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. 2025 Aug 1;14(15):2708.
doi: 10.3390/foods14152708.

Hylocereus polyrhizus Pulp Residues Polysaccharide Alleviates High-Fat Diet-Induced Obesity by Modulating Intestinal Mucus Secretion and Glycosylation

Guanghui Li  1   2   3   4   5 , Kit-Leong Cheong  1   2   3   4   5 , Yunhua He  1   2   3   4   5   6 , Ahluk Liew  6 , Jiaxuan Huang  1   2   3   4   5 , Chen Huang  7 , Saiyi Zhong  1   2   3   4   5 , Malairaj Sathuvan  8
Affiliations

Hylocereus polyrhizus Pulp Residues Polysaccharide Alleviates High-Fat Diet-Induced Obesity by Modulating Intestinal Mucus Secretion and Glycosylation

Guanghui Li et al. Foods. .

Abstract

Although Hylocereus polyrhizus pulp residues polysaccharides (HPPP) have shown potential in improving metabolic disorders and intestinal barrier function, the mechanism by which they exert their effects through regulating O-glycosylation modifications in the mucus layer remains unclear. Therefore, this study established a HFD-induced obese colitis mouse model (n = 5 per group) and combined nano-capillary liquid chromatography-tandem mass spectrometry (nanoLC-MS/MS) technology to quantitatively analyze the dynamic changes in O-glycosylation. Additionally, through quantitative O-glycosylation proteomics and whole-proteome analysis, we identified 155 specifically altered O-glycosylation sites in colon tissue, with the glycosylation modification level of the MUC2 core protein increased by approximately 2.1-fold. The results indicate that HPPP alleviates colonic mucosal damage by regulating interactions between mucus O-glycosylation. Overall, we demonstrated that HPPP increases HFD-induced O-glycosylation sites, improves intestinal mucosal structure in obese mice, and provides protective effects against obesity-induced intestinal mucosal damage.

Keywords: Hylocereus polyrhizus pulp residues polysaccharide; Metabolic syndrome; O-glycopeptide; antioxidant activity; site-specific o-glycoproteomics.

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Conflict of interest statement

Author Ahluk Liew and Yunhua He were employed by the company (Guangdong Meichen Biotechnology Co., Ltd.). The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Physicochemical properties of HPPP. (A) X-diffraction pattern of HPPP; (B) Thermogravimetric analysis of HPPP; (C) Viscosity of HPPP solutions as a function of shear rate; (D) DPPH radical scavenging activity; (E) ABTS radical scavenging activity.
Figure 2
Figure 2
HPPP modulates colonic O-glycosylation. Overall qualitative (left pie) and quantitative results (right pie) of O-glycopeptides from TMT-labeled RPLC-MS/MS analyses of (A) stacked Venn diagrams of the qualitative and HFD vs. NC quantitative results for sample NC; (B) stacked Venn diagrams of the qualitative and HFD vs. HFD-PC quantitative results for sample HFD-PC; and (C) stacked Venn diagrams of the qualitative and HFD vs. HFD-HPPP quantitative results for sample HFD-HPPP quantitative results stacked Venn diagrams. (D) Volcano plot of differentially expressed proteins in the HFD vs. NC sample group; (E) Volcano plot of differentially expressed proteins in the HFD vs. HFD-PC sample group; (F) Volcano plot of differentially expressed proteins in the HFD vs. HFD-HPPP sample group.
Figure 3
Figure 3
HPPP remodeling glycoprotein structural domains in obese mice. (A) Analysis of differentially expressed glycoprotein structural domains in the HFD vs. NC sample group; (B) Analysis of differentially expressed glycoprotein structural domains in the HFD vs. HFD-PC sample group; (C) Analysis of differentially expressed glycoprotein structural domains in the HFD vs. HFD-HPPP sample group.
Figure 4
Figure 4
HPPP drives glycoprotein functional remodeling for efficient intestinal mucosal barrier defense. (A) Differential expression of glycoprotein GO annotation diagram for HFD vs. NC sample group; (B) Differential expression of glycoprotein GO annotation diagram for HFD vs. HFD-PC sample group; (C) Differential expression of glycoprotein GO annotation diagram for HFD vs. HFD-HPPP sample group.
Figure 5
Figure 5
Radical repair of metabolic pathways by HPPP intervention. (A) Differential expression of glycoprotein KEGG metabolic pathway analysis in the HFD vs. NC sample group; (B) Differential expression of glycoprotein KEGG metabolic pathway analysis in the HFD vs. HFD-PC sample group; (C) Differential expression of glycoprotein KEGG metabolic pathway analysis in the HFD vs. HFD-HPPP sample group. (D) Heatmap of O-glycosidases found in the colon of mice in each group; (E) Differential expression of glycoprotein PPI interactions network in the HFD vs. NC sample group; (F) Differential expression of glycoprotein PPI interactions network in the HFD vs. HFD-PC sample group; (G) Differential expression of glycoprotein PPI interactions network in the HFD vs. HFD-HPPP sample group.
Figure 6
Figure 6
Structure dependence of high-fat diet-induced inhibition of O-glycosylation. (A) HFD vs. NC down-regulation of intact O-glycopeptide EFHHGPDPTDTAPGEQDQDVASSPPESS mass spectral dissociation plots; (B) HFD vs. HFD-PC down-regulation of intact O-glycopeptide FJGSVSFFR mass spectral dissociation plots; (C) HFD vs. HFD-HPPP down-regulation of intact O-glycopeptide PTPRFPQAPEPAEPTDLPPPLPPGPPSVFPDCPR mass spectrometry dissociation plot.
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