title: Porcine surfactant protein D is N-glycosylated in its carbohydrate recognition domain and is assembled into differently charged oligomers.
abstract: Surfactant protein D (SP-D) belongs to a subgroup of mammalian collagenous Ca(2+)-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.
authors.affiliation: Department of Biochemistry and Cell Biology, Graduate School of Animal Health, Faculty of Veterinary Medicine, Utrecht University, The Netherlands. m.vaneijk@vet.uu.nl
authors.forename: Martin
authors.initials: M
authors.lastname: van Eijk
authors.forename: Chris H A
authors.initials: CH
authors.lastname: van de Lest
authors.forename: Joseph J
authors.initials: JJ
authors.lastname: Batenburg
authors.forename: Arie B
authors.initials: AB
authors.lastname: Vaandrager
authors.forename: Joseph
authors.initials: J
authors.lastname: Meschi
authors.forename: Kevan L
authors.initials: KL
authors.lastname: Hartshorn
authors.forename: Lambert M G
authors.initials: LM
authors.lastname: van Golde
authors.forename: Henk P
authors.initials: HP
authors.lastname: Haagsman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001704:Biopolymers; D015153:Blotting, Western; D001992:Bronchoalveolar Lavage Fluid / Q000737:chemistry; D050260:Carbohydrate Metabolism; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006031:Glycosylation; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D037663:Pulmonary Surfactant-Associated Protein D; D011663:Pulmonary Surfactants / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013552:Swine
chemical_list: D001704:Biopolymers; D006023:Glycoproteins; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D037663:Pulmonary Surfactant-Associated Protein D; D011663:Pulmonary Surfactants