Article(id=1277254206079766846, tenantId=1146029695717560320, journalId=1235980609244409860, issueId=1277254112370623080, articleNumber=null, orderNo=null, doi=10.3969/j.issn.1000-2561.2026.02.008, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=null, receivedDate=1758384000000, receivedDateStr=2025-09-21, revisedDate=null, revisedDateStr=null, acceptedDate=1762185600000, acceptedDateStr=2025-11-04, onlineDate=1782450732965, onlineDateStr=2026-06-26, pubDate=1771948800000, pubDateStr=2026-02-25, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1782450732965, onlineIssueDateStr=2026-06-26, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1782450732965, creator=13701087609, updateTime=1782450732965, updator=13701087609, issue=Issue{id=1277254112370623080, tenantId=1146029695717560320, journalId=1235980609244409860, year='2026', volume='47', issue='2', pageStart='281', pageEnd='551', issueExtLink='null', onlineDate='null', pubDate='1771948800000', pubDateStr='2026-02-25', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=1, issueType=-1, specialIssue=null, createTime=1782450710622, creator='13701087609', updateTime=1782451594955, updator='13701087609', preIssue=null, nextIssue=null, articleTotal=null, ext={EN=IssueExt(id=1277257821632729830, tenantId=1146029695717560320, journalId=1235980609244409860, issueId=1277254112370623080, language=EN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=), CN=IssueExt(id=1277257821632729831, tenantId=1146029695717560320, journalId=1235980609244409860, issueId=1277254112370623080, language=CN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=)}, issueFiles=null, downloadFileDto=null}, startPage=364, endPage=371, ext={EN=ArticleExt(id=1277254206897656128, articleId=1277254206079766846, tenantId=1146029695717560320, journalId=1235980609244409860, language=EN, title=Prokaryotic Induction of Recombinant Flg22 Protein and Functional Comparative Analysis with flg22 Peptide, columnId=1236256430337085821, journalTitle=Chinese Journal of Tropical Crops, columnName=Omics & Biotechnology, runingTitle=null, highlight=null, articleAbstract=

Flg22 is an artificially synthesized 22-amino-acid peptide derived from the conserved N-terminal region of bacterial flagellin, playing a crucial role in regulating plant immune responses. Due to the high cost of artificially synthesized flg22 short peptides and limitations for large-scale application, this study aimed to determine the suitable conditions for prokaryotic induction expression of the flg22 protein and to verify its function, thereby determining whether it could replace the commercially used flg22 short peptides. In this study, the pET32a-flg22 prokaryotic expression vector was synthesized, and we then compared protein expression efficiency under induction at 28 ℃ and 37 ℃. Additionally, we detected the dynamic burst of reactive oxygen species (ROS) in cassava treated with flg22 peptides and flg22 proteins at different concentrations to validate the functions. The results indicated that 28 ℃ was the optimal induction temperature for inducing flg22 protein expression. ROS measurements showed that within a specific concentration range, the peak intensity of ROS increased with the increase in flg22 protein concentration. Furthermore, after spraying cassava leaves with 60 μg/mL and 600 μg/mL of flg22 recombinant proteins, as well as 2.27 μg/mL of flg22 peptides, for three days, we inoculated plants with the pathogen Xam (Xanthomonas axonopodis pv. manihotis, Xam). Compared to treatment with sterile water, both flg22 protein and flg22 peptide treatments showed significant antibacterial effects against Xam in cassava plants, with the 60 μg/mL and 600 μg/mL flg22 protein treatments showing notably stronger antibacterial activity than the flg22 peptide. The results preliminarily identified the prokaryotic expression conditions of flg22 recombinant protein and verified that its function in inducing plant defense responses is consistent with that of the peptide, providing a theoretical basis for substituting commercial peptides with flg22 recombinant protein.

, authors=null, authorsList=Mengyuan WANG, Ke CHENG, Lan YANG, Huiping ZHAO, authorCompany=null, correspAuthors=Huiping ZHAO, authorNote=null, correspAuthorsNote=null, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=null, magXml=null, pdfUrl=null, pdf=null, pdfFileSize=null, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=null, mapNumber=null, fund=null), CN=ArticleExt(id=1277254207707156802, articleId=1277254206079766846, tenantId=1146029695717560320, journalId=1235980609244409860, language=CN, title=Flg22重组蛋白的原核诱导及与flg22短肽的功能比较, columnId=1236256430517440904, journalTitle=热带作物学报, columnName=组学与生物技术, runingTitle=null, highlight=null, articleAbstract=

Flg22是细菌鞭毛蛋白(flagellin)N端保守的22个氨基酸合成肽段,在调节植物免疫应答调节中发挥重要作用,也常被用于免疫细胞功能研究。由于人工合成的flg22短肽成本较高,其规模化应用受限。因此,本研究拟探究flg22蛋白原核诱导表达的适宜条件并验证其功能,评估其替代商用flg22短肽的可行性。本研究通过合成pET32a-flg22原核表达载体,比较28 ℃与37 ℃诱导温度下的蛋白表达效率,并分别检测经flg22短肽及不同浓度flg22蛋白处理的木薯中活性氧(reactive oxygen species, ROS)的爆发动态,验证其功能。结果显示:28 ℃为flg22蛋白诱导的最佳温度;ROS测定结果表明,在一定浓度范围内,ROS峰值强度随flg22蛋白浓度增加呈递增趋势。进一步将60、600 μg/mL的flg22重组蛋白及2.27 μg/mL flg22短肽分别外源喷施于木薯叶片,3 d后,接种木薯萎焉致病变种XamXanthomonas axonopodis pv. Manihotis, Xam)病原菌,与无菌水处理相比,经flg22蛋白或flg22短肽处理的木薯植株均表现出对Xam的显著抑菌效果,且60、600 μg/mL flg22蛋白的抑菌效果均显著优于flg22短肽。本研究初步筛选出flg22重组蛋白的原核表达条件,并验证其在诱导植物防御响应的功能与短肽具有一致性,为以flg22重组蛋白替代商用短肽提供初步的理论依据。

, authors=

王萌媛(1999—),女,硕士研究生,研究方向:作物遗传育种。

, authorsList=王萌媛, 程科, 杨澜, 赵惠萍, authorCompany=null, correspAuthors=赵惠萍, authorNote=null, correspAuthorsNote=
* 赵惠萍(ZHAO Huiping),E-mail:
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王萌媛(1999—),女,硕士研究生,研究方向:作物遗传育种。

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王萌媛(1999—),女,硕士研究生,研究方向:作物遗传育种。

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Flg22重组蛋白的原核诱导及与flg22短肽的功能比较
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王萌媛 1, 2 , 程科 1, 2 , 杨澜 1, 2, 3 , 赵惠萍 1, 2, *, *
热带作物学报 | 组学与生物技术 2026,47(2): 364-371
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热带作物学报 |组学与生物技术 2026 , 47 (2) : 364 -371
Flg22重组蛋白的原核诱导及与flg22短肽的功能比较
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王萌媛(1999—),女,硕士研究生,研究方向:作物遗传育种。

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2.海南大学三亚南繁研究院,海南三亚 572025
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王萌媛1, 2, 程科1, 2, 杨澜1, 2, 3, 赵惠萍1, 2, *, *
作者信息
  • 1.海南大学热带农林学院/海南省耐盐作物生物技术重点实验室,海南海口 570228
  • 2.海南大学三亚南繁研究院,海南三亚 572025
  • 3.贵州省园艺研究所/贵州省园艺工程技术研究中心,贵州贵阳 550025
通讯作者:
* 赵惠萍(ZHAO Huiping),E-mail:
Prokaryotic Induction of Recombinant Flg22 Protein and Functional Comparative Analysis with flg22 Peptide
Mengyuan WANG1, 2, Ke CHENG1, 2, Lan YANG1, 2, 3, Huiping ZHAO1, 2
Affiliations
  • 1.School of Tropical Agriculture and Forestry, Hainan University/Key Laboratory of Biotechnology of Salt Tolerant Crops of Hainan Province, Haikou, Hainan 570228, China
  • 2.Sanya Institute of Breeding and Multiplication, Hainan University, Sanya, Hainan 572025, China
  • 3.Guizhou Horicultural Institute/Guizhou Research Center of Horicultural Engineering Technology, Guiyang, Guizhou 550025, China
出版时间: 2026-02-25 doi: 10.3969/j.issn.1000-2561.2026.02.008
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Flg22是细菌鞭毛蛋白(flagellin)N端保守的22个氨基酸合成肽段,在调节植物免疫应答调节中发挥重要作用,也常被用于免疫细胞功能研究。由于人工合成的flg22短肽成本较高,其规模化应用受限。因此,本研究拟探究flg22蛋白原核诱导表达的适宜条件并验证其功能,评估其替代商用flg22短肽的可行性。本研究通过合成pET32a-flg22原核表达载体,比较28 ℃与37 ℃诱导温度下的蛋白表达效率,并分别检测经flg22短肽及不同浓度flg22蛋白处理的木薯中活性氧(reactive oxygen species, ROS)的爆发动态,验证其功能。结果显示:28 ℃为flg22蛋白诱导的最佳温度;ROS测定结果表明,在一定浓度范围内,ROS峰值强度随flg22蛋白浓度增加呈递增趋势。进一步将60、600 μg/mL的flg22重组蛋白及2.27 μg/mL flg22短肽分别外源喷施于木薯叶片,3 d后,接种木薯萎焉致病变种XamXanthomonas axonopodis pv. Manihotis, Xam)病原菌,与无菌水处理相比,经flg22蛋白或flg22短肽处理的木薯植株均表现出对Xam的显著抑菌效果,且60、600 μg/mL flg22蛋白的抑菌效果均显著优于flg22短肽。本研究初步筛选出flg22重组蛋白的原核表达条件,并验证其在诱导植物防御响应的功能与短肽具有一致性,为以flg22重组蛋白替代商用短肽提供初步的理论依据。

原核诱导表达  /  flg22  /  短肽  /  病原菌  /  ROS

Flg22 is an artificially synthesized 22-amino-acid peptide derived from the conserved N-terminal region of bacterial flagellin, playing a crucial role in regulating plant immune responses. Due to the high cost of artificially synthesized flg22 short peptides and limitations for large-scale application, this study aimed to determine the suitable conditions for prokaryotic induction expression of the flg22 protein and to verify its function, thereby determining whether it could replace the commercially used flg22 short peptides. In this study, the pET32a-flg22 prokaryotic expression vector was synthesized, and we then compared protein expression efficiency under induction at 28 ℃ and 37 ℃. Additionally, we detected the dynamic burst of reactive oxygen species (ROS) in cassava treated with flg22 peptides and flg22 proteins at different concentrations to validate the functions. The results indicated that 28 ℃ was the optimal induction temperature for inducing flg22 protein expression. ROS measurements showed that within a specific concentration range, the peak intensity of ROS increased with the increase in flg22 protein concentration. Furthermore, after spraying cassava leaves with 60 μg/mL and 600 μg/mL of flg22 recombinant proteins, as well as 2.27 μg/mL of flg22 peptides, for three days, we inoculated plants with the pathogen Xam (Xanthomonas axonopodis pv. manihotis, Xam). Compared to treatment with sterile water, both flg22 protein and flg22 peptide treatments showed significant antibacterial effects against Xam in cassava plants, with the 60 μg/mL and 600 μg/mL flg22 protein treatments showing notably stronger antibacterial activity than the flg22 peptide. The results preliminarily identified the prokaryotic expression conditions of flg22 recombinant protein and verified that its function in inducing plant defense responses is consistent with that of the peptide, providing a theoretical basis for substituting commercial peptides with flg22 recombinant protein.

prokaryotic induced expression  /  flg22  /  peptide  /  pathogen  /  reactive oxygen species
王萌媛, 程科, 杨澜, 赵惠萍. Flg22重组蛋白的原核诱导及与flg22短肽的功能比较. 热带作物学报, 2026 , 47 (2) : 364 -371 . DOI: 10.3969/j.issn.1000-2561.2026.02.008
Mengyuan WANG, Ke CHENG, Lan YANG, Huiping ZHAO. Prokaryotic Induction of Recombinant Flg22 Protein and Functional Comparative Analysis with flg22 Peptide[J]. Chinese Journal of Tropical Crops, 2026 , 47 (2) : 364 -371 . DOI: 10.3969/j.issn.1000-2561.2026.02.008
  • 海南省教育厅项目(Hnky2024-10)
  • 海南大学南繁学院创新创业训练项目(NFJD2024-15)
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doi: 10.3969/j.issn.1000-2561.2026.02.008
  • 接收时间:2025-09-21
  • 首发时间:2026-06-26
  • 出版时间:2026-02-25
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  • 收稿日期:2025-09-21
  • 录用日期:2025-11-04
基金
海南省教育厅项目(Hnky2024-10)
海南大学南繁学院创新创业训练项目(NFJD2024-15)
作者信息
    1.海南大学热带农林学院/海南省耐盐作物生物技术重点实验室,海南海口 570228
    2.海南大学三亚南繁研究院,海南三亚 572025
    3.贵州省园艺研究所/贵州省园艺工程技术研究中心,贵州贵阳 550025

通讯作者:

* 赵惠萍(ZHAO Huiping),E-mail:
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https://castjournals.cast.org.cn/joweb/rdzwxb/CN/10.3969/j.issn.1000-2561.2026.02.008
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2种不同金属材料的力学参数

Family
属数
Number of
genus
种数
Number of
species
占总种数比例
Percentage of
total species (%)

Genus
种数
Number of
species
占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
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