The role of surfactant-associated protein A in pulmonary host defense

Immunol Res. 2001;23(2-3):111-20. doi: 10.1385/IR:23:2-3:111.


Resident alveolar macrophages play a key role in the initial defense against inhaled pathogens. Surface molecules bind opsonized as well as nonopsonized microbes and mediate their internalization by the macrophage. The recent discovery that specific C-type lectins can bind to the surface of a wide range of pathogens has led to the hypothesis that these lectins are involved in the initial phases of microbe recognition by the macrophage. Studies in our laboratory focus on the role of the lung-specific lectin surfactant associated protein A (SP-A) in host defense against pulmonary pathogens. SP-A contains a carbohdyrate recognition domain that appears to bind specifically to exposed carbohydrate residues on the surface of microorganisms. This lectin-microorganism interaction leads to entry of specific pathogens into macrophages and activation of intracellular pathways, resulting in the production of antimicrobial mediators such as nitric oxide. Many studies, including those involving SP-A-deficient mice, underscore the importance of this protein in pulmonary innate immunity. However, the intramacrophage mechanisms underlying the effects of SP-A are still unclear. This article describes our current knowledge of SP-A and its interactions with immune cells and pathogens with a focus on recent findings from our laboratory regarding SP-A interactions with mycobacteria.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Animals
  • Bacterial Outer Membrane Proteins / metabolism
  • Bacterial Physiological Phenomena
  • Chemotaxis
  • Humans
  • Immunity, Innate
  • Inflammation Mediators / metabolism
  • Lectins / chemistry
  • Lectins / physiology
  • Lung / microbiology*
  • Macrophages, Alveolar / metabolism
  • Macrophages, Alveolar / physiology*
  • Membrane Glycoproteins / metabolism
  • Mice
  • Mycobacterium / physiology
  • Opsonin Proteins / physiology
  • Phagocytosis
  • Proteolipids / chemistry
  • Proteolipids / physiology*
  • Pulmonary Surfactant-Associated Protein A
  • Pulmonary Surfactant-Associated Proteins
  • Pulmonary Surfactants / chemistry
  • Pulmonary Surfactants / physiology*
  • Receptors, Cell Surface / metabolism
  • Signal Transduction


  • Bacterial Outer Membrane Proteins
  • Inflammation Mediators
  • Lectins
  • Membrane Glycoproteins
  • Opsonin Proteins
  • Proteolipids
  • Pulmonary Surfactant-Associated Protein A
  • Pulmonary Surfactant-Associated Proteins
  • Pulmonary Surfactants
  • Receptors, Cell Surface
  • surfactant protein A receptor