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Am. J. Respir. Cell Mol. Biol., Volume 23, Number 1, July, 2000 71-78

Surfactant Protein A Binding to Cytomegalovirus Proteins Enhances Virus Entry into Rat Lung Cells

Christiane Weyer, Robert Sabat, Heide Wissel, Detlev H. Krüger, Paul A. Stevens, and Susanna Prösch

Departments of Virology, Medical Immunology, and Neonatology, Humboldt University, Medical School (Charité), Berlin, Germany

The role of surfactant protein (SP)-A in cytomegalovirus (CMV) infection of the lung was investigated. We found that SP-A binds to various immobilized human CMV proteins and those exposed on the surface of infected embryonal lung fibroblasts. The interaction between SP-A and immobilized CMV proteins was found to be calcium-dependent and inhibited by mannan, suggesting involvement of the carbohydrate recognition domain of SP-A and high-mannose carbohydrate residues of viral envelope glycoproteins. Using flow cytometry and confocal laser fluorescence microscopy in the rat model we showed that preincubation of rat CMV with SP-A stimulates its binding and internalization by rat type II pneumocytes and alveolar tissue macrophages. This effect was concentration- and Ca2+-dependent but was not inhibited by mannan. Therefore, the domains of SP-A involved in SP-A CMV interaction and in interaction of the SP-A/virus complex with rat lung cells are distinct. Additionally, in the human CMV model, sheep as well as human proteinosis SP-A did not significantly affect human CMV replication in embryonal lung fibroblasts. Thus, SP-A may contribute to CMV-associated pathology of the lung by increasing the efficiency of target cell infection.




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Proc. Am. Thorac. Soc. Am. J. Respir. Crit. Care Med.
Copyright © 2000 American Thoracic Society.