The rise of intact protein analysis by mass spectrometry (MS) was accompanied by an increasing need for flexible tools allowing data visualization and analysis. These include inspection of the deconvoluted molecular weights of the proteoforms eluted alongside liquid chromatography (LC) through their representation in three-dimensional (3D) liquid chromatography coupled to mass spectrometry (LC-MS) maps (plots of deconvoluted molecular weights, retention times, and intensity of the MS signal). With this aim, we developed a free and open-source web application named VisioProt-MS (https://masstools.ipbs.fr/mstools/visioprot-ms/). VisioProt-MS is highly compatible with many algorithms and software developed by the community to integrate and deconvolute top-down and intact protein MS data. Its dynamic and user-friendly features greatly facilitate analysis through several graphical representations dedicated to MS and tandem mass spectrometry (MS/MS) analysis of proteoforms in complex samples. Here, we will illustrate the importance of LC-MS map visualization to optimize top-down acquisition/search parameters and analyze intact protein MS data. We will go through the main features of VisioProt-MS using the human proteasomal 20S core particle as a user-case.
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http://dx.doi.org/10.1177/1177932219868223 | DOI Listing |
Proc Natl Acad Sci U S A
January 2025
Department of Microbiology, Immunology and Cancer Biology, University of Virginia, Charlottesville, VA 22908.
Although viruses subvert innate immune pathways for their replication, there is evidence they can also co-opt antiviral responses for their benefit. The ubiquitous human pathogen, Herpes simplex virus-1 (HSV-1), encodes a protein (UL12.5) that induces the release of mitochondrial nucleic acid into the cytosol, which activates immune-sensing pathways and reduces productive replication in nonneuronal cells.
View Article and Find Full Text PDFTransl Vis Sci Technol
January 2025
UCL Institute of Ophthalmology, University College London, London, UK.
Purpose: A human model able to simulate the manifestation of corneal endothelium decompensation could be advantageous for wound healing and future cell therapy assessment. The study aimed to establish an ex vivo human cornea endothelium wound model where endothelium function can be evaluated by measuring corneal thickness changes.
Methods: The human cornea was maintained in an artificial anterior chamber, with a continuous culture medium infusion system designed to sustain corneal endothelium and epithelium simultaneously.
Adv Wound Care (New Rochelle)
January 2025
Kenatha Scientific Consulting LLC, Fort Worth, Texas, USA.
SN514 is a thermolysin-like enzyme under development as a debrider. Preclinical and non-clinical studies supported a first in human healthy volunteer study to predict the need for protection of periwound skin. Pharmacologic activity testing compared digestion of collagen, fibrin, and elastin with relevant enzymes.
View Article and Find Full Text PDFVet Sci
January 2025
Graduate Program in Animal Science and Health, Federal University of Campina Grande, Patos 58708110, Brazil.
The use of escape protein, which is absorbed in the small intestine, can improve the production of ruminant animals because it meets their protein requirements better. This study hypothesized that wax lipid matrices are effective encapsulants for escape lysine in ruminants and tested tannin extract as an adjuvant. Forty intact male Santa Ines × Dorper sheep (~4 months old, BW 23 ± 1.
View Article and Find Full Text PDFCells
January 2025
Key Laboratory of Resource Biology and Biotechnology Western China, Ministry of Education, Provincial Key Laboratory of Biotechnology, College of Life Sciences, Northwest University, Xi'an 710069, China.
Glycosylation plays a critical role in various biological processes, yet identifying specific glycosyltransferase substrates remains a challenge due to the complexity of glycosylation. Here, we employ proximity labeling with biotin ligases BASU and TurboID to map the proximitome of MGAT3, a glycosyltransferase responsible for the biosynthesis of the bisecting GlcNAc structure, in HEK293T cells. This approach enriched 116 and 189 proteins, respectively, identifying 17 common substrates shared with bisecting GlcNAc-bearing proteome obtained via intact glycopeptide enrichment methods.
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