scholarly journals More than a Toxin: Protein Inventory of Clostridium tetani Toxoid Vaccines

Proteomes ◽  
2019 ◽  
Vol 7 (2) ◽  
pp. 15 ◽  
Author(s):  
Jens Möller ◽  
Max Edmund Kraner ◽  
Andreas Burkovski
Keyword(s):  
Protein Content ◽  
Tetanus Toxin ◽  
Protein Quantification ◽  
Label Free ◽  
Clostridium Tetani ◽  
Tetanus Neurotoxin ◽  
Formaldehyde Crosslinking ◽  
Life Threatening ◽  
Toxin Protein ◽  
Efficient Protection

Clostridium tetani is the etiological agent of tetanus, a life-threatening bacterial infection. The most efficient protection strategy against tetanus is a vaccination with the C. tetani neurotoxin, which is inactivated by formaldehyde-crosslinking. Since we assumed that besides the tetanus toxin, other proteins of C. tetani may also be present in toxoid preparations, we analyzed commercially available vaccines from different countries in respect to their protein content using mass spectrometry. In total 991 proteins could be identified in all five analyzed vaccines, 206 proteins were common in all analyzed vaccines and 54 proteins from the 206 proteins were potential antigens. The additionally present proteins may contribute at least partially to protection against C. tetani infection by supporting the function of the vaccine against the devastating effects of the tetanus toxin indirectly. Two different label-free protein quantification methods were applied for an estimation of protein contents. Similar results were obtained with a Total Protein Approach (TPA)-based method and Protein Discoverer 2.2 software package based on the minora algorithm. Depending on the tetanus toxoid vaccine and the quantification method used, tetanus neurotoxin contributes between 14 and 76 % to the total C. tetani protein content and varying numbers of other C. tetani proteins were detected.

scholarly journals Label-free proteomic analysis of serum exosomes from paroxysmal atrial fibrillation patients

2021 ◽  
Vol 18 (1) ◽  
Author(s):  
Hanwen Ni ◽  
Wenqi Pan ◽  
Qi Jin ◽  
Yucai Xie ◽  
Ning Zhang ◽  
...  
Keyword(s):  
Atrial Fibrillation ◽  
Protein Folding ◽  
Protein Content ◽  
Complement System ◽  
Proteomic Analysis ◽  
Surface Composition ◽  
Label Free ◽  
Healthy Donors ◽  
Variable Surface ◽  
Serum Exosomes

Abstract Background Atrial fibrillation (AF) is the most common cardiac heterogeneous rhythm disorder. It represents a major cause of mortality and morbidity, mainly related to embolic events and heart failure. Mechanisms of AF are complex and remain incompletely understood. Recent evidence suggests exosomes are membrane-coated objects released by many cell-types. Their presence in body fluids and the variable surface composition and content render them attractive as a mechanism for potential biomarkers. However, the content of serum exosomes of AF patients has not been fully delineated. Methods In this work, the serum exosomes from AF patients and healthy donors were used to compare changes in the exosome protein content. Exosomes were isolated from serum of AF patients and healthy donors and their purity was confirmed by Western blotting assays and transmission electron microscopy (TEM). Label-free LC–MS/MS quantitative proteomic analysis was applied to analyze protein content of serum exosomes. Results A total of 440 exosomal protein groups were identified, differentially expressed proteins were filtrated with fold change ≥ 2.0 (AF/controls protein abundance ratio ≥ 2 or ≤ 0.5) and p value less than 0.05 (p < 0.05), significantly changed in abundance group contains 39 elevated proteins and 18 reduced proteins, while consistent presence/absence expression profile group contains 40 elevated proteins and 75 reduced proteins. Bioinformatic analysis of differential exosomal proteins confirmed the significant enrichment of components involved in the anticoagulation, complement system and protein folding. Parallel-Reaction Monitoring Relative Quantitative Analysis (PRM) further suggested that AF related to complement system and protein folding. Conclusions These results revealed the composition and potential function of AF serum exosomes, thus providing a new perspective on the complement system and protein folding to AF.

scholarly journals LFAQ: Toward Unbiased Label-Free Absolute Protein Quantification by Predicting Peptide Quantitative Factors

2018 ◽  
Vol 91 (2) ◽  
pp. 1335-1343 ◽  
Author(s):  
Cheng Chang ◽  
Zhiqiang Gao ◽  
Wantao Ying ◽  
Yan Fu ◽  
Yan Zhao ◽  
...  
Keyword(s):  
Protein Quantification ◽  
Label Free

Recent Technological Advances in the Mass Spectrometry-based Nanomedicine Studies: An Insight from Nanoproteomics

2019 ◽  
Vol 25 (13) ◽  
pp. 1536-1553 ◽  
Author(s):  
Jing Tang ◽  
Yunxia Wang ◽  
Yi Li ◽  
Yang Zhang ◽  
Runyuan Zhang ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Information Sources ◽  
Protein Quantification ◽  
Protein Profiling ◽  
Label Free ◽  
Dynamic Information ◽  
Data Repositories ◽  
Research Directions ◽  
Technological Advances ◽  
Recent Trends

Nanoscience becomes one of the most cutting-edge research directions in recent years since it is gradually matured from basic to applied science. Nanoparticles (NPs) and nanomaterials (NMs) play important roles in various aspects of biomedicine science, and their influences on the environment have caused a whole range of uncertainties which require extensive attention. Due to the quantitative and dynamic information provided for human proteome, mass spectrometry (MS)-based quantitative proteomic technique has been a powerful tool for nanomedicine study. In this article, recent trends of progress and development in the nanomedicine of proteomics were discussed from quantification techniques and publicly available resources or tools. First, a variety of popular protein quantification techniques including labeling and label-free strategies applied to nanomedicine studies are overviewed and systematically discussed. Then, numerous protein profiling tools for data processing and postbiological statistical analysis and publicly available data repositories for providing enrichment MS raw data information sources are also discussed.

scholarly journals Electrochemical detection of different p53 conformations by using nanostructured surfaces

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Sarah Tonello ◽  
Francesca Stradolini ◽  
Giulia Abate ◽  
Daniela Uberti ◽  
Mauro Serpelloni ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
Limit Of Detection ◽  
Direct Electrochemistry ◽  
Protein Quantification ◽  
Label Free ◽  
Limited Information ◽  
Clinical Practices ◽  
Nanostructured Surfaces ◽  
Integrated Devices ◽  
Biochemical Assays

AbstractProtein electrochemistry represents a powerful technique for investigating the function and structure of proteins. Currently available biochemical assays provide limited information related to the conformational state of proteins and high costs. This work provides novel insights into the electrochemical investigation of the metalloprotein p53 and its redox products using label-free direct electrochemistry and label-based antibody-specific approaches. First, the redox activities of different p53 redox products were qualitatively investigated on carbon-based electrodes. Then, focusing on the open p53 isoform (denatured p53), a quantitative analysis was performed, comparing the performances of different bulk and nanostructured materials (carbon and platinum). Overall, four different p53 products could be successfully discriminated, from wild type to denatured. Label-free analysis suggested a single electron exchange with electron transfer rate constants on the order of 1 s−1. Label-based analysis showed decreasing affinity of pAb240 towards denatured, oxidized and nitrated p53. Furthermore, platinum nanostructured electrodes showed the highest enhancement of the limit of detection in the quantitative analysis (100 ng/ml). Overall, the obtained results represent a first step towards the implementation of highly requested complex integrated devices for clinical practices, with the aim to go beyond simple protein quantification.

scholarly journals Botulinum toxin A for trismus in cephalic tetanus

1994 ◽  
Vol 52 (3) ◽  
pp. 410-413 ◽  
Author(s):  
Luiz Augusto F. Andrade ◽  
Sonia Maria D. Brucki
Keyword(s):  
Botulinum Toxin ◽  
Botulinum Toxin A ◽  
Pulmonary Complications ◽  
Toxin A ◽  
Clostridium Tetani ◽  
Considerable Difficulty ◽  
Respiratory Problems ◽  
Life Threatening ◽  
The Difference ◽  
Cephalic Tetanus

Cephalic tetanus is a localized form of tetanus. As in generalized forms , trismus is a prominent feature of the disease, leading to considerable difficulty in feeding, swallowing of the saliva and mouth hygiene. These difficulties often precede respiratory problems and aspiration bronchopneumonia is a frequent life-threatening complication. Muscle relaxants other than curare drugs may show a limited benefit for relieving trismus. Tetanospasmin, the tetanic neurotoxin, and botulinum toxin share many similarities, having a closely related chemical structure, an origin from related microorganisms (Clostridium tetani and Clostridium botulinum, respectively), and presumably, the same mechanisms of action in the neuron. The difference between the two lies in their peculiar neurospecificity, acting in different neurons. Injection of minute doses of botulinum toxin in the muscles involved in focal dystonias or other localized spastic disorders have proved to be very effective in these conditions. We describe the use of botulinum toxin A in the successful treatment of trismus in a patient suffering from cephalic tetanus. We believe that this form of treatment may be of value in lowering the risk of pulmonary complications in tetanic patients.

scholarly journals Statistical protein quantification and significance analysis in label-free LC-MS experiments with complex designs

2012 ◽  
Vol 13 (Suppl 16) ◽  
pp. S6 ◽  
Author(s):  
Timothy Clough ◽  
Safia Thaminy ◽  
Susanne Ragg ◽  
Ruedi Aebersold ◽  
Olga Vitek
Keyword(s):  
Protein Quantification ◽  
Label Free ◽  
Significance Analysis

scholarly journals Genetics Meets Proteomics: Correlating the Portuguese Water Dog Blood Serum Proteome with Genetic Markers

2011 ◽  
Vol 4 ◽  
pp. PRI.S6470
Author(s):  
Sandra Sénéchal ◽  
Martin Kussmann
Keyword(s):  
Blood Serum ◽  
Biomarker Discovery ◽  
Protein Quantification ◽  
Label Free ◽  
Blood Profile ◽  
Serum Proteome ◽  
Genetic Level ◽  
Portuguese Water ◽  
Dog Blood ◽  
Genetically Determined

Blood serum is a body fluid widely used for biomarker discovery and therefore numerous studies aim at defining its proteome. The serum proteome is subject to fluctuations resulting from biological variability (eg, diurnal variations) reflecting both healthy and/or disease-related conditions. Inter-individual differences originate partly at the genetic level and may influence clinical blood profile including the serum proteome. Therefore we investigated whether serum protein abundance is genetically determined: we report the study of a cohort of 146 Portuguese Water Dogs, a dog breed whose genetic background has been well characterized. We generated protein profiles of dog sera on 1D-gels and correlated them with microsatellite markers. We detected correlations between 7 gel bands and 11 genetic regions and developed a label-free protein quantification method to identify and quantify the proteins most accountable for serum proteome variation. An association between the abundance of RBP4 in dog serum and the adiponectin gene was detected.

scholarly journals Label-free single-cell protein quantification using a drop-based mix-and-read system

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Alireza Abbaspourrad ◽  
Huidan Zhang ◽  
Ye Tao ◽  
Naiwen Cui ◽  
Haruichi Asahara ◽  
...  
Keyword(s):  
Single Cell ◽  
Single Cell Protein ◽  
Protein Quantification ◽  
Cell Protein ◽  
Label Free
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