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1 Department of Anatomy and Cell Biology, University of Iowa College of Medicine, Iowa City, Iowa, USA
* To whom correspondence should be addressed. E-mail: jeanne-snyder{at}uiowa.edu.
Surfactant protein A is a member of the collectin family of proteins and plays a role in innate host defense of the lung. SP-A binds to the carbohydrates of lung pathogens via its calcium-dependant carbohydrate-binding domain. Native human alveolar SP-A consists of two distinct gene products: SP-A1 and SP-A2, however only SP-A2 is expressed in the submucosal glands of the conducting airways. The function of the isolated SP-A2 protein is unknown. We hypothesize that SP-A1 and SP-A2 might have different carbohydrate-binding properties. In this study, we characterized the carbohydrate binding specificities of native human alveolar SP-A and recombinant human SP-A1 and SP-A2 in the presence of either 1 mM or 5 mM Ca2+. We found that all of the SP-A proteins bind carbohydrates but with different affinities. All of the SP-A proteins bind to fucose with the greatest affinity. SP-A2 binds with a higher affinity to a wider variety of sugars than SP-A1 at either 1 mM or 5 mM Ca2+. These findings are suggestive that SP-A2 may interact with a greater variety of pathogens than native SP-A.
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