IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Allen, M. J.
Right arrow Articles by Mason, R. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Allen, M. J.
Right arrow Articles by Mason, R. J.

 Previous Article  |  Next Article 

Infection and Immunity, April 2001, p. 2037-2044, Vol. 69, No. 4
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.4.2037-2044.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Interactions of Surfactant Proteins A and D with Saccharomyces cerevisiae and Aspergillus fumigatus

Martin J. Allen,1 Dennis R. Voelker,1,2,3 and Robert J. Mason1,3,*

Department of Medicine, National Jewish Medical and Research Center, Denver, Colorado 80206,1 and Departments of Biochemistry and Molecular Genetics2 and Medicine,3 University of Colorado Health Sciences Center, Denver, Colorado 80262

Received 10 October 2000/Returned for modification 21 November 2000/Accepted 28 December 2000

Surfactant proteins A (SP-A) and D (SP-D) are members of the collectin family of calcium-dependent lectins and are important pulmonary host defense molecules. Human SP-A and SP-D and rat SP-D bind to Aspergillus fumigatus conidia, but the ligand remains unidentified. To identify a fungal ligand for SP-A and/or SP-D, we examined the interactions of the proteins with Saccharomyces cerevisiae. SP-D but not SP-A bound yeast cells, and EDTA inhibited the binding. SP-D also aggregated yeast cells and isolated yeast cell walls. Treating yeast cells to remove cell wall mannoprotein did not reduce SP-D binding, and SP-D failed to aggregate chitin. However, SP-D aggregated yeast glucan before and after treatment with a beta (1right-arrow3)-glucanase, suggesting a specific interaction between the collectin and beta (1right-arrow6)-glucan. In support of this idea, SP-D-induced yeast aggregation was strongly inhibited by pustulan [a beta (1right-arrow6)-linked glucose homopolymer] but was not inhibited by laminarin [a beta (1right-arrow3)-linked glucose homopolymer]. Additionally, pustulan but not laminarin strongly inhibited SP-D binding to A. fumigatus. The pustulan concentration for 50% inhibition of SP-D binding to A. fumigatus is 1.0 ± 0.3 µM glucose equivalents. Finally, SP-D showed reduced binding to the beta (1right-arrow6)-glucan-deficient kre6 yeast mutant. Taken together, these observations demonstrate that beta (1right-arrow6)-glucan is an important fungal ligand for SP-D and that glycosidic bond patterns alone can determine if an extended carbohydrate polymer is recognized by SP-D.

* Corresponding author. Mailing address: Department of Medicine, National Jewish Medical and Research Center, 1400 Jackson St., Denver, CO 80206. Phone: (303) 398-1302. Fax: (303) 398-1806. E-mail: masonb{at}njc.org.

Infection and Immunity, April 2001, p. 2037-2044, Vol. 69, No. 4
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.4.2037-2044.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2001 by the American Society for Microbiology. All rights reserved.