scholarly journals Comparative Proteomics Analysis of Phosphine-Resistant and Phosphine-Susceptible Sitophilus oryzae (Coleoptera: Curculionidae)

2021 ◽  
Vol 11 (9) ◽  
pp. 4163
Author(s):  
Hyun-Na Koo ◽  
Seung Ju Seok ◽  
Hyun Kyung Kim ◽  
Gil-Hah Kim ◽  
Jeong Oh Yang
Keyword(s):  
Molecular Mechanisms ◽  
Citrate Synthase ◽  
Expression Profiles ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sitophilus Oryzae ◽  
Time Of Flight ◽  
Ionization Time ◽  
Flight Mass Spectrometry ◽  
Phosphine Resistance ◽  
Protein Expression Profiles

A proteomic method combining two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) and matrix-assisted laser desorption/ionization-time-of-flight/time-of-flight mass spectrometry (MALDI-TOF/TOF) was used to compare the protein expression profiles of phosphine-resistant (PH3-R) and -susceptible (PH3-S) strains of Sitophilus oryzae. Thirty-nine differentially expressed protein spots were identified between the PH3-R and PH3-S strains; 20 protein spots were upregulated, and 19 protein spots were downregulated in the PH3-R strain compared with their expression in the PH3-S strain. In particular, cytochrome oxidase subunit I showed 15-fold higher expression in the PH3-R strain than in the PH3-S strain. Additionally, citrate synthase 2, delta-1-pyrolline-5-carboxylate dehydrogenase, and triose-phosphate isomerase were highly expressed in the PH3-R strain. In summary, our study has improved understanding of the molecular mechanisms of phosphine resistance in the rice weevil.

Evaluation of Docetaxel-Sensitive and Docetaxel-Resistant Proteomes in PC-3 Cells

2015 ◽  
Vol 95 (1) ◽  
pp. 114-119 ◽  
Author(s):  
Shulu Zu ◽  
Weiming Ma ◽  
Pan Xiao ◽  
Yazhou Cui ◽  
Tianjia Ma ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Molecular Mechanisms ◽  
Polyacrylamide Gel Electrophoresis ◽  
Acquired Resistance ◽  
Castration Resistant Prostate Cancer ◽  
Ionization Time ◽  
Flight Mass Spectrometry ◽  
Docetaxel Resistance ◽  
Castration Resistant ◽  
Glucose Regulated Protein

Objectives: Docetaxel was the first drug with proven survival benefit in men with castration-resistant prostate cancer. Acquired resistance to docetaxel precedes fatality in castration-resistant prostate cancer. The aims of this study were to evaluate docetaxel-sensitive and docetaxel-resistant proteomes in PC-3 cells, and to investigate the molecular mechanism of docetaxel-resistant PC-3 cells. Methods: Docetaxel-resistant PC-3 cells were developed by docetaxel dose escalation. The global profiling of the protein expression was investigated in docetaxel-sensitive and docetaxel-resistant proteomes in PC-3 cells using 2-dimensional polyacrylamide gel electrophoresis/matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Results: Forty-nine differential proteins were found in docetaxel-resistant PC-3 cells in comparison with docetaxel-sensitive PC-3 cells. Expression in 29 proteins was upregulated, whereas expression in 20 proteins was downregulated. ATP synthase and galectin-1 were involved in the formation of tumor vessels; calreticulin, cathepsin D, and cofilin were involved in tumor metastasis, and GRP78 (78-kDa glucose-regulated protein) and microtubule-associated protein-6 were involved in drug resistance of tumor. Conclusion: It is suggested that a proteomic expression difference exists between docetaxel-sensitive and docetaxel-resistant PC-3 cells, which would be helpful for further understanding the molecular mechanisms of docetaxel resistance in PC-3 cells.

scholarly journals Aptamers Against the β-Conglutin Allergen: Insights into the Behavior of the Shortest Multimeric(Intra)Molecular DNA G-Quadruplex

2021 ◽  
Vol 22 (3) ◽  
pp. 1150
Author(s):  
Ciara K. O’ Sullivan ◽  
Teresa Mairal ◽  
Miriam Jauset-Rubio ◽  
Marketa Svobodova ◽  
Vasso Skouridou ◽  
...  
Keyword(s):  
High Performance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Time Of Flight ◽  
Higher Order ◽  
Binding Ability ◽  
Ionization Time ◽  
Flight Mass Spectrometry ◽  
G Quadruplex ◽  
Derivatives Of ◽  
Order Structures

In previous work, a 93-mer aptamer was selected against the anaphylactic allergen, β-conglutin and truncated to an 11-mer, improving the affinity by two orders of magnitude, whilst maintaining the specificity. This 11-mer was observed to fold in a G-quadruplex, and preliminary results indicated the existence of a combination of monomeric and higher-order structures. Building on this previous work, in the current study, we aimed to elucidate a deeper understanding of the structural forms of this 11-mer and the effect of the structure on its binding ability. A battery of techniques including polyacrylamide gel electrophoresis, high-performance liquid chromatography in combination with electrospray ionization time-of-flight mass spectrometry, matrix-assisted laser desorption/ionization time-of-flight, thermal binding analysis, circular dichroism and nuclear magnetic resonance were used to probe the structure of both the 11-mer and the 11-mer flanked with TT- at either the 5′ or 3′ end or at both ends. The TT-tail at the 5′ end hinders stacking effects and effectively enforces the 11-mer to maintain a monomeric form. The 11-mer and the TT- derivatives of the 11-mer were also evaluated for their ability to bind its cognate target using microscale thermophoresis and surface plasmon resonance, and biolayer interferometry confirmed the nanomolar affinity of the 11-mer. All the techniques utilized confirmed that the 11-mer was found to exist in a combination of monomeric and higher-order structures, and that independent of the structural form present, nanomolar affinity was observed.

Proteins differentially expressed in conidia and mycelia of the entomopathogenic fungusMetarhizium anisopliaesensu stricto

2013 ◽  
Vol 59 (7) ◽  
pp. 443-448 ◽  
Author(s):  
Yubin Su ◽  
Qingfeng Guo ◽  
Jie Tu ◽  
Xiaoxia Li ◽  
Lixue Meng ◽  
...  
Keyword(s):  
Protein Expression ◽  
Proteomic Analysis ◽  
Developmental Stages ◽  
Expression Profiles ◽  
Laser Desorption Ionization ◽  
Appressorium Formation ◽  
Ionization Time ◽  
Flight Mass Spectrometry ◽  
Protective Processes ◽  
Protein Expression Profiles

Metarhizium anisopliae is a well-characterized entomopathogenic fungus that attacks a variety of insects. Its conidia are involved in its propagation and also in its infection of host insects. To investigate the protein expression profiles and to identify the proteins related to development and pathogenesis, we performed a comparative proteomic analysis of the conidia and mycelia of an M. anisopliae strain (Ma1291). The analysis used 2-dimensional gel electrophoresis and matrix-assisted laser desorption ionization time-of-flight mass spectrometry. We detected 898 ± 37 protein spots in conidia and 1072 ± 24 in mycelia of strain Ma1291. A comparison of the 2 protein-expression profiles indicated that only 28% of protein spots were common to both developmental stages. Finally, we identified 30 proteins (19 from conidia and 11 from mycelia). The identified proteins exclusive to conidia were those involved in protective processes, appressorium formation, and degradation of the host cuticle (protease PR1H). The identified proteins exclusive to mycelia included major proteins participating in biosynthetic and energy metabolism, such as UTP-glucose-1-phosphate uridylyltransferase and heat shock protein 70. This research provides the first proteomic analysis of different developmental stages of M. anisopliae, and the results should facilitate clarification of the molecular basis of these epigenetic variations.

scholarly journals Proteins Associated with Culex nigripalpus Nucleopolyhedrovirus Occluded Virions

2007 ◽  
Vol 81 (9) ◽  
pp. 4585-4590 ◽  
Author(s):  
Omaththage Perera ◽  
Terry B. Green ◽  
Stanley M. Stevens ◽  
Susan White ◽  
James J. Becnel
Keyword(s):  
Mass Spectrometry ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Time Of Flight ◽  
Open Reading Frames ◽  
Structural Proteins ◽  
Ionization Time ◽  
Protein Databases ◽  
Flight Mass Spectrometry ◽  
Culex Nigripalpus

ABSTRACT Occlusion-derived virions (ODVs) of the nucleopolyhedrovirus of Culex nigripalpus (CuniNPV) were purified by Ludox density gradient ultracentrifugation, and the proteins were separated by one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Proteins were identified by using Edman sequencing, matrix-assisted laser desorption ionization-time of flight mass spectrometry, nanoelectrospray quadrupole time-of-flight mass spectrometry, or a combination of these methods. Half of the 44 polypeptide sequences identified in this analysis were unique open reading frames (ORFs) encoded by the CuniNPV genome and did not show similarity to any other sequences present in protein databases. Of the 22 polypeptides that showed similarities to other baculovirus-encoded proteins, only 17 sequences have previously been identified as structural proteins. The newly identified CuniNPV structural proteins cun058, cun059, cun087, cun106, and cun109 are homologues of Autographa californica nucleopolyhedrovirus (AcMNPV) ORFs 68, 62, 98, 81, and 2, respectively. The products of four genes, namely, lef-1 (cun045), alkaline exonuclease (cun054), helicase (cun089), and DNA polymerase (cun091), were not detected in the CuniNPV ODV preparations. These four genes are conserved among all annotated baculovirus genomes, and their homologues have been detected in the ODV of AcMNPV.

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