Pulmonary surfactant protein A binds to <i>Cryptococcus neoformans</i> without promoting phagocytosis

Walenkamp, Annemiek; Verheul, A. F. M.; Scharringa, Jelle; Hoepelman, I. M.

doi:10.1046/j.1365-2362.1999.00429.x

Cited by 34 publications

(24 citation statements)

References 30 publications

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“…These results were unexpected as it has previously been reported that SP-D does not bind to capsular C. neoformans (35,43). The exact cause of the differences between the data obtained in the present study and those in previous reports is as yet unclear but may be related to differences in sensitivities of the antibodies used (35) or the different experimental approaches to the detection of bound protein (43).…”

Section: Discussioncontrasting

confidence: 89%

“…Based on previous studies (35,43), the finding that SP-D had the highest affinity for the acapsular mutant of C. neoformans (strain B4131) was as expected. On the other hand, SP-D did also bind to the encapsulated strains but with much lower affinity.…”

Section: Sp-d Binds Encapsulated As Well As Acapsular C Neoformanssupporting

confidence: 76%

“…Furthermore, two papers have reported that SP-D binds to the acapsular, but not to the encapsulated, form of C. neoformans (35,43). Interestingly, it was also found that SP-D binding resulted in the aggregation of acapsular but not encapsulated C. neoformans (35).…”

mentioning

confidence: 99%

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Aggregation ofCryptococcus neoformansby Surfactant Protein D Is Inhibited by Its Capsular Component Glucuronoxylomannan

et al. 2004

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Section: Discussioncontrasting

confidence: 89%

Section: Sp-d Binds Encapsulated As Well As Acapsular C Neoformanssupporting

confidence: 76%

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Aggregation ofCryptococcus neoformansby Surfactant Protein D Is Inhibited by Its Capsular Component Glucuronoxylomannan

et al. 2004

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“…SP-A has been shown to inhibit TNF-␣ synthesis induced by LPS-stimulated cells (24), but can also independently stimulate TNF-␣ production (25). Moreover, SP-A binds to LPS (26) and to the surface of a variety of bacteria (27,28), viruses (29), and fungi (30) and enhances the phagocytosis of some micro-organisms (31), but inhibits (32) or does not affect the phagocytosis of others (33).…”

mentioning

confidence: 99%

Surfactant Protein A Suppresses Lipopolysaccharide-Induced IL-10 Production by Murine Macrophages

Salez

Balloy

Rooijen

et al. 2001

The Journal of Immunology

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Upon LPS exposure, mononuclear phagocytes produce TNF-α and IL-10, two cytokines with pro- and anti-inflammatory activities, respectively. We previously described that murine resident alveolar macrophages, which play a central role in the immunosurveillance of the lung alveoli, do not synthesize IL-10 in vivo or in vitro when exposed to LPS. In the present report we demonstrate that during lung inflammation induced by the intranasal administration of LPS, bronchoalveolar cells collected between days 3 and 5 are able to synthesize IL-10 when exposed to LPS. We also show that depletion of resident alveolar macrophages by an intratracheal instillation of liposome-encapsulated clodronate is followed by subsequent replenishment of the airspaces by mononuclear phagocytes. This is accompanied by the transient competence of cells for IL-10 production. The cell capacity to produce IL-10 is evident up to 3 days and then decreases. This led us to hypothesize that the alveolar environment contains a down-regulator of LPS-induced IL-10 synthesis by recently emigrating mononuclear phagocytes. We show that the surfactant protein A, an airspace protein that has known immunomodulatory activities, dramatically inhibits LPS-induced IL-10 formation by bone marrow-derived macrophages. These data show a difference between resident and inflammatory macrophages with respect to IL-10 synthesis. Moreover, this study highlights for the first time the inhibitory role of surfactant protein A in the anti-inflammatory activity of macrophages through inhibition of IL-10 production.

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“…For instance, it is claimed that for some organisms, collectins suppress phagocytosis; other studies suggest that SP-A and SP-D have opposite effects on host cell function (9). In addition, the functional comparisons between the lung collectins and MBP are clearly limited, since there have been no reports of complement activation by SP-A or SP-D.…”

Section: Surfactant Proteins and Pulmonary Host Defensementioning

confidence: 99%

The pulmonary collectins, SP-A and SP-D, orchestrate innate immunity in the lung

McCormack

Whitsett²

2002

J. Clin. Invest.

167

141

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Pulmonary surfactant protein A binds to Cryptococcus neoformans without promoting phagocytosis

Abstract: Our results indicate that SP-A binds in a concentration-dependent manner to both encapsulated and acapsular C. neoformans. Despite SP-A binding to the acapsular C. neoformans, phagocytosis by various phagocytes was not enhanced.

Cited by 34 publications

References 30 publications

Aggregation ofCryptococcus neoformansby Surfactant Protein D Is Inhibited by Its Capsular Component Glucuronoxylomannan

Aggregation ofCryptococcus neoformansby Surfactant Protein D Is Inhibited by Its Capsular Component Glucuronoxylomannan

Surfactant Protein A Suppresses Lipopolysaccharide-Induced IL-10 Production by Murine Macrophages

The pulmonary collectins, SP-A and SP-D, orchestrate innate immunity in the lung

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