Proteomics

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Structural Diversity of Lipid A Modulates Neutrophil Proteome and Secretome Responses

ABSTRACT: We applied quantitative high-resolution proteomics to systematically evaluate how the human PMN proteome is shaped in response to two LPS preparations that differ primarily in the number of acyl chains associated with their lipid A (E. coli and F. tularensis LPS). To capture both stimulus-specific effects and response kinetics, PMNs were analyzed at multiple time points, allowing assessment of treatment-dependent differences and proteomic changes over time within each condition. We characterized the PMN secretome following exposure to these agents, enabling the comparison of process between intracellular proteomic and protein release. Together, this integrated cellular proteome and secretome approach provides a comprehensive framework to define how structurally distinct LPS molecules modulate PMN functional programs over time. While PMN responses to LPS have been extensively investigated, their temporal proteomic and secretory landscapes in primary human PMNs, particularly in response to LPS with divergent lipid A architectures, remain incompletely characterized.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Primary Cell

SUBMITTER: Aleksandra Nita-Lazar  

LAB HEAD: Aleksandra Nita-Lazar

PROVIDER: PXD072780 | Pride | 2026-04-27

REPOSITORIES: Pride

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Structural diversity of lipid A modulates neutrophil proteome and secretome responses.

Pittaluga Villarreal Jose R JR   Kim Doeun D   Yoon Sung Hwan SH   Bhushan Vanya V   Issara-Amphorn Jiraphorn J   Pederson Jacob J   Manes Nathan P NP   Nita-Lazar Aleksandra A  

Journal of proteomics 20260310

Neutrophils (PMNs) are central effector cells of the innate immune system, deploying antimicrobial functions such as degranulation, ROS production, and release of antimicrobial mediators. However, the neutrophil reprogramming in response to structurally distinct lipopolysaccharide (LPS) stimuli remains incompletely defined. Here, we integrated functional profiling with quantitative high-resolution proteomics to compare human PMN responses to two LPS preparations differing primarily in lipid A ac  ...[more]

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