Putative Role of Pith Cell Wall Phenylpropanoids inSesamia nonagrioides(Lepidoptera:  Noctuidae) Resistance

2006 ◽  
Vol 54 (6) ◽  
pp. 2274-2279 ◽  
Author(s):  
Rogelio Santiago ◽  
Ana Butron ◽  
John T. Arnason ◽  
Lana M. Reid ◽  
Xose C. Souto ◽  
...  
2002 ◽  
Vol 22 (1-2) ◽  
pp. 209-222 ◽  
Author(s):  
Bénédicte Flambard

2020 ◽  
Vol 2 (1) ◽  
Author(s):  
Fangwei Yu ◽  
Shenyun Wang ◽  
Wei Zhang ◽  
Hong Wang ◽  
Li Yu ◽  
...  

Abstract The members of myeloblastosis transcription factor (MYB TF) family are involved in the regulation of biotic and abiotic stresses in plants. However, the role of MYB TF in phosphorus remobilization remains largely unexplored. In the present study, we show that an R2R3 type MYB transcription factor, MYB103, is involved in phosphorus (P) remobilization. MYB103 was remarkably induced by P deficiency in cabbage (Brassica oleracea var. capitata L.). As cabbage lacks the proper mutant for elucidating the mechanism of MYB103 in P deficiency, another member of the crucifer family, Arabidopsis thaliana was chosen for further study. The transcript of its homologue AtMYB103 was also elevated in response to P deficiency in A. thaliana, while disruption of AtMYB103 (myb103) exhibited increased sensitivity to P deficiency, accompanied with decreased tissue biomass and soluble P concentration. Furthermore, AtMYB103 was involved in the P reutilization from cell wall, as less P was released from the cell wall in myb103 than in wildtype, coinciding with the reduction of ethylene production. Taken together, our results uncover an important role of MYB103 in the P remobilization, presumably through ethylene signaling.


Medicines ◽  
2021 ◽  
Vol 8 (7) ◽  
pp. 38
Author(s):  
Kyung-Hyun Cho

The composition and properties of apolipoprotein (apo) A-I and apoA-II in high-density lipoproteins (HDL) might be critical to SARS-CoV-2 infection via SR-BI and antiviral activity against COVID-19. HDL containing native apoA-I showed potent antiviral activity, while HDL containing glycated apoA-I or other apolipoproteins did not. However, there has been no report to elucidate the putative role of apoA-II in the antiviral activity of HDL.


2021 ◽  
Vol 22 (3) ◽  
pp. 1110
Author(s):  
Gema González-Rubio ◽  
Ángela Sellers-Moya ◽  
Humberto Martín ◽  
María Molina

The Mitogen-Activated Protein Kinase (MAPK) Slt2 is central to signaling through the yeast Cell Wall Integrity (CWI) pathway. MAPKs are regulated by phosphorylation at both the threonine and tyrosine of the conserved TXY motif within the activation loop (T190/Y192 in Slt2). Since phosphorylation at both sites results in the full activation of MAPKs, signaling through MAPK pathways is monitored with antibodies that detect dually phosphorylated forms. However, most of these antibodies also recognize monophosphorylated species, whose relative abundance and functionality are diverse. By using different phosphospecific antibodies and phosphate-affinity (Phos-tag) analysis on distinct Slt2 mutants, we determined that Y192- and T190-monophosphorylated species coexist with biphosphorylated Slt2, although most of the Slt2 pool remains unphosphorylated following stress. Among the monophosphorylated forms, only T190 exhibited biological activity. Upon stimulation, Slt2 is first phosphorylated at Y192, mainly by the MAPKK Mkk1, and this phosphorylation is important for the subsequent T190 phosphorylation. Similarly, dephosphorylation of Slt2 by the Dual Specificity Phosphatase (DSP) Msg5 is ordered, with dephosphorylation of T190 depending on previous Y192 dephosphorylation. Whereas Y192 phosphorylation enhances the Slt2 catalytic activity, T190 is essential for this activity. The conserved T195 residue is also critical for Slt2 functionality. Mutations that abolish the activity of Slt2 result in a high increase in inactive Y192-monophosphorylated Slt2. The coexistence of different Slt2 phosphoforms with diverse biological significance highlights the importance of the precise detection of the Slt2 phosphorylation status.


Author(s):  
Giulia Maria Pires dos Santos ◽  
Gustavo Ramalho Cardoso dos Santos ◽  
Mariana Ingrid Dutra da Silva Xisto ◽  
Rodrigo Rollin-Pinheiro ◽  
Andréa Regina de Souza Baptista ◽  
...  

2021 ◽  
Vol 31 (1) ◽  
Author(s):  
Gurmehar Kaur Grewal ◽  
Neelam Joshi ◽  
Yadhu Suneja

Abstract Background Spodoptera litura (Fab.) (Lepidoptera: Noctuidae) is a serious agricultural pest that infests many commercially important crops of Southeast Asian countries. Indiscriminate use of chemical pesticides has led to various health hazards as well as insecticide resistance. Entomopathogenic fungi (EPF) provide an important alternative as biological control agents. Metarhizium rileyi is an EPF with a specific host range for lepidopteran pests. The present study aimed to identify virulent M. rileyi isolate against S. litura larvae and analyse their extracellular cuticle-degrading enzyme activities. Results Three M. rileyi isolates viz M. rileyi NIPHM, M. rileyi MTCC 4254 and M. rileyi MTCC 10395 formulations were evaluated at different concentrations against 2nd instar larvae of S. litura. A maximum percent mortality of 63.33% was recorded in M. rileyi NIPHM (12 g/l), followed by M. rileyi MTCC 4254 (58.33%) at the same concentration, 10 days post-treatment. Maximum means of chitinase, protease and lipase activities (0.44, 1.58 and 2.95 U/ml, respectively) were recorded in the case of M. rileyi NIPHM. Correlation analysis was positive between enzyme activity and larval mortality. Conclusions Metarhizium rileyi NIPHM recorded the highest enzymatic activity and exhibited the maximum mortality rate against 2nd instar larvae of S. litura, suggesting the possible role of these enzymes in the pathogenicity of the fungus. Further knowledge in this regard may help in the development of enzyme-based screening methods for selecting virulent fungal isolates for the eco-friendly management of crop pests.


Yeast ◽  
2021 ◽  
Author(s):  
Qingguo Guo ◽  
Na Meng ◽  
Guanzhi Fan ◽  
Dong Sun ◽  
Yuan Meng ◽  
...  

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