Conclusions
The surfactant-associated proteins, SP-A and SP-D, are members of a family of collagenous host defense lectins. There is increasing evidence that these pulmonary epithelial-derived proteins are important components of the innate immune response to microbial challenge. The lung collectins bind to glycoconjugates expressed by a wide variety of microorganisms in vitro. Such binding may cause microbial aggregation with resulting enhancement of mucociliary or leukocyte-mediated clearance. However, SP-A and SP-D also have the capacity to opsonize microorganisms with enhancement of phagocytosis and killing. Complementary or cooperative interactions between SP-A and SP-D and other lectins such as the macrophage mannose receptor could contribute to the efficiency of this defense system. Environmental or growth-phase-dependent modulation of glycoconjugates expressed on the surface of microorganisms could influence the mechanism or effectiveness of lectin-mediated clearance. Collectins may play particularly important roles in settings of inadequate or impaired specific immunity. Studies are needed to examine the possibility that acquired deficiencies of the lung collectins in certain hospitalized patients may render them susceptible to pathogens that otherwise are harmless to healthy individuals.
Keywords
- Alveolar Macrophage
- Surfactant Protein
- Carbohydrate Recognition Domain
- Pulmonary Alveolar Proteinosis
- Macrophage Mannose Receptor
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Ofek, I., Crouch, E. (2002). Interactions of Microbial Glycoconjugates with Collectins. In: Doyle, R.J. (eds) Glycomicrobiology. Springer, Boston, MA. https://doi.org/10.1007/0-306-46821-2_18
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