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Departments of 1 Anesthesiology, 3 Physiology and Biophysics, and 4 Pediatrics, University of Alabama at Birmingham, Birmingham, Alabama 35233; and 2 Division of Pulmonary, Critical Care, and Occupational Medicine, Department of Medicine, Indiana University School of Medicine, Indianapolis, Indiana 46202
We investigated whether nitration of
surfactant apoprotein (SP) A alters its ability to bind to
mannose-containing saccharides on Pneumocystis
carinii and its potential role in the mediation of
P. carinii adherence to alveolar
macrophages. Human SP-A was nitrated by incubation with
tetranitromethane at pH 8.0 or synthetic peroxynitrite
(ONOO
) at pH 7.4, which
resulted in significant nitration of tyrosines in its carbohydrate
recognition domain [0.63 ± 0.001 (SE) and 1.25 ± 0.02 mol
nitrotyrosine/mol monomeric SP-A, respectively; n = 3 samples]. Binding of SP-A
to P. carinii was calcium dependent and competitively inhibited by
-methyl-D-mannopyranoside.
Nitration of SP-A by ONOO
or tetranitromethane decreases its binding to P. carinii by increasing its dissociation constant from
7.8 × 109 to 1.6 × 108 or 2.4 × 108 M, respectively,
without significantly affecting the number of binding sites (7.1 × 106/P.
carinii organisms, assuming that the native molecular
mass of oligomeric SP-A is 650 kDa). Furthermore,
ONOO-nitrated SP-A failed
to mediate the adherence and phagocytosis of P. carinii to rat alveolar macrophages as observed with
normal SP-A. Binding of SP-A to rat alveolar macrophages was not
altered by nitration. These results indicate that nitration of SP-A
interferes with its ability to serve as a ligand for
P. carinii adherence to alveolar
macrophages at the site of the SP-A moleculeP.
carinii interaction.
surfactant protein A; collectin; tyrosine nitration; parasite adherence; nitric oxide; lung host defense
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