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Am J Physiol Lung Cell Mol Physiol 274: L958-L969, 1998;
1040-0605/98 $5.00
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Vol. 274, Issue 6, L958-L969, June 1998

Pulmonary surfactant proteins A and D enhance neutrophil uptake of bacteria

Kevan L. Hartshorn1, Erika Crouch2, Mitchell R. White1, Maria L. Colamussi1, Anand Kakkanatt1, Benjamin Tauber1, Virginia Shepherd3, and Kedarnath N. Sastry1

1 Department of Medicine, Boston University School of Medicine, Boston, Massachusetts 02118; 3 Department of Biochemisty, Vanderbilt University School of Medicine, Nashville, Tennessee 37203; and 2 Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110

The collectins are a class of collagenous lectin proteins present in serum and pulmonary secretions [pulmonary surfactant protein (SP) A and SP-D] that are believed to participate in innate immune responses to various pathogens. With the use of flow cytometric and fluorescent-microscopic assays, SP-A and SP-D were shown to increase calcium-dependent neutrophil uptake of Escherichia coli, Streptococcus pneumoniae, and Staphylococcus aureus. Evidence is provided that the collectins enhanced bacterial uptake through a mechanism that involved both bacterial aggregation and direct actions on neutrophils. The degree of multimerization of SP-D preparations was a critical determinant of both aggregating activity and potency in enhancing bacterial uptake. The mechanisms of opsonizing activity of SP-D and SP-A differed in important respects from those of opsonizing antibodies. These results provide the first evidence that surfactant collectins may promote neutrophil-mediated clearance of bacteria in the lung independently of opsonizing antibody.

Escherichia coli; Streptococcus pneumoniae; opsonization; collectins; antibodies


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