Related Experiment Video
Updated: Mar 27, 2026

07:35
Laser Microdissection-Based Protocol for the LC-MS/MS Analysis of the Proteomic Profile of Neuromelanin Granules
Published on: December 16, 2021
2.9K
A proteomic characterization of NTHi lysates
Diego Preciado1, Marian Poley2, Stephanie Tsai3
1Sheihk Zayed Institute, Washington, DC, United States; Division of Pediatric Otolaryngology-Head and Neck Surgery, Washington, DC, United States.
International Journal of Pediatric Otorhinolaryngology
|January 10, 2016
Summary
This study characterized non-typeable Haemophilus influenzae (NTHi) bacterial lysates using proteomics. Despite protein variability, all NTHi lysate batches effectively activated NF-kB inflammatory pathways, crucial for understanding respiratory infections.
Area of Science:
- Microbiology
- Proteomics
- Immunology
Background:
- Non-typeable Haemophilus influenzae (NTHi) causes common respiratory infections.
- NTHi lysates are used to study inflammatory responses in epithelial cells.
- Understanding NTHi lysate composition is vital for accurate biological effect studies.
Purpose of the Study:
- To identify abundant proteins in NTHi lysates using unbiased proteomics.
- To assess protein content variability across different NTHi lysate batches.
- To correlate NTHi lysate composition with biological inflammatory effects.
Main Methods:
- Proteomic analysis of NTHi lysates via liquid chromatography tandem mass spectrometry (LC-MS/MS).
- Western blot analysis for outer membrane protein 6 (OMP6) validation.
- Luciferase assays to measure NF-kB activation.
Main Results:
- Identified 793 unique NTHi proteins, including those involved in biofilm formation and immune evasion.
- Confirmed presence of OMP6 in all lysate preparations.
- Demonstrated consistent NF-kB promoter response activation across all NTHi lysate batches.
Conclusions:
- Proteomics successfully characterized NTHi lysate protein content.
- This is the first proteomic report of commonly used NTHi lysates.
- NTHi lysates induce similar NF-kB activation despite batch-to-batch protein variability.

