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J. Biol. Chem., Vol. 269, Issue 42, 26419-26423, 10, 1994
PJ Muchowski, L Zhang, ER Chang, HR Soule, EF Plow and M Moyle
Neutrophil inhibitory factor (NIF) is a hookworm-derived glycoprotein
ligand of the integrin CD11b/CD18 that inhibits human neutrophil function
(Moyle, M., Foster, D. L., McGrath, D. E., Brown, S. M., Laroche, Y., De
Meutter, J., Stanssens, P., Bogowitz, C. A., Fried, V. A., Ely, J. A.,
Soule, H. R., and Vlasuk, G. P. (1994) J. Biol. Chem. 269, 1008-10015).
Here, we present evidence that recombinant NIF (rNIF) associates with the
approximately 200-amino acid residue I domain of CD11b/CD18 and that this
interaction is essential for inhibition of neutrophil function by NIF.
First, radiolabeled rNIF binds to a recombinant glutathione S-transferase
fusion protein that contains the CD11b I domain. This high affinity
interaction has a partial dependence on divalent cations. The association
of rNIF with the CD11b I domain is specific because 125I-rNIF does not bind
either a glutathione S- transferase fusion protein that contains the I
domain of the integrin CD11a/CD18 or recombinant glutathione S-transferase
without the I domain. Second, the CD11b I domain fusion protein effectively
competes with CD11b/CD18 on human neutrophils for 125I-rNIF binding. Third,
the CD11b I domain fusion protein blocks the inhibition of certain
neutrophil functions by rNIF, including adhesion of neutrophils to human
endothelial cell monolayers and adhesion-dependent release of hydrogen
peroxide from neutrophils. Specificity is demonstrated by the inability of
the CD11a I domain fusion protein to block either rNIF binding to
neutrophils or rNIF activity. Fourth, rNIF blocks the interaction between
neutrophils and fibrinogen, a CD11b/CD18 ligand that is also thought to
bind the I domain of CD11b. In contrast, rNIF does not appear to block the
binding of factor X to CD11b/CD18 on neutrophils. These results suggest
that CD11b/CD18 has multiple distinct binding sites for its cognate
ligands, including, but not limited to, the I domain. NIF interferes with
the binding of a subset of these CD11b/CD18 ligands in a highly selective
manner.
Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18 [published erratum appears in J Biol Chem 1995 Mar 17;270(11):6420]
Corvas International, Inc., San Diego, California 92121.
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