Interactions of recombinant human pulmonary surfactant protein d
and sp-d multimers with influenza a.
Hartshorn, Kevan, Donald Chang, Kevin Rust, Mitchell White, John
Heuser, and Edmond Crouch.
Departments of Medicine and Pathology, Boston University School of
Medicine, and the Departments of Pathology and Cell Biology and
Physiology, Washington University School of Medicine, St. Louis,
Missouri
APStracts 3:0101L, 1996.
To further study the structure and function of SP-D, recombinant human
SP-D (RhSP-D) was isolated from the culture medium of CHO-K1 cells
stably transfected with a full length hSP-D cDNA. Although a
significant fraction of the secreted RhSP-D was recovered as
dodecamers similar to recombinant rat SP-D (RrSP-D), a major fraction
accumulated as multimers of dodecamers indistinguishable from human
proteinosis SP-D. As previously shown for the rat protein, RhSP-D
agglutinated specific strains of influenza A virus (IAV), inhibited
viral hemagglutinin activity, and protected neutrophils (PMNs) from
deactivation by IAV. However, the potency of RhSP-D multimers was
several-fold greater than for purified dodecamers, comparable to
natural, proteinosis hSP-D. Although RhSP-D multimers were also more
potent than the serum collectins in mediating viral aggregation and
protection of neutrophils, they were less potent than conglutinin in
inhibiting infectivity in vitro. These studies establish that the
propensity of hSP-D to form multimers of dodecamers is determined by
its primary structure, and demonstrate CRD valency-dependent
interactions of SP-D with IAV.
Received 30 January 1996; accepted in final form June 1996.
APS Manuscript Number L34-6.
Article publication pending Am. J. Physiol. (Lung Cell. Mol.
Physiology).
ISSN 1080-4757 Copyright 1996 The American Physiological Society.
Published in APStracts on 4 July 96