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Related Experiment Video

Updated: Sep 20, 2025

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
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Malondialdehyde Acetaldehyde-Adduction Changes Surfactant Protein D Structure and Function.

Claire G Nissen1, Deanna D Mosley2, Kusum K Kharbanda2,3

  • 1Department of Environmental, Agricultural and Occupational Health, College of Public Health, University of Nebraska Medical Center, Omaha, NE, United States.

Frontiers in Immunology
|June 7, 2022
PubMed
Summary

Alcohol and smoking damage lung surfactant protein D (SPD), altering its structure and impairing its ability to fight bacterial infections and repair lung injury. This may explain increased pneumonia risk in alcohol use disorders.

Keywords:
adductionalcoholaldehydeslungpneumoniasurfactant

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Area of Science:

  • Pulmonary immunology
  • Environmental toxicology
  • Innate immunity

Background:

  • Lung surfactant protein D (SPD) is crucial for innate immunity, mediating bacterial clearance and macrophage function.
  • Alcohol and cigarette smoke generate malondialdehyde acetaldehyde (MAA), which adducts proteins, including SPD.
  • MAA-adducted SPD (SPD-MAA) negatively impacts lung cilia, macrophages, and epithelial repair.

Purpose of the Study:

  • To investigate how MAA-adduction affects the structure and function of SPD.
  • To determine if MAA-induced structural changes in SPD alter its anti-microbial and protective capabilities.

Main Methods:

  • Purified human SPD and SPD-MAA were analyzed using gel filtration (Sephadex G-200) to resolve different quaternary structures.
  • Protein concentration, MAA-adduction, and binding to GFP-labeled *Streptococcus pneumoniae* (GFP-SP) were quantified.
  • Assays included bacterial aggregation, macrophage phagocytosis, bacterial permeability, and viral-induced epithelial cell injury.

Main Results:

  • SPD exists as monomeric, trimeric, and multimeric forms, with multimers being most prevalent.
  • MAA-adduction shifted SPD structure towards monomer and trimer forms, significantly reducing bacterial binding and aggregation.
  • SPD-MAA failed to enhance macrophage phagocytosis, increase bacterial permeability, or protect epithelial cells from viral injury.

Conclusions:

  • MAA-adduction alters SPD's quaternary structure from multimers to monomers/trimers, diminishing its anti-microbial functions.
  • These structural and functional deficits of SPD-MAA contribute to impaired innate immunity.
  • This provides a potential mechanism for the increased incidence of pneumonia in individuals with alcohol use disorders.