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1 Edward A. Doisy Department of
Biochemistry and Molecular Biology,
Human pulmonary surfactant protein D (SP-D) is a
collagenous C-type lectin with high binding specificity to
-D-glucosyl
residues. It is composed of four regions: a short
NH2-terminal noncollagen sequence,
a collagenous domain, a short linking domain ("neck" region), and
a COOH-terminal carbohydrate recognition domain (CRD). Previous studies demonstrated that SP-D is chemotactic
for inflammatory cells. To test which domain of SP-D might play a role
in this function, a mutant that contains only neck and CRD
regions was expressed in Escherichia
coli and purified by affinity chromatography on
maltosyl-agarose. A 17-kDa recombinant SP-D CRD was identified by two
antibodies (antisynthetic SP-D COOH-terminal and neck region peptides)
but not by synthetic SP-D
NH2-terminal peptide antibody. The
recombinant SP-D CRD was confirmed by amino acid sequencing. Gel-filtration analysis found that 84% of CRD was trimeric and the
rest was monomeric. Analysis of the chemotactic properties of the
trimeric CRD demonstrated that the CRD was chemotactic for neutrophils
(polymorphonuclear leukocytes), with peak activity at
10
10 M equal to the
positive control [formyl-Met-Leu-Phe (fMLP) at 108 M]. The
chemotactic activity was abolished by 20 mM maltose, which did not
suppress the chemotactic response to fMLP. The peak chemotactic
activity of the CRD is comparable to the activity of native SP-D,
although a higher concentration is required for peak activity
(1010 vs.
1011 M). The chemotactic
response to CRD was largely prevented by preincubation of
polymorphonuclear leukocytes with SP-D, and the response to SP-D was
prevented by preincubation with CRD. These preincubations did not
affect chemotaxis to fMLP. These results suggest that trimeric CRD
accounts for the chemotactic activity of SP-D.
surfactant protein D; collectins; host defense proteins; chemotaxis
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