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Surfactant Protein A Inhibits Human Rhinovirus C Binding and Infection of Airway Epithelial Cells from Pediatric

Sasipa Tanyaratsrisakul1,2, Yury A Bochkov3, Vanessa White1

  • 1Department of Medicine, National Jewish Health, Denver, CO 80206, USA.

Viruses
|November 27, 2024
PubMed

Insights

Surfactant protein A (SP-A) effectively inhibits Rhinovirus C (RV-C) infection in nasal cells, reducing viral load and potentially preventing asthma exacerbations. This antiviral action stems from SP-A binding to RV-C, blocking its entry into cells.

Area of Science:

  • Pulmonary immunology
  • Virology
  • Innate immunity

Background:

  • Rhinovirus C (RV-C) infections are a major trigger for asthma exacerbations in children and adults.
  • Surfactant protein A (SP-A) is crucial for pulmonary innate immunity, interacting with various respiratory pathogens.
  • SP-A exists as isoforms (SP-A1 and SP-A2) that form hetero-oligomers.

Purpose of the Study:

  • To evaluate the efficacy of SP-A in antagonizing RV-C infection in pediatric nasal epithelial cells (NECs).
  • To elucidate the antiviral mechanism of SP-A against RV-C infection.
  • To compare the binding affinities of native SP-A, recombinant SP-A1, and SP-A2 variants to RV-C.

Main Methods:

  • Utilized wild-type (RV-C15) and reporter-expressing (RV-C15-GFP) viruses in differentiated NECs from asthmatic and non-asthmatic children.
  • Purified native SP-A from alveolar proteinosis patients and expressed recombinant SP-A1 and SP-A2 variants.
  • Assessed viral load reduction using fluorescent focus-forming units (FFUs) and viral RNA quantification.
  • Investigated SP-A binding to RV-C and its effect on viral attachment to NECs.

Main Results:

  • SP-A significantly reduced RV-C15-GFP FFUs by 99% and viral RNA load by 97%.
  • SP-A inhibited RV-C propagation, preventing the induction of antiviral genes and chemokines.
  • Native SP-A and recombinant SP-A2 variants demonstrated strong binding to RV-C in a dose- and calcium-dependent manner, inhibiting viral attachment to NECs.

Conclusions:

  • SP-A exhibits potent antiviral activity against RV-C infection in human nasal epithelial cells.
  • SP-A's mechanism involves direct binding to RV-C, preventing viral entry and subsequent replication.
  • SP-A, particularly SP-A2 variants, shows promise as a potential antiviral therapeutic for RV infections and associated asthma exacerbations.

Keywords:
human rhinovirus Cinnate immunitypediatric asthmapulmonary surfactant protein A

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