Pub Date : 2024-07-01DOI: 10.1016/j.jia.2024.07.025
Junxia Deng, Ke Liu, Xiangqian Feng, Jiayu Ye, Matthew Tom Harrison, Peter de Voil, Tajamul Hussain, Liying Huang, Xiaohai Tian, Meixue Zhou, Yunbo Zhang
{"title":"Exploring strategies for agricultural sustainability in super hybrid rice using the food-carbon-nitrogen-water-energy-profit nexus framework","authors":"Junxia Deng, Ke Liu, Xiangqian Feng, Jiayu Ye, Matthew Tom Harrison, Peter de Voil, Tajamul Hussain, Liying Huang, Xiaohai Tian, Meixue Zhou, Yunbo Zhang","doi":"10.1016/j.jia.2024.07.025","DOIUrl":"https://doi.org/10.1016/j.jia.2024.07.025","url":null,"abstract":"","PeriodicalId":16305,"journal":{"name":"Journal of Integrative Agriculture","volume":null,"pages":null},"PeriodicalIF":4.6,"publicationDate":"2024-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141842804","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-01DOI: 10.1016/j.jia.2024.07.033
Bing Han, Yicheng He, Jun Zhou, Yufei Wang, Lina Shi, Zhenrong Lin, Lu Yu, Wantong Zhang, Yiyi Geng, Xinqing Shao
{"title":"Non-linear responses of the plant phosphorus pool and soil available phosphorus to short-term nitrogen addition in an alpine meadow","authors":"Bing Han, Yicheng He, Jun Zhou, Yufei Wang, Lina Shi, Zhenrong Lin, Lu Yu, Wantong Zhang, Yiyi Geng, Xinqing Shao","doi":"10.1016/j.jia.2024.07.033","DOIUrl":"https://doi.org/10.1016/j.jia.2024.07.033","url":null,"abstract":"","PeriodicalId":16305,"journal":{"name":"Journal of Integrative Agriculture","volume":null,"pages":null},"PeriodicalIF":4.6,"publicationDate":"2024-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141850251","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-01DOI: 10.1016/j.jia.2024.07.019
Dongdong Sun, Yutong Zhang, Song Cao, Xiaoqing Wang, Qian Cao, Sai Zhang, Guirong Wang, Yang Liu
{"title":"A compound produced by Helicoverpa armigera male genitalia activates a conserved pheromone receptor","authors":"Dongdong Sun, Yutong Zhang, Song Cao, Xiaoqing Wang, Qian Cao, Sai Zhang, Guirong Wang, Yang Liu","doi":"10.1016/j.jia.2024.07.019","DOIUrl":"https://doi.org/10.1016/j.jia.2024.07.019","url":null,"abstract":"","PeriodicalId":16305,"journal":{"name":"Journal of Integrative Agriculture","volume":null,"pages":null},"PeriodicalIF":4.6,"publicationDate":"2024-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141844039","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-01DOI: 10.1016/j.jia.2024.07.037
Ting Pan, Ruiting Guo, Weiwei Wang, Xing Liu, Bing Xia, Linshu Jiang, Ming Liu
{"title":"Mechanism of mitigating on Deoxynivalenol-induced intestinal toxicity in swine and its dietary regulation strategy1","authors":"Ting Pan, Ruiting Guo, Weiwei Wang, Xing Liu, Bing Xia, Linshu Jiang, Ming Liu","doi":"10.1016/j.jia.2024.07.037","DOIUrl":"https://doi.org/10.1016/j.jia.2024.07.037","url":null,"abstract":"","PeriodicalId":16305,"journal":{"name":"Journal of Integrative Agriculture","volume":null,"pages":null},"PeriodicalIF":4.6,"publicationDate":"2024-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141847736","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-01DOI: 10.1016/j.jia.2024.07.022
Ameer Khan, Farah Kanwal, Muhammad Shazad, Shama Naz, Sanaullah Jalil, Guoping Zhang
{"title":"Interactions of arsenic and phosphorus in their uptake and transportation in plants: Advances and prospective research on the mechanisms and approaches for alleviating arsenic stress","authors":"Ameer Khan, Farah Kanwal, Muhammad Shazad, Shama Naz, Sanaullah Jalil, Guoping Zhang","doi":"10.1016/j.jia.2024.07.022","DOIUrl":"https://doi.org/10.1016/j.jia.2024.07.022","url":null,"abstract":"","PeriodicalId":16305,"journal":{"name":"Journal of Integrative Agriculture","volume":null,"pages":null},"PeriodicalIF":4.6,"publicationDate":"2024-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141853941","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-07-01DOI: 10.1016/j.jia.2024.07.031
Xi-jun Wang, Hong Huo, Lei Shuai, Jin-ying Ge, Liyan Peng, Jinming Wang, Shuang Xiao, Wei-ye Chen, Z. Wen, Jinliang Wang, Z. Bu
{"title":"Evaluation of safety and immunogenicity of a genetically modified rabies virus for use as an oral vaccine in several non-target species1","authors":"Xi-jun Wang, Hong Huo, Lei Shuai, Jin-ying Ge, Liyan Peng, Jinming Wang, Shuang Xiao, Wei-ye Chen, Z. Wen, Jinliang Wang, Z. Bu","doi":"10.1016/j.jia.2024.07.031","DOIUrl":"https://doi.org/10.1016/j.jia.2024.07.031","url":null,"abstract":"","PeriodicalId":16305,"journal":{"name":"Journal of Integrative Agriculture","volume":null,"pages":null},"PeriodicalIF":4.6,"publicationDate":"2024-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141853988","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-27DOI: 10.1016/j.jia.2024.06.005
Jikun Mei, Xuan Jiang, Fengyang Li, Zengshuai Wu, Tong Wu, Junhui Zhu, Hexiang Jiang, Ziheng Li, Na Li, Liancheng Lei
serotype 2 (SS2) is an emerging zoonotic pathogen that causes meningitis in humans and pigs. It not only brings huge economic losses to the pig industry but also seriously threatens public health security. However, the mechanisms by which SS2 enters the brain and induces meningitis is not fully understood. Here, we investigated the role and mechanism of the SS2 collagenase-like protease (Clp) in promoting the passage of the bacterium across the blood-brain barrier (BBB). We found that SS2 Clp enhanced virulence and tissue colonization, and promoted the destruction of the BBB in mice. Compared with wild-type SS2, the ability of a Δ mutant to cross human brain microvascular endothelial (hCMEC/D3) cell monolayers decreased, whereas the addition of recombinant protein rClp increased permeability. rClp also significantly promoted the adhesion of SS2 to hCMEC/D3, inhibited the expression of intercellular tight junction proteins ZO-1, Occludin, and Claudin-5 independent of its enzyme activity, and induced hCMEC/D3 apoptosis through the cell receptor ligand apoptosis and mitochondrial apoptosis pathways partly dependent on its enzyme activity, resulting in BBB destruction and increased permeability. Moreover, Clp increased macrophage (F4/80+), monocytes (F4/80-Ly6C+), and neutrophils (Ly6G+) infiltration into the brain after SS2 infection. Thus, SS2 Clp is required for the passage of the bacterium across the BBB, and the results, provide a theoretical basis for better prevention and treatment of SS2-induced meningitis.
{"title":"Streptococcus suis serotype 2 collagenase-like protease promotes meningitis by increasing blood-brain barrier permeability1","authors":"Jikun Mei, Xuan Jiang, Fengyang Li, Zengshuai Wu, Tong Wu, Junhui Zhu, Hexiang Jiang, Ziheng Li, Na Li, Liancheng Lei","doi":"10.1016/j.jia.2024.06.005","DOIUrl":"https://doi.org/10.1016/j.jia.2024.06.005","url":null,"abstract":"serotype 2 (SS2) is an emerging zoonotic pathogen that causes meningitis in humans and pigs. It not only brings huge economic losses to the pig industry but also seriously threatens public health security. However, the mechanisms by which SS2 enters the brain and induces meningitis is not fully understood. Here, we investigated the role and mechanism of the SS2 collagenase-like protease (Clp) in promoting the passage of the bacterium across the blood-brain barrier (BBB). We found that SS2 Clp enhanced virulence and tissue colonization, and promoted the destruction of the BBB in mice. Compared with wild-type SS2, the ability of a Δ mutant to cross human brain microvascular endothelial (hCMEC/D3) cell monolayers decreased, whereas the addition of recombinant protein rClp increased permeability. rClp also significantly promoted the adhesion of SS2 to hCMEC/D3, inhibited the expression of intercellular tight junction proteins ZO-1, Occludin, and Claudin-5 independent of its enzyme activity, and induced hCMEC/D3 apoptosis through the cell receptor ligand apoptosis and mitochondrial apoptosis pathways partly dependent on its enzyme activity, resulting in BBB destruction and increased permeability. Moreover, Clp increased macrophage (F4/80+), monocytes (F4/80-Ly6C+), and neutrophils (Ly6G+) infiltration into the brain after SS2 infection. Thus, SS2 Clp is required for the passage of the bacterium across the BBB, and the results, provide a theoretical basis for better prevention and treatment of SS2-induced meningitis.","PeriodicalId":16305,"journal":{"name":"Journal of Integrative Agriculture","volume":null,"pages":null},"PeriodicalIF":4.8,"publicationDate":"2024-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141577664","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-27DOI: 10.1016/j.jia.2024.06.006
Xiaodong Gong, Dan Han, Lu Zhang, Guibo Yin, Junfang Yang, Hui Jia, Zhiyan Cao, Jingao Dong, Yuwei Liu, Shouqin Gu
LysM proteins contain the lysin domain (LysM), bind chitin and are found in various organisms including fungi. In phytopathogenic fungi, certain LysM proteins act as effectors to inhibit host immunity, thus increasing fungal virulence. However, our understanding of the LysM protein family in is limited. In this study, eight genes are identified and designated as to . The analysis of sequence features indicates that five proteins (StLysM1, StLysM2, StLysM5, StLysM6, and StLysM7) are potential effectors. Phylogenetic analysis suggests that the StLysMs are divided into fungal/bacterial and fungus-specific subclasses. Domain architecture analysis reveals that the five StLysM effectors exclusively harbor the LysM domain, whereas the other three StLysM proteins contain additional functional domains. Sequence conservation analysis shows that the fungal-specific LysM domain sequences share the GDxTC and WNP motifs as well as three highly conserved cysteine residues. Conversely, the LysM domain sequences from the bacterial/fungal branch have few conserved sites. Moreover, expression profiling analysis shows that the gene is significantly upregulated during the infection of maize. Yeast secretion assays and transient expression experiments demonstrate that StLysM1 is a secreted protein that can suppress BAX/INF1-induced programmed cell death in . Further functional analysis suggests that StLysM1 cannot interact with itself but it can bind chitin. The transient expression of inhibits the chitin-triggered plant immune response, increasing susceptibility to the phytopathogenic fungus in . This study reveals that the LySM protein family consists of eight members, highlighting the significance of StLysM1 as a vital effector in regulating plant immunity. The results provide insight into StLysMs and establish a foundation for understanding the roles of StLysM proteins in the pathogenic process of
{"title":"Comprehensive analysis of the LysM protein family and functional characterization of the key LysM effector StLysM1, which modulates plant immunity in Setosphaeria turcica1","authors":"Xiaodong Gong, Dan Han, Lu Zhang, Guibo Yin, Junfang Yang, Hui Jia, Zhiyan Cao, Jingao Dong, Yuwei Liu, Shouqin Gu","doi":"10.1016/j.jia.2024.06.006","DOIUrl":"https://doi.org/10.1016/j.jia.2024.06.006","url":null,"abstract":"LysM proteins contain the lysin domain (LysM), bind chitin and are found in various organisms including fungi. In phytopathogenic fungi, certain LysM proteins act as effectors to inhibit host immunity, thus increasing fungal virulence. However, our understanding of the LysM protein family in is limited. In this study, eight genes are identified and designated as to . The analysis of sequence features indicates that five proteins (StLysM1, StLysM2, StLysM5, StLysM6, and StLysM7) are potential effectors. Phylogenetic analysis suggests that the StLysMs are divided into fungal/bacterial and fungus-specific subclasses. Domain architecture analysis reveals that the five StLysM effectors exclusively harbor the LysM domain, whereas the other three StLysM proteins contain additional functional domains. Sequence conservation analysis shows that the fungal-specific LysM domain sequences share the GDxTC and WNP motifs as well as three highly conserved cysteine residues. Conversely, the LysM domain sequences from the bacterial/fungal branch have few conserved sites. Moreover, expression profiling analysis shows that the gene is significantly upregulated during the infection of maize. Yeast secretion assays and transient expression experiments demonstrate that StLysM1 is a secreted protein that can suppress BAX/INF1-induced programmed cell death in . Further functional analysis suggests that StLysM1 cannot interact with itself but it can bind chitin. The transient expression of inhibits the chitin-triggered plant immune response, increasing susceptibility to the phytopathogenic fungus in . This study reveals that the LySM protein family consists of eight members, highlighting the significance of StLysM1 as a vital effector in regulating plant immunity. The results provide insight into StLysMs and establish a foundation for understanding the roles of StLysM proteins in the pathogenic process of","PeriodicalId":16305,"journal":{"name":"Journal of Integrative Agriculture","volume":null,"pages":null},"PeriodicalIF":4.8,"publicationDate":"2024-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141720125","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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