protein Glycosylation Modification in Regulating Intestinal Health of Livestock and Poultry[J].Scientia Agricultura Sinica, 2026, 59(10): 2265-2275.

Figures/Tables 1

Table 1

The function and interaction of the core FUT gene"

基因 Gene	催化修饰类型 Catalytic modification type	关键功能 Key function	菌群调控作用 The regulatory role of microbiota	疾病关联与协同机制 Disease association and synergistic mechanisms
FUT2	催化α1,2-岩藻糖基化 Catalyze α1,2- fucosylation	合成黏蛋白岩藻糖基化层，为共生菌提供碳源；激活AHR/IL-22免疫轴^[43-44] Synthesize the mucin fucosylation layer to provide a carbon source for the symbiotic bacteria; activate the AHR/IL-22 immune axis ^[43-44]	维持双歧杆菌丰度；抑制变形菌门；促进Ruminococcus gnavus定植^[44-45] Maintain the abundance of bifidobacteria; inhibit the Proteobacteria phylum; promote the colonization of Ruminococcus gnavus^[44-45]	CD易感性↑：缺失导致菌群紊乱→LPC代谢物累积→破坏屏障^[46]；与FUT8协同维持黏液层厚度^[47] CD susceptibility ↑: Deficiency leads to imbalance of the microbiota → Accumulation of LPC metabolites → Destruction of the barrier ^[46]; Cooperates with FUT8 to maintain the thickness of the mucus layer^[47]
FUT3	α1,3/4-岩藻糖基化 α1,3/4-fucosylation	合成Lewis抗原，介导菌群黏附与免疫识别^[48] Synthesize Lewis antigens to mediate bacterial adhesion and immune recognition ^[48]	维持拟杆菌门丰度；抑制变形菌门丰度^[49] Maintain the abundance of Bacteroidetes; inhibit the abundance of Proteobacteria^[49]	与FUT2共调Th17/Treg平衡^[26] Regulates the Th17/Treg balance together with FUT2^[26]
FUT8	催化核心岩藻糖基化 Catalytic core fucosylation	调控黏蛋白分泌^[47] Regulation of mucin secretion^[47]	促进阿克曼菌丰度；抑制致病菌黏附^[49-50] Promote the abundance of Acman bacteria; inhibit the adhesion of pathogenic bacteria^[49-50]	过表达致黏液增厚，促进细菌入侵^[47]；与FUT2共同调节线粒体功能^[51] Overexpression leads to increased mucus production and promotes bacterial invasion^[47]; it also jointly regulates mitochondrial function with FUT2^[51]

Table 1

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Research Progress on the Mechanism of Protein Glycosylation Modification in Regulating Intestinal Health of Livestock and Poultry

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