ABSTRACT
Small secreted peptides (SSPs) are essential for defense mechanisms in plant-microbe interactions, acting as danger-associated molecular patterns (DAMPs). Despite the first discovery of SSPs over three decades ago, only a limited number of SSP families, particularly within Solanaceae plants, have been identified due to inefficient approaches. This study employed comparative genomics screens with Solanaceae proteomes (tomato, tobacco, and pepper) to discover a novel SSP family, SolP. Bioinformatics analysis suggests that SolP may serve as an endogenous signal initiating the plant PTI response. Interestingly, SolP family members from tomato, tobacco, and pepper share an identical sequence (VTSNALALVNRFAD), named SlSolP12 (also referred to as NtSolP15 or CaSolP1). Biochemical and phenotypic analyses revealed that synthetic SlSolP12 peptide triggers multiple defense responses: ROS burst, MAPK activation, callose deposition, stomatal closure, and expression of immune defense genes. Furthermore, SlSolP12 enhances systemic resistance against Botrytis cinerea infection in tomato plants and interferes with classical peptides, flg22 and Systemin, which modulate the immune response. Remarkably, SolP12 activates ROS in diverse plant species, such as Arabidopsis thaliana, soybean, and rice, showing a broad spectrum of biological activities. This study provides valuable approaches for identifying endogenous SSPs and highlights SlSolP12 as a novel DAMP that could serve as a useful target for crop protection.
Subject(s)
Botrytis , Genomics , Plant Diseases , Plant Immunity , Plant Proteins , Solanum lycopersicum , Solanum lycopersicum/immunology , Solanum lycopersicum/genetics , Solanum lycopersicum/microbiology , Plant Proteins/genetics , Plant Proteins/immunology , Plant Proteins/metabolism , Plant Diseases/microbiology , Plant Diseases/immunology , Plant Diseases/genetics , Plant Immunity/genetics , Peptides/immunology , Peptides/chemistry , Disease Resistance/genetics , Disease Resistance/immunology , Gene Expression Regulation, Plant , Nicotiana/immunology , Nicotiana/genetics , Nicotiana/microbiology , Nicotiana/metabolism , Capsicum/immunology , Capsicum/genetics , Capsicum/microbiology , Capsicum/chemistryABSTRACT
Pancreatic ductal adenocarcinoma (PDAC) is characterized by hypoxic tumor microenvironment (TME), which aids tumor progression, drug resistance, and immune evasion. Dual-specificity phosphatase 2 (DUSP2), a member of the mitogen-activated protein kinase phosphatase family, regulates pancreatic cancer metastasis. However, its role in the hypoxic TME in PDAC remains unknown. We explored the role of DUSP2 by simulating the hypoxic TME. DUSP2 significantly promoted apoptosis in PDAC both in vitro and in vivo, mainly through AKT1 rather than ERK1/2. Mechanistically, DUSP2 competed with AKT1 to bind to casein kinase 2 alpha 1 (CSNK2A1) and inhibited the phosphorylation of AKT1, which plays a crucial role in apoptosis resistance. Interestingly, aberrant activation of AKT1 resulted in an increase in the ubiquitin E3 ligase tripartite motif-containing 21 (TRIM21), which binds to and mediates the ubiquitination-dependent proteasomal degradation of DUSP2. Overall, we identified CSNK2A1 as a novel binding partner of DUSP2 that promotes PDAC apoptosis through CSN2KA1/AKT1 in an ERK1/2-independent manner. Activation of AKT1 also mediated proteasomal degradation of DUSP2 via the AKT1/TRIM21 positive feedback loop. We propose increasing the level of DUSP2 as a potential therapeutic strategy for PDAC.
Subject(s)
Carcinoma, Pancreatic Ductal , Pancreatic Neoplasms , Humans , Dual Specificity Phosphatase 2/metabolism , Pancreatic Neoplasms/pathology , Hypoxia , Carcinoma, Pancreatic Ductal/pathology , Apoptosis , Cell Line, Tumor , Tumor Microenvironment , Proto-Oncogene Proteins c-akt , Pancreatic NeoplasmsABSTRACT
OBJECTIVE: To explore the variations of gene S in hepatitis B viruses of hepatitis B patients and provide experimental evidences for the mutation analysis of viral gene. METHODS: The virus DNA load in hepatitis B patient donors was detected by real-time polymerase chain reaction (PCR) and gene sequence analysis. And a comparison was made with standard strain by the software DNAstar. RESULTS: (1) Gene S was successfully amplified and sequenced in 15 hepatitis B patients. Three samples had IâT mutation at residue 126 in HBsAg "a" antigenic determinant. (2) Sixteen hepatitis B patients had 67 nucleotide mutations, including 14 residues in PreS1 and 6 residues in PreS2. Mutations nt 3036 TâC, nt 3039 TâG, nt 3066 CâT and L88V existed in PreS1 gene in all samples. CONCLUSION: HBV genome is susceptible to nucleotide mutations. Some residues have geographically restricted mutations in gene S region. And understanding the significance of these mutations may help clarify the pathogenesis of hepatitis B and provide new experimental evidence for its gene diagnosis and prevention.
Subject(s)
Hepatitis B Surface Antigens/genetics , Hepatitis B virus/genetics , Hepatitis B/virology , Mutation , Polymorphism, Single Nucleotide , DNA Mutational Analysis , Genes, Viral , HumansABSTRACT
The asymmetric unit of the title complex, [Ag(4)W(2)S(8)(C(25)H(22)P(2))(3)]·2C(3)H(7)NO, tris-[µ(2)-bis-(diphenyl-phosphino)meth-ane]-3:6κ(2)P:P';4:5κ(2)P:P';5:6κ(2)P:P'-µ(5)-sulfido-2:3:4:5:6κ(5)S-µ(3)-sulfido-1:3:4κ(3)S-tetra-µ(2)-sulfido-1:3κ(2)S;1:4κ(2)S;2:5κ(2)S;2:6κ(2)S-disulfido-1κS,2κS-tetra-silver(I)ditungsten(VI) N,N-dimethyl-formamide disolvate, contains two [WS(4)](2-) anions, four silver cations, three bidentate-bridging bis-(diphenyl-phosphino)methane (dppm) ligands and two N,N-dimethyl-formamide (DMF) solvent mol-ecules. The coordination geometry of each Ag atom is distorted tetra-hedral. Two Ag ions are coordinated by µ(2)-S and µ(5)-S atoms, and by two P atoms from two dppm ligands, while the other two Ag atoms are coordinated by µ(2)-S, µ(3)-S and µ(5)-S atoms, and by one P atom from a dppm ligand.
ABSTRACT
In the title complex, [Ag(C(18)H(15)P)(3)(ClO(4))], the silver coord-ination environment is dominated by the distorted P(3)AgO tetra-hedron in which Ag-O = 2.608â (12)â Å and the Ag-P bond lengths are 2.5663â (17), 2.5076(16) and 2.5450â (17)â Å. The perchlorate O-atoms are disordered over two positions in a 0.584â (14):0.416â (14) ratio.
ABSTRACT
In the title complex, [Ag(ClO(4))(CH(3)OH)(C(18)H(15)P)(2)], the angles around the central Ag(+) ion indicate that it is in a distorted tetrahedral coordination. The coordination sphere of silver is formed by two P atoms of two triphenyl-phosphine ligands, one O atom of a perchlorate anion and one O atom of a methanol mol-ecule. The crystal structure is stablized by a bifurcated inter-molecular O-Hâ¯O hydrogen bond, involving the O-H donor from methanol and two acceptor O atoms from the perchlorate anion, so forming a zigzag chain propagating in [010].
ABSTRACT
The structure of the title complex, [Ag(C(12)H(8)N(2))(C(18)H(15)P)]CF(3)SO(3), is based on a distorted trigonal-planar N(2)P coordination of the Ag(I) ion, provided by two N atoms of the bidentate phenanthroline ligand and one P atom of the triphenyl-phosphine ligand. The phenanthroline ligand and one phenyl ring of the triphenyl-phosphine ligand almost lie in one plane (maximum deviation = 0.014â Å from the best planes). The crystal structure may be stabilized by an inter-molecular C-Hâ¯O hydrogen bond between the phenanthroline ligand and the O atom of the trifluoro-methane-sulfonate anion.