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Interleukin-8 (IL-8) has at least two binding regions for both
the A and the B type IL-8 receptors. This study defines an important
region between Cys
Volume 270,
Number 18,
Issue of May 5, pp. 10428-10431, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
and Lys
of Interleukin-8 in the High
Affinity Interaction with the Interleukin-8 Receptor Type
A
and Cys that, together with
the Glu
-Leu
-Arg
sequence of the
NH
terminus, accounts for the high affinity binding of IL-8
to the IL-8 A receptor on leukocytes. Utilizing rabbit IL-8 that shares
82% sequence identity with human IL-8, but has 200-fold lower binding
affinity for the IL-8 A receptor, residues of the human homologue were
sequentially exchanged into the rabbit molecule. Replacement of rabbit
His and Thr
with Tyr
and
Lys
of the human molecule converted the low affinity
binding of the rabbit IL-8 to the high affinity binding of human IL-8
as shown by both competitive binding and by Ca
mobilization. As a corollary, replacement of the Tyr
and Lys
of the human IL-8 with His
and
Thr
of the rabbit IL-8 reduced binding activity of this
mutated human IL-8 200-fold. The site of interaction on the IL-8
receptor type A for the Tyr
and Lys
sequence
was found to be in the NH
-terminal region of this receptor.
A structural pattern of the binding between IL-8 and the A type IL-8
receptor is proposed.
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