Am. J. Respir. Cell Mol. Biol., Volume 20, Number 2, February, 1999 279-286

Surfactant Protein-A Binds Group B Streptococcus Enhancing Phagocytosis and Clearance from Lungs of Surfactant Protein-A-Deficient Mice

Ann Marie LeVine, Kim E. Kurak, Jo Rae Wright, Wendy T. Watford, Michael D. Bruno, Gary F. Ross, Jeffrey A. Whitsett, and Thomas R. Korfhagen

Children's Hospital Medical Center, Division of Pulmonary Biology, Cincinnati, Ohio; and Department of Cell Biology, Duke University Medical Center, Durham, North Carolina

Surfactant protein-A (SP-A) gene-targeted mice clear group B streptococcus (GBS) from the lungs at a slower rate than wild-type mice. To determine mechanisms by which SP-A enhances pulmonary clearance of GBS, the role of SP-A in binding and phagocytosis of GBS was assessed in SP-A (/) mice infected with GBS in the presence and absence of exogenous SP-A. Coadministration of GBS with exogenous SP-A decreased GBS colony counts in lung homogenates of SP-A (/) mice. SP-A bound to GBS in a calcium-dependent manner. Although pulmonary infiltration with macrophages was not altered in SP-A (/) versus wild-type mice after GBS infection, the number of alveolar macrophages with phagocytosed bacteria was lower in the SP-A (/) mice than in the wild-type mice. When SP-A was coadministered with GBS, phagocytosis was significantly increased. Oxygen radical production by alveolar macrophages from SP-A (/) mice infected with GBS was decreased compared with wild-type controls and was increased when SP-A (/) mice were infected in the presence of exogenous SP-A. Superoxide (SO) radical generation was deficient in macrophages from SP-A (/) mice. SP-A plays an important role in GBS clearance in vivo, mediated in part by binding to and enhancing GBS phagocytosis and by increasing SO production by alveolar macrophages.

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