Surfactant proteins A and D protect mice against pulmonary hypersensitivity induced by Aspergillus fumigatus antigens and allergens

Madan, Taruna; Kishore, Uday; Singh, Mamta; Strong, Peter; Clark, Howard; Hussain, Ejaj M.; Reid, Kenneth B.M.; Sarma, P. Usha

doi:10.1172/jci10124

Cited by 180 publications

(183 citation statements)

References 30 publications

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“…Similar results were observed with both SP-A and SP-D in mouse models of allergy to Aspergillus fumigatus (17). The mechanisms by which SP-A and SP-D bring about these protective effects are not clearly defined but in vitro studies have shown that SP-A and SP-D bind to glycosylated Der p and A. fumigatus allergens through their CRDs in a calcium-dependent manner (18,19) with consequent inhibitory effects on allergeninduced histamine release (19,20), and furthermore, SP-A and SP-D have also been shown to inhibit allergen-induced T lymphocyte proliferation (20).…”

supporting

confidence: 85%

“…It is plausible that many of the protective, anti-allergic effects of collectins seen in vitro and in vivo are mediated through interactions with the allergens themselves (15)(16)(17)(18)(19). To determine whether the collectins could bind to the allergens within the lung environment, solid phase binding assays were performed in BALF, which contains lipids and competitor proteins that would normally be present in the lung environment.…”

Section: Discussionmentioning

confidence: 99%

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Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

Deb

Shakib

Reid

et al. 2007

Journal of Biological Chemistry

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supporting

confidence: 85%

Section: Discussionmentioning

confidence: 99%

Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

Deb

Shakib

Reid

et al. 2007

Journal of Biological Chemistry

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“…The crystal structure of SP-A has not been reported, but the cleft between the three CRDs of SP-D presents a large positively charged surface that could potentially bind and disrupt bacterial membranes (54). C-terminal fragments of SP-A and SP-D have also been reported to enhance neutrophil chemotaxis (55), clearance of respiratory syncytial virus (56), and Aspergillus fumigatus infection (57), and to reduce allergic pulmonary hypersensitivity to A. fumigatus (58).…”

Section: Figure 12mentioning

confidence: 99%

Surfactant proteins A and D inhibit the growth of Gram-negative bacteria by increasing membrane permeability

Wu¹,

Kuzmenko²,

Wan³

et al. 2003

J. Clin. Invest.

130

154

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The pulmonary collectins, surfactant proteins A (SP-A) and D (SP-D), have been reported to bind lipopolysaccharide (LPS), opsonize microorganisms, and enhance the clearance of lung pathogens. In this study, we examined the effect of SP-A and SP-D on the growth and viability of Gram-negative bacteria. The pulmonary clearance of Escherichia coli K12 was reduced in SP-A–null mice and was increased in SP-D–overexpressing mice, compared with strain-matched wild-type controls. Purified SP-A and SP-D inhibited bacterial synthetic functions of several, but not all, strains of E. coli, Klebsiella pneumoniae, and Enterobacter aerogenes. In general, rough E. coli strains were more susceptible than smooth strains, and collectin-mediated growth inhibition was partially blocked by coincubation with rough LPS vesicles. Although both SP-A and SP-D agglutinated E. coli K12 in a calcium-dependent manner, microbial growth inhibition was independent of bacterial aggregation. At least part of the antimicrobial activity of SP-A and SP-D was localized to their C-terminal domains using truncated recombinant proteins. Incubation of E. coli K12 with SP-A or SP-D increased bacterial permeability. Deletion of the E. coli OmpA gene from a collectin-resistant smooth E. coli strain enhanced SP-A and SP-D–mediated growth inhibition. These data indicate that SP-A and SP-D are antimicrobial proteins that directly inhibit the proliferation of Gram-negative bacteria in a macrophage- and aggregation-independent manner by increasing the permeability of the microbial cell membrane

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“…This protein is a constitutive mediator of Ag clearance and is capable of interacting with cellular components of both the innate and adaptive immune systems on mucosal surfaces (1,2). SP-D is a potent inhibitor of T cell function in vitro (3)(4)(5)(6) and was shown to protect against various inflammatory responses in the lung in vivo (7)(8)(9)(10)(11)(12)(13). SP-D is synthesized and secreted primarily by type II alveolar cells, Clara cells, and cells of submucosal glands in the lung (14), but this collectin can also be found in epithelial surfaces of many other organs (14 -18).…”

mentioning

confidence: 99%

IL-4 and IL-13 Form a Negative Feedback Circuit with Surfactant Protein-D in the Allergic Airway Response

Haczku

Cao

Vass

et al. 2006

The Journal of Immunology

127

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The innate immune molecule surfactant protein-D (SP-D) plays an important regulatory role in the allergic airway response. In this study, we demonstrate that mice sensitized and challenged with either Aspergillus fumigatus (Af) or OVA have increased SP-D levels in their lung. SP-D mRNA and protein levels in the lung also increased in response to either rIL-4 or rIL-13 treatment. Type II alveolar epithelial cell expression of IL-4Rs in mice sensitized and challenged with Af, and in vitro induction of SP-D mRNA and protein by IL-4 and IL-13, but not IFN-γ, suggested a direct role of IL-4R-mediated events. The regulatory function of IL-4 and IL-13 was further supported in STAT-6-deficient mice as well as in IL-4/IL-13 double knockout mice that failed to increase SP-D production upon allergen challenge. Interestingly, addition of rSP-D significantly inhibited Af-driven Th2 cell activation in vitro whereas mice lacking SP-D had increased numbers of CD4+ cells with elevated IL-13 and thymus- and activation-regulated chemokine levels in the lung and showed exaggerated production of IgE and IgG1 following allergic sensitization. We propose that allergen exposure induces elevation in SP-D protein levels in an IL-4/IL-13-dependent manner, which in turn, prevents further activation of sensitized T cells. This negative feedback regulatory circuit could be essential in protecting the airways from inflammatory damage after allergen inhalation.

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Surfactant proteins A and D protect mice against pulmonary hypersensitivity induced by Aspergillus fumigatus antigens and allergens

Cited by 180 publications

References 30 publications

Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

Surfactant proteins A and D inhibit the growth of Gram-negative bacteria by increasing membrane permeability

IL-4 and IL-13 Form a Negative Feedback Circuit with Surfactant Protein-D in the Allergic Airway Response

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