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学者姓名：聂鑫怡
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Abstract ：
Aspergillus flavus and its secondary metabolites, aflatoxins (AFs), especially aflatoxin B1 (AFB1), seriously affect agricultural production, food storage, and human health. Succinyl-CoA synthase ADP-forming subunit beta (SCS) is involved in the synthesis of succinate from succinyl-CoA in the tricarboxylic acid cycle. In this study, we demonstrated that SCS led to decreased aflatoxin production. Bioassay results showed that deletion of sucB (the gene coding for SCS) led to increased succinyl-CoA accumulation. Catalyzed by succinyl transferase (STA), the increased amount of succinyl-CoA in Delta sucB leads to increased levels of global protein succinylation, which causes upregulation of AFB1 accumulation in Delta sucB. To elucidate the mechanism of increased AFB1 accumulation in Delta sucB, the relevant enzymes and metabolites involved in the aflatoxin biosynthesis pathway were examined through proteome and metabolome analyses. These data illustrate that the deletion of sucB results in an increase in (1'S, 5'S) - averufin catalyzed by AflK, (1'S)-averantin catalyzed by AflD, and aflatoxin G2/O- methylsterigmatocystin catalyzed by AflP. We also found that AflM is not only upregulated but also succinylated in Delta sucB; Ach1 (acetyl-CoA hydrolase, Ach1) is downregulated in Delta sucB and interacts with SCS. Therefore, we deduce a pathway of Ach1/STA-SCS-succinylated AflM for AFB1 biosynthesis, which provides knowledge for the control of A. flavus and AFs.
Keyword ：
aflatoxin B1 aflatoxin B1 Aspergillus flavus Aspergillus flavus development development succinylation level succinylation level succinyl-CoA synthetase succinyl-CoA synthetase
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| GB/T 7714 | Xie, Rui , Zhuang, Zhenhong , Chen, Qionghui et al. STA regulates succinylated AflM triggered by SCS to contribute to aflatoxin biosynthesis through the Ach1 [J]. | VIRULENCE , 2025 , 16 (1) . |
| MLA | Xie, Rui et al. "STA regulates succinylated AflM triggered by SCS to contribute to aflatoxin biosynthesis through the Ach1" . | VIRULENCE 16 . 1 (2025) . |
| APA | Xie, Rui , Zhuang, Zhenhong , Chen, Qionghui , Xie, Chunlan , Adejor, John , Nie, Xinyi et al. STA regulates succinylated AflM triggered by SCS to contribute to aflatoxin biosynthesis through the Ach1 . | VIRULENCE , 2025 , 16 (1) . |
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Pathogenic filamentous fungi pose a significant threat to global food security and human health. The limitations of available antifungal agents, including resistance and toxicity, highlight the need for developing innovative antifungal strategies. Antifungal proteins (AFPs) are a class of secreted small proteins that exhibit potent antifungal activity against filamentous fungi, yet the underlying mechanism remains partially understood. In this study, we investigate the molecular and cellular effects of two AFPs, PgAFP and AfAFP, on Aspergillus flavus, a representative filamentous fungus. These AFPs affect various fungal phenotypes and exert an intracellular effect by interacting with Ntp1, a fungi exclusive protein modulating diverse fungal traits. We find that Ntp1 amino acids 417-588 are critical for AFP binding and play a role in regulating growth, development, sporulation, sclerotia formation, toxin synthesis, and pathogenicity. Results generated from this study will help to control pathogenic fungi.
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| GB/T 7714 | Wang, Yu , Wang, Sen , Chen, Yuanyuan et al. The role of Npt1 in regulating antifungal protein activity in filamentous fungi [J]. | NATURE COMMUNICATIONS , 2025 , 16 (1) . |
| MLA | Wang, Yu et al. "The role of Npt1 in regulating antifungal protein activity in filamentous fungi" . | NATURE COMMUNICATIONS 16 . 1 (2025) . |
| APA | Wang, Yu , Wang, Sen , Chen, Yuanyuan , Xie, Chunlan , Xu, Haibo , Lin, Yunhua et al. The role of Npt1 in regulating antifungal protein activity in filamentous fungi . | NATURE COMMUNICATIONS , 2025 , 16 (1) . |
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Filamentous fungi pose a significant threat to global food security and human well-being due to their potent pathogenicity and the resulting infectious diseases.Limitations associated with current antifungal agents,such as resistance development and toxicity concerns,necessitate the pursuit of innovative antifungal strategies.Antifungal proteins(AFPs) are a class of secreted small proteins exhibiting potent antifungal activity against filamentous fungi.Despite their discovery several decades ago,the precise mechanisms underlying their antifungal effects remain partially elucidated.In this study,we investigated the molecular and cellular consequences of two AFPs,PgAFP and AfAFP,on Aspergillus flavus(A.flavus),a representative filamentous fungus.We found that these two AFPs not only affect various fungal phenotypes,but also exert a novel intracellular effect by interacting with a newly identified protein,Ntp1,which modulates diverse fungal traits.Furthermore,we identified amino acids417-588 within Ntp1 as cruci...
Keyword ：
AFP-interacting proteins AFP-interacting proteins Antifungal Protein Antifungal Protein Aspergillus flavus Aspergillus flavus Filamentous Fungi Filamentous Fungi Ntp1 Ntp1
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| GB/T 7714 | 王宇 , 王森 , 陈媛媛 et al. Insights from the Microorganism-Specific Protein Ntp1 in Regulating Antifungal Protein Activity in Filamentous Fungi [C] //中国菌物学会2024年学术年会 . 2024 . |
| MLA | 王宇 et al. "Insights from the Microorganism-Specific Protein Ntp1 in Regulating Antifungal Protein Activity in Filamentous Fungi" 中国菌物学会2024年学术年会 . (2024) . |
| APA | 王宇 , 王森 , 陈媛媛 , 谢春兰 , 林云华 , 林染荀 et al. Insights from the Microorganism-Specific Protein Ntp1 in Regulating Antifungal Protein Activity in Filamentous Fungi 中国菌物学会2024年学术年会 . (2024) . |
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SUMO adducts occur in Aspergillus flavus, and are implicated in fungal biology, while the underlying mechanism and the SUMOylation apparatus components in this saprophytic food spoilage mould, remain undefined. Herein, genes encoding SUMOylation cascade enzymes in A. flavus, including two heterodimeric SUMO E1 activating enzymes, a unique SUMO E2 conjugating enzyme, and one of SUMO E3 ligases, were identified and functionally analyzed. Global SUMO adducts immunoassay, multiple morphological comparison, aflatoxin attributes test, fungal infection and transcriptomic analyses collectively revealed that: E1 and E2 were essential for intracellular SUMOylation, and contributed to both stress response and fungal virulence-related events, including sporulation, colonization, aflatoxins biosynthesis; the primary E3 in this fungus, AfSizA, might serve as the molecular linkage of SUMOylation pathway to fungal virulence rather than SUMOylation-mediated stress adaptation. These findings demonstrated that SUMOylation machinery in A. flavus was functionally intact and contributed to multiple pathobiological processes, hence offering ideas and targets to control food contamination by this mycotoxigenic fungus.
Keyword ：
Aspergillus flavus Aspergillus flavus E1 activating enzyme E1 activating enzyme E2 conjugating enzyme E2 conjugating enzyme E3 ligase E3 ligase Food contamination Food contamination SUMOylation SUMOylation
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| GB/T 7714 | Nie, Xin-Yi , Xue, Yang , Li, Ling et al. A functional intact SUMOylation machinery in Aspergillus flavus contributes to fungal and aflatoxin contamination of food [J]. | INTERNATIONAL JOURNAL OF FOOD MICROBIOLOGY , 2023 , 398 . |
| MLA | Nie, Xin-Yi et al. "A functional intact SUMOylation machinery in Aspergillus flavus contributes to fungal and aflatoxin contamination of food" . | INTERNATIONAL JOURNAL OF FOOD MICROBIOLOGY 398 (2023) . |
| APA | Nie, Xin-Yi , Xue, Yang , Li, Ling , Jiang, Zhixin , Qin, Bei , Wang, Yu et al. A functional intact SUMOylation machinery in Aspergillus flavus contributes to fungal and aflatoxin contamination of food . | INTERNATIONAL JOURNAL OF FOOD MICROBIOLOGY , 2023 , 398 . |
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Candida albicans ( C. albicans) is an opportunistic pathogen in humans and possesses a white-opaque heritable switching system. Wor1 is a master regulator of white-opaque switching and is essential for opaque cell formation in C. albicans. However, the regulatory network of Wor1 in white-opaque switching is still vague. In this study, we obtain a series of Wor1-interacting proteins using LexA-Wor1 as bait. Among these proteins, function unknown now 30 (Fun30) interacts with Wor1 in vitro and in vivo. Fun30 expression is upregulated in opaque cells at the transcriptional and protein levels. Loss of FUN30 attenuates white-to-opaque switching, while ectopic expression of FUN30 significantly increases white-to-opaque switching in an ATPase activity-dependent manner. Furthermore, FUN30 upregulation is dependent on CO2; loss of FLO8, a key CO2-sensing transcriptional regulator, abolishes FUN30 upregulation. Interestingly, deletion of FUN30 affects the WOR1 expression regulation feedback loop. Thus, our results indicate that the chromatin remodeller Fun30 interacts with Wor1 and is required for WOR1 expression and opaque cell formation.
Keyword ：
Candida albicans Candida albicans chromatin remodeller chromatin remodeller Fun30 Fun30 white-opaque switching white-opaque switching Wor1 Wor1
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| GB/T 7714 | Gao, Ning , Dai, Baodi , Nie, Xinyi et al. Fun30 nucleosome remodeller regulates white-to-opaque switching in Candida albicans [J]. | ACTA BIOCHIMICA ET BIOPHYSICA SINICA , 2023 , 55 (3) : 508-517 . |
| MLA | Gao, Ning et al. "Fun30 nucleosome remodeller regulates white-to-opaque switching in Candida albicans" . | ACTA BIOCHIMICA ET BIOPHYSICA SINICA 55 . 3 (2023) : 508-517 . |
| APA | Gao, Ning , Dai, Baodi , Nie, Xinyi , Zhao, Qun , Zhu, Wencheng , Chen, Jiangye . Fun30 nucleosome remodeller regulates white-to-opaque switching in Candida albicans . | ACTA BIOCHIMICA ET BIOPHYSICA SINICA , 2023 , 55 (3) , 508-517 . |
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Aflatoxins are a series of highly toxic and carcinogenic secondary metabolites that are synthesized by Aspergillus species. The degradation of aflatoxin enzymes is an important regulatory mechanism which modulates mycotoxin producing. The retromer complex is responsible for the retrograde transport of specific biomolecules and the vacuolar fusion in the intracellular transport. Late endosomal-associated GTPase (Rab7) has been shown to be a downstream effector protein of the retromer complex. A deficiency in the retromer complex or Rab7 results in several cellular trafficking problems in yeast and humans, like protein abnormal accumulation. However, whether retromer dysfunction is involved in aflatoxin synthesis remains unclear. Here, we report that the core retromer complex, which comprises three vacuolar protein sortingassociated proteins (AflVps26-AflVps29-AflVps35), is essential for the development of dormant and resistant fungal forms such as conidia (asexual reproductive spore) and sclerotia (hardened fungal mycelium), as well as aflatoxin production and pathogenicity, in Aspergillus flavus. In particular, we show the AflVps26-AflVps29-AflVps35 complex is negatively correlated with aflatoxin exportation. Structural simulation, sitespecific mutagenesis, and coimmunoprecipitation experiments showed that interactions among AflVps26, AflVps29, and AflVps35 played crucial roles in the retromer complex executing its core functions. We further found an intrinsic connection between AflRab7 and the retromer involved in vesicle-vacuole fusion, which in turn affected the accumulation of aflatoxin synthesis-associated enzymes, suggesting that they work together to regulate the production of toxins. Overall, our understanding of the regulatory role of the core retromer complex in aflatoxin metabolism.
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| GB/T 7714 | Wang, Sen , Wang, Yu , Liu, Yinghang et al. The regulatory role of the Aspergillus flavus core retromer complex in aflatoxin metabolism [J]. | JOURNAL OF BIOLOGICAL CHEMISTRY , 2022 , 298 (7) . |
| MLA | Wang, Sen et al. "The regulatory role of the Aspergillus flavus core retromer complex in aflatoxin metabolism" . | JOURNAL OF BIOLOGICAL CHEMISTRY 298 . 7 (2022) . |
| APA | Wang, Sen , Wang, Yu , Liu, Yinghang , Liu, Lin , Li, Jinyu , Yang, Kunlong et al. The regulatory role of the Aspergillus flavus core retromer complex in aflatoxin metabolism . | JOURNAL OF BIOLOGICAL CHEMISTRY , 2022 , 298 (7) . |
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As an opportunistic pathogen, A. flavus causes crop loss due to fungal growth and mycotoxin contamination. Investigating the role of virulence factors during infection and searching for novel drug targets have been popular scientific topics in the field of fungal control. Nmt has become a potential target in some organisms. The filamentous fungus Aspergillus flavus causes devastating diseases not only to cash crops but also to humans by secreting a series of secondary metabolites called aflatoxins. In the cotranslational or posttranslational process, N-myristoyltransferase (Nmt) is a crucial enzyme that catalyzes the myristate group from myristoyl-coenzyme A (myristoyl-CoA) to the N terminus or internal glycine residue of a protein by forming a covalent bond. Members of the Nmt family execute a diverse range of biological functions across a broad range of fungi. However, the underlying mechanism of AflNmt action in the A. flavus life cycle is unclear, particularly during the growth, development, and secondary metabolic synthesis stages. In the present study, AlfNmt was found to be essential for the development of spore and sclerotia, based on the regulation of the xylose-inducible promoter. AflNmt, located in the cytoplasm of A. flavus, is also involved in modulating aflatoxin (AFB1) in A. flavus, which has not previously been reported in Aspergillus spp. In addition, we purified, characterized, and crystallized the recombinant AflNmt protein (rAflNmt) from the Escherichia coli expression system. Interestingly, the crystal structure of rAlfNmt is moderately different from the models predicted by AlphaFold2 in the N-terminal region, indicating the limitations of machine-learning prediction. In conclusion, these results provide a molecular basis for the functional role of AflNmt in A. flavus and structural insights concerning protein prediction.IMPORTANCE As an opportunistic pathogen, A. flavus causes crop loss due to fungal growth and mycotoxin contamination. Investigating the role of virulence factors during infection and searching for novel drug targets have been popular scientific topics in the field of fungal control. Nmt has become a potential target in some organisms. However, whether Nmt is involved in the developmental stages of A. flavus and aflatoxin synthesis, and whether AlfNmt is an ideal target for structure-based drug design, remains unclear. This study systematically explored and identified the role of AlfNmt in the development of spore and sclerotia, especially in aflatoxin biosynthesis. Moreover, although there is not much difference between the AflNmt model predicted using the AlphaFold2 technique and the structure determined using the X-ray method, current AI prediction models may not be suitable for structure-based drug development. There is still room for further improvements in protein prediction.
Keyword ：
aflatoxin aflatoxin AlphaFold2 AlphaFold2 Aspergillus flavus Aspergillus flavus crystal structure crystal structure N-myristoyltransferase N-myristoyltransferase protein prediction protein prediction sclerotia sclerotia spore spore
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| GB/T 7714 | Wang, Yu , Lin, Ranxun , Liu, Mengxin et al. N-Myristoyltransferase, a Potential Antifungal Candidate Drug-Target for Aspergillus flavus [J]. | MICROBIOLOGY SPECTRUM , 2022 , 11 (1) . |
| MLA | Wang, Yu et al. "N-Myristoyltransferase, a Potential Antifungal Candidate Drug-Target for Aspergillus flavus" . | MICROBIOLOGY SPECTRUM 11 . 1 (2022) . |
| APA | Wang, Yu , Lin, Ranxun , Liu, Mengxin , Wang, Sen , Chen, Hongyu , Zeng, Wanlin et al. N-Myristoyltransferase, a Potential Antifungal Candidate Drug-Target for Aspergillus flavus . | MICROBIOLOGY SPECTRUM , 2022 , 11 (1) . |
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为解决黄曲霉遗传转化操作过程中遗传筛选标记受限及传统URA3/pyrG环出系统存在重复序列残留的问题,以具有尿嘧啶营养缺陷的黄曲霉CA14PTs(Δku70ΔpyrG)菌株为出发菌,利用pyrG筛选标记构建表达HA-SumO的重组菌株GHS(pyrG+),再通过重叠PCR法构建包含GHS(pyrG+)基因组中pyrG整合位点上、下游片段的融合片段,导入GHS(pyrG+)菌株原生质体,利用DNA同源重组和5-氟乳清酸(5-FOA)的负筛选剔除pyrG筛选标记,重新获得具有尿嘧啶营养缺陷的重组菌株GHS(pyrG-).通过测序分析,确认GHS(pyrG-)重组菌株基因组中的pyrG筛选标记已被剔除且无其他序列残留.免疫杂交分析结果表明,剔除pyrG筛选标记不影响重组菌株的蛋白表达模式.
Keyword ：
pyrG遗传筛选标记 pyrG遗传筛选标记 不依赖同向重复序列 不依赖同向重复序列 循环利用 循环利用 黄曲霉 黄曲霉
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| GB/T 7714 | 聂鑫怡 , 薛杨 , 王银春 et al. 黄曲霉中pyrG筛选标记循环利用的方法 [J]. | 福建农林大学学报(自然科学版) , 2021 , 50 (02) : 270-275 . |
| MLA | 聂鑫怡 et al. "黄曲霉中pyrG筛选标记循环利用的方法" . | 福建农林大学学报(自然科学版) 50 . 02 (2021) : 270-275 . |
| APA | 聂鑫怡 , 薛杨 , 王银春 , 丁霞飞 , 汪世华 . 黄曲霉中pyrG筛选标记循环利用的方法 . | 福建农林大学学报(自然科学版) , 2021 , 50 (02) , 270-275 . |
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本发明公开了一种热休克转录因子1显性负效应突变体dn‑Hsf1及其应用，属于生物技术领域。通过同源比对人类和黄曲霉(Aspergillus flavus)中的热休克转录因子1 HSF1蛋白，将黄曲霉Hsf1蛋白C末端的第576位至第788位共213个氨基酸残基删除，获得黄曲霉中热休克转录因子1显性负效应突变体dn‑Hsf1蛋白的氨基酸序列如SEQ ID NO.1所示，编码核苷酸序列如SEQ ID NO.2所示。该显性负效应突变体dn‑Hsf1能抑制正常Hsf1在真菌体内发挥功能，从而抑制真菌的生长，应用于防控真菌的污染方面。
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| GB/T 7714 | 聂鑫怡 , 王银春 , 李博文 et al. 一种热休克转录因子1显性负效应突变体及其应用 : CN202010121694.X[P]. | 2020-02-26 . |
| MLA | 聂鑫怡 et al. "一种热休克转录因子1显性负效应突变体及其应用" : CN202010121694.X. | 2020-02-26 . |
| APA | 聂鑫怡 , 王银春 , 李博文 , 张轶 , 薛杨 , 王佳琪 et al. 一种热休克转录因子1显性负效应突变体及其应用 : CN202010121694.X. | 2020-02-26 . |
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本发明公开了一种新的pyrG筛选标记循环利用的方法及其应用，属于生物技术领域。该方法可从真菌基因组中剔除pyrG筛选标记而不依赖于pyrG两端的同向重复序列，不会在基因组上残留多余重复序列片段，剔除pyrG的重组菌能再次作为出发菌株使用pyrG进行遗传转化，实现pyrG筛选标记的循环利用。本发明的pyrG循环利用方法适用于以乳清苷‑5’‑磷酸脱羧酶编码基因URA3/pyrG表达元件作为遗传筛选标记的真菌，操作简便易行，不影响菌株遗传背景和性状，应用前景广阔。
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| GB/T 7714 | 聂鑫怡 , 王银春 , 薛杨 et al. 一种pyrG筛选标记循环利用的方法及应用 : CN202010974420.5[P]. | 2020-09-16 . |
| MLA | 聂鑫怡 et al. "一种pyrG筛选标记循环利用的方法及应用" : CN202010974420.5. | 2020-09-16 . |
| APA | 聂鑫怡 , 王银春 , 薛杨 , 汪世华 , 丁霞飞 , 王佳琪 . 一种pyrG筛选标记循环利用的方法及应用 : CN202010974420.5. | 2020-09-16 . |
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