Heterologous expression, purification and characterization of Lactobacillus acidophilus CICC6074-derived slpX protein and the molecular mechanism of its anti-inflammatory effect on LPS-induced RAW264.7 cells

The role of S-layer proteins (SLP), which form the outermost layer of cell walls in lactic acid bacteria (LAB), plays a crucial role in regulating immune-stimulating activity, thereby closely influencing LAB’s ability to boost host immunity. In this study, the heterologous expression, purification,...

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Main Authors: Yingying Cao, Xiankang Fan, Zihang Shi, Mingzhen Liu, Jue Xu, Tao Zhang, Xiaoqun Zeng, Zhen Wu, Daodong Pan
Format: Article
Language:English
Published: Tsinghua University Press 2025-05-01
Series:Food Science and Human Wellness
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Online Access:https://www.sciopen.com/article/10.26599/FSHW.2024.9250230
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author Yingying Cao
Xiankang Fan
Zihang Shi
Mingzhen Liu
Jue Xu
Tao Zhang
Xiaoqun Zeng
Zhen Wu
Daodong Pan
author_facet Yingying Cao
Xiankang Fan
Zihang Shi
Mingzhen Liu
Jue Xu
Tao Zhang
Xiaoqun Zeng
Zhen Wu
Daodong Pan
author_sort Yingying Cao
collection DOAJ
description The role of S-layer proteins (SLP), which form the outermost layer of cell walls in lactic acid bacteria (LAB), plays a crucial role in regulating immune-stimulating activity, thereby closely influencing LAB’s ability to boost host immunity. In this study, the heterologous expression, purification, and characterization of Lactobacillus acidophilus CICC6074-derived slpX protein and the molecular mechanism of its anti-inflammatory effect on LPS-induced RAW264.7 cells were investigated. Initially, the PCR results were shown to successfully clone the slpX DNA sequence by homologous recombination to obtain the pet-32a-slpX recombinant plasmid. SDS-PAGE results revealed that slpX protein with a molecular weight of 54 kDa was successfully obtained under 0.7 mmol/L IPTG-induced conditions, which was further demonstrated by Western blot (WB) and LC-MS/MS. ELISA, WB and molecular docking results indicated that slpX protein can inhibit LPS-induced cellular inflammatory responses by linking to TLR4 and MD2 via hydrogen bonding and increasing the levels of anti-inflammatory factor IL-10 and decreasing the levels of inflammatory factors (TNF-α, IL-6, NO) and ROS via MAPK and NF-κB signaling pathways. The study is essential for the preparation of pure slpX protein and revealing its anti-inflammatory molecular mechanism.
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spelling doaj-art-ab5fda1a2daa496d9616afc3582f74322025-08-20T03:12:14ZengTsinghua University PressFood Science and Human Wellness2097-07652213-45302025-05-01145925023010.26599/FSHW.2024.9250230Heterologous expression, purification and characterization of Lactobacillus acidophilus CICC6074-derived slpX protein and the molecular mechanism of its anti-inflammatory effect on LPS-induced RAW264.7 cellsYingying Cao0Xiankang Fan1Zihang Shi2Mingzhen Liu3Jue Xu4Tao Zhang5Xiaoqun Zeng6Zhen Wu7Daodong Pan8State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo 315211, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo 315211, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo 315211, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo 315211, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo 315211, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo 315211, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo 315211, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo 315211, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo 315211, ChinaThe role of S-layer proteins (SLP), which form the outermost layer of cell walls in lactic acid bacteria (LAB), plays a crucial role in regulating immune-stimulating activity, thereby closely influencing LAB’s ability to boost host immunity. In this study, the heterologous expression, purification, and characterization of Lactobacillus acidophilus CICC6074-derived slpX protein and the molecular mechanism of its anti-inflammatory effect on LPS-induced RAW264.7 cells were investigated. Initially, the PCR results were shown to successfully clone the slpX DNA sequence by homologous recombination to obtain the pet-32a-slpX recombinant plasmid. SDS-PAGE results revealed that slpX protein with a molecular weight of 54 kDa was successfully obtained under 0.7 mmol/L IPTG-induced conditions, which was further demonstrated by Western blot (WB) and LC-MS/MS. ELISA, WB and molecular docking results indicated that slpX protein can inhibit LPS-induced cellular inflammatory responses by linking to TLR4 and MD2 via hydrogen bonding and increasing the levels of anti-inflammatory factor IL-10 and decreasing the levels of inflammatory factors (TNF-α, IL-6, NO) and ROS via MAPK and NF-κB signaling pathways. The study is essential for the preparation of pure slpX protein and revealing its anti-inflammatory molecular mechanism.https://www.sciopen.com/article/10.26599/FSHW.2024.9250230lactic acid bacterias-layer proteininflammationliquid chromatography-tandem mass spectrometryenzyme-linked immunosorbnent assaymolecular docking
spellingShingle Yingying Cao
Xiankang Fan
Zihang Shi
Mingzhen Liu
Jue Xu
Tao Zhang
Xiaoqun Zeng
Zhen Wu
Daodong Pan
Heterologous expression, purification and characterization of Lactobacillus acidophilus CICC6074-derived slpX protein and the molecular mechanism of its anti-inflammatory effect on LPS-induced RAW264.7 cells
Food Science and Human Wellness
lactic acid bacteria
s-layer protein
inflammation
liquid chromatography-tandem mass spectrometry
enzyme-linked immunosorbnent assay
molecular docking
title Heterologous expression, purification and characterization of Lactobacillus acidophilus CICC6074-derived slpX protein and the molecular mechanism of its anti-inflammatory effect on LPS-induced RAW264.7 cells
title_full Heterologous expression, purification and characterization of Lactobacillus acidophilus CICC6074-derived slpX protein and the molecular mechanism of its anti-inflammatory effect on LPS-induced RAW264.7 cells
title_fullStr Heterologous expression, purification and characterization of Lactobacillus acidophilus CICC6074-derived slpX protein and the molecular mechanism of its anti-inflammatory effect on LPS-induced RAW264.7 cells
title_full_unstemmed Heterologous expression, purification and characterization of Lactobacillus acidophilus CICC6074-derived slpX protein and the molecular mechanism of its anti-inflammatory effect on LPS-induced RAW264.7 cells
title_short Heterologous expression, purification and characterization of Lactobacillus acidophilus CICC6074-derived slpX protein and the molecular mechanism of its anti-inflammatory effect on LPS-induced RAW264.7 cells
title_sort heterologous expression purification and characterization of lactobacillus acidophilus cicc6074 derived slpx protein and the molecular mechanism of its anti inflammatory effect on lps induced raw264 7 cells
topic lactic acid bacteria
s-layer protein
inflammation
liquid chromatography-tandem mass spectrometry
enzyme-linked immunosorbnent assay
molecular docking
url https://www.sciopen.com/article/10.26599/FSHW.2024.9250230
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