Related Experiment Video
Updated: Jun 18, 2026
From a 2DE-Gel Spot to Protein Function: Lesson Learned From HS1 in Chronic Lymphocytic Leukemia
Published on: October 19, 2014
Data Independent Acquisition Reveals In-Depth Serum Proteome Changes in Canine Leishmaniosis
Franjo Martinković1, Marin Popović2, Ozren Smolec1
1Faculty of Veterinary Medicine, University of Zagreb, Heinzelova 55, HR-10000 Zagreb, Croatia.
Insights
Data-independent acquisition mass spectrometry (DIA-MS) enabled deep serum proteomic profiling in dogs with leishmaniosis. This approach identified key proteins involved in lipid metabolism, immune response, and oxidative stress, aiding biomarker discovery.
Area of Science:
- Proteomics
- Biomarker Discovery
- Veterinary Medicine
Background:
- Serum proteome profiling is crucial for understanding health and disease, but high protein dynamic range limits comprehensive analysis.
- Existing enrichment methods can introduce bias and reduce proteome-wide information.
- Canine leishmaniosis presents a complex host response that requires advanced proteomic strategies for elucidation.
Purpose of the Study:
- To apply next-generation proteomics for deep serum profiling in canine leishmaniosis.
- To identify differentially abundant proteins and understand the host response.
- To evaluate data-independent acquisition mass spectrometry (DIA-MS) for serum biomarker development.
Main Methods:
- Utilized label-free sequential window acquisition of all theoretical mass spectra (SWATH-MS), a type of DIA-MS.
- Analyzed non-depleted serum samples from healthy and *Leishmania*-infected dogs.
- Employed a 60-min gradient for deep proteomic profiling.
Main Results:
- Identified a total of 554 proteins in the serum samples.
- Found 140 proteins with significantly different abundance between healthy and infected dogs.
- Detected proteins associated with lipid metabolism, hematological abnormalities, immune response, and oxidative stress.
Conclusions:
- DIA-MS provides high-quality, proteome-wide information from non-depleted serum.
- The identified proteins offer insights into the molecular basis of canine leishmaniosis.
- DIA-MS is a powerful method for serum biomarker discovery and understanding complex pathophysiological processes.
Abstract:
Comprehensive profiling of serum proteome provides valuable clues of health status and pathophysiological processes, making it the main strategy in biomarker discovery. However, the high dynamic range significantly decreases the number of detectable proteins, obstructing the insights into the underlying biological processes. To circumvent various serum enrichment methods, obtain high-quality proteome wide information using the next-generation proteomic, and study host response in canine leishmaniosis, we applied data-independent acquisition mass spectrometry (DIA-MS) for deep proteomic profiling of clinical samples. The non-depleted serum samples of healthy and naturally Leishmania-infected dogs were analyzed using the label-free 60-min gradient sequential window acquisition of all theoretical mass spectra (SWATH-MS) method. As a result, we identified 554 proteins, 140 of which differed significantly in abundance. Those were included in lipid metabolism, hematological abnormalities, immune response, and oxidative stress, providing valuable information about the complex molecular basis of the clinical and pathological landscape in canine leishmaniosis. Our results show that DIA-MS is a method of choice for understanding complex pathophysiological processes in serum and serum biomarker development.
