Document Detail


Surfactant protein D increases phagocytosis of hypocapsular Cryptococcus neoformans by murine macrophages and enhances fungal survival.
MedLine Citation:
PMID:  19451250     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cryptococcus neoformans is a facultative intracellular opportunistic pathogen and the leading cause of fungal meningitis in humans. In the absence of a protective cellular immune response, the inhalation of C. neoformans cells or spores results in pulmonary infection. C. neoformans cells produce a polysaccharide capsule composed predominantly of glucuronoxylomannan, which constitutes approximately 90% of the capsular material. In the lungs, surfactant protein A (SP-A) and SP-D contribute to immune defense by facilitating the aggregation, uptake, and killing of many microorganisms by phagocytic cells. We hypothesized that SP-D plays a role in C. neoformans pathogenesis by binding to and enhancing the phagocytosis of the yeast. Here, the abilities of SP-D to bind to and facilitate the phagocytosis and survival of the wild-type encapsulated strain H99 and the cap59Delta mutant hypocapsular strain are assessed. SP-D binding to cap59Delta mutant cells was approximately sixfold greater than binding to wild-type cells. SP-D enhanced the phagocytosis of cap59Delta cells by approximately fourfold in vitro. To investigate SP-D binding in vivo, SP-D(-/-) mice were intranasally inoculated with Alexa Fluor 488-labeled cap59Delta or H99 cells. By confocal microscopy, a greater number of phagocytosed C. neoformans cells in wild-type mice than in SP-D(-/-) mice was observed, consistent with in vitro data. Interestingly, SP-D protected C. neoformans cells against macrophage-mediated defense mechanisms in vitro, as demonstrated by an analysis of fungal viability using a CFU assay. These findings provide evidence that C. neoformans subverts host defense mechanisms involving surfactant, establishing a novel virulence paradigm that may be targeted for therapy.
Authors:
Scarlett Geunes-Boyer; Timothy N Oliver; Guilhem Janbon; Jennifer K Lodge; Joseph Heitman; John R Perfect; Jo Rae Wright
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2009-05-18
Journal Detail:
Title:  Infection and immunity     Volume:  77     ISSN:  1098-5522     ISO Abbreviation:  Infect. Immun.     Publication Date:  2009 Jul 
Date Detail:
Created Date:  2009-06-22     Completed Date:  2009-07-14     Revised Date:  2011-02-11    
Medline Journal Info:
Nlm Unique ID:  0246127     Medline TA:  Infect Immun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2783-94     Citation Subset:  IM    
Affiliation:
Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Line
Colony Count, Microbial
Cryptococcus neoformans / immunology*
Macrophages / microbiology*
Mice
Mice, Inbred C57BL
Mice, Knockout
Microbial Viability*
Phagocytosis*
Protein Binding
Pulmonary Surfactant-Associated Protein D / deficiency,  immunology*,  metabolism
Grant Support
ID/Acronym/Agency:
AI28388/AI/NIAID NIH HHS; AI42159/AI/NIAID NIH HHS; AI50184/AI/NIAID NIH HHS; AI73896/AI/NIAID NIH HHS; HL-30923/HL/NHLBI NIH HHS; HL-51134/HL/NHLBI NIH HHS; R01 HL030923-27/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Pulmonary Surfactant-Associated Protein D
Comments/Corrections

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