Am. J. Respir. Cell Mol. Biol.,
Volume 26, Number 6, June, 2002 739-747
Porcine Surfactant Protein D Is N-glycosylated in its Carbohydrate
Recognition Domain and Is Assembled into Differently Charged Oligomers
Martin
van Eijk,
Chris H.A.
van de Lest,
Joseph J.
Batenburg,
Arie B.
Vaandrager,
Joseph
Meschi,
Kevan L.
Hartshorn,
Lambert M.G.
van Golde,
and
Henk P.
Haagsman
Department of Biochemistry and Cell Biology and Department of the Science of Food of Animal Origin, Graduate School of Animal
Health, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands; and Department of Medicine and Pathology,
Boston University School of Medicine, Boston, Massachusetts
Surfactant protein D (SP-D) belongs to a subgroup of mammalian collagenous Ca2+-dependent lectins known as the collectins. It is thought to play a significant role in the innate immune response against microorganisms within the lungs and
at other mucosal surfaces. This report documents the isolation
and characterization of SP-D purified from porcine lung lavage
using mannan affinity chromatography and gel filtration. Ultrastructural analysis shows both dodecameric and higher order oligomeric complexes of SP-D. The molecular mass of monomeric porcine SP-D (50 kD) is larger than that of SP-D from
humans (43 kD). The difference in mass is due to the presence
of an Asparagine-linked glycosylation in the carbohydrate recognition domain of porcine SP-D, which is absent in SP-D of
other species investigated so far. Analysis of this carbohydrate
moiety indicates that it is a highly heterogeneous, complex type
oligosaccharide which is sialylated. The heterogeneity of oligosaccharide sialylation results in the existence of many differently charged porcine SP-D isoforms. The removal of the carbohydrate moiety reduces the inhibitory effect of porcine SP-D
on influenza A virus haemagglutination. Therefore, the carbohydrate moiety may influence interactions with pathogens.
Abbreviations: 8-aminonaphtalene-1,3,6-trisulfonate, ANTS; bronchoalveolar lavage, BAL; BAL fluid, BALF; bovine serum albumin, BSA; carbohydrate recognition domain, CRD; collagenase resistant fragment, CRF; ethylenediaminetetraacetic acid, EDTA; fluorophore-assisted carbohydrate
electrophoresis, FACE; hemagglutination, HA; human SP-D, hSP-D; immunoglobulin G, IgG; influenza A virus, IAV; endo-/N-Glycosidase F,
NGF; porcine SP-D, pSP-D; surfactant protein, SP.
This article has been cited by other articles:
|
|
|
|
 
L. Zhang, M. Ikegami, T. R. Korfhagen, F. X. McCormack, M. Yoshida, R. M. Senior, J. M. Shipley, S. D. Shapiro, and J. A. Whitsett
Neither SP-A nor NH2-terminal domains of SP-A can substitute for SP-D in regulation of alveolar homeostasis
Am J Physiol Lung Cell Mol Physiol,
August 1, 2006;
291(2):
L181 - L190.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. R. White, E. Crouch, M. van Eijk, M. Hartshorn, L. Pemberton, I. Tornoe, U. Holmskov, and K. L. Hartshorn
Cooperative anti-influenza activities of respiratory innate immune proteins and neuraminidase inhibitor
Am J Physiol Lung Cell Mol Physiol,
May 1, 2005;
288(5):
L831 - L840.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. van Eijk, M. R. White, J. J. Batenburg, A. B. Vaandrager, L. M. G. van Golde, H. P. Haagsman, and K. L. Hartshorn
Interactions of Influenza A Virus with Sialic Acids Present on Porcine Surfactant Protein D
Am. J. Respir. Cell Mol. Biol.,
June 1, 2004;
30(6):
871 - 879.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. van Eijk, M. R. White, E. C. Crouch, J. J. Batenburg, A. B. Vaandrager, L. M. G. van Golde, H. P. Haagsman, and K. L. Hartshorn
Porcine Pulmonary Collectins Show Distinct Interactions with Influenza A Viruses: Role of the N-Linked Oligosaccharides in the Carbohydrate Recognition Domain
J. Immunol.,
August 1, 2003;
171(3):
1431 - 1440.
[Abstract]
[Full Text]
[PDF]
|
|
|
Copyright © 2002 American Thoracic Society.
|
|
|
