Enzymatically active eosinophil peroxidase associates with CD177 and alters oxidative activity in a subset of neutrophils
Abstract
CD177 is a membrane protein present on some, but not all, circulating neutrophils in a given individual, dividing the total neutrophil population into two distinct subsets. We investigated proteomic differences between CD177pos and CD177neg neutrophils from healthy human subjects. Neutrophils were isolated from peripheral blood, followed by magnetic separation based on the surface expression of CD177. We performed tandem mass tag (TMT) using mass-spectrometry-based comparative proteomic analysis on ≥95% pure subpopulations, enabling reliable quantification of more than 3,400 proteins. Most proteins were similarly expressed in both neutrophil subsets, confirming a strong shared neutrophil identity. However, certain canonical eosinophil proteins, including eosinophil peroxidase (EPX), major basic protein (MBP), and MBP2 (PRG3), were upregulated in CD177pos cells. Lysates of CD177pos neutrophils showed higher peroxidase activity than CD177neg neutrophils under conditions favoring EPX over myeloperoxidase, consistent with enzymatically active EPX, and flow cytometry showed surface localization of EPX on CD177pos cells. Co-immunoprecipitation indicated that EPX associates with CD177. Our findings suggest that CD177pos neutrophils exhibit a unique proteomic signature enriched in eosinophil-related proteins, and that EPX associated with CD177 may provide a neutrophil subset with altered enzymatic activity.
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BibTeX
@article{popovic2026enzymatically,
title = {{Enzymatically active eosinophil peroxidase associates with CD177 and alters oxidative activity in a subset of neutrophils}},
author = {Jordan Popović and Agnes Dahlstrand Rudin and Alan Bäckerholm and Vignesh Venkatakrishnan and Karin Christenson and Johan Bylund},
journal = {Frontiers in Immunology},
year = {2026},
month = nov,
doi = {10.3389/fimmu.2026.1985429},
url = {https://www.frontiersin.org/articles/10.3389/fimmu.2026.1985429},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Enzymatically active eosinophil peroxidase associates with CD177 and alters oxidative activity in a subset of neutrophils
AU - Jordan Popović
AU - Agnes Dahlstrand Rudin
AU - Alan Bäckerholm
AU - Vignesh Venkatakrishnan
AU - Karin Christenson
AU - Johan Bylund
PY - 2026
DA - 2026/11/02
JO - Frontiers in Immunology
DO - 10.3389/fimmu.2026.1985429
UR - https://www.frontiersin.org/articles/10.3389/fimmu.2026.1985429
AB - CD177 is a membrane protein present on some, but not all, circulating neutrophils in a given individual, dividing the total neutrophil population into two distinct subsets. We investigated proteomic differences between CD177pos and CD177neg neutrophils from healthy human subjects. Neutrophils were isolated from peripheral blood, followed by magnetic separation based on the surface expression of CD177. We performed tandem mass tag (TMT) using mass-spectrometry-based comparative proteomic analysis on ≥95% pure subpopulations, enabling reliable quantification of more than 3,400 proteins. Most proteins were similarly expressed in both neutrophil subsets, confirming a strong shared neutrophil identity. However, certain canonical eosinophil proteins, including eosinophil peroxidase (EPX), major basic protein (MBP), and MBP2 (PRG3), were upregulated in CD177pos cells. Lysates of CD177pos neutrophils showed higher peroxidase activity than CD177neg neutrophils under conditions favoring EPX over myeloperoxidase, consistent with enzymatically active EPX, and flow cytometry showed surface localization of EPX on CD177pos cells. Co-immunoprecipitation indicated that EPX associates with CD177. Our findings suggest that CD177pos neutrophils exhibit a unique proteomic signature enriched in eosinophil-related proteins, and that EPX associated with CD177 may provide a neutrophil subset with altered enzymatic activity.
SN - 1664-3224
ER -