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J Biol Chem, Vol. 274, Issue 34, 23916-23925, August 20, 1999
Associates with Heparan
Sulfates through the First 
-Strand of the Chemokine
From the a Unité d'Immunologie Virale,
d Unité de Chimie Organique, h Laboratoire de
Résonance Magnetique Nucléaire CNRS URA 1129, Institut
Pasteur, 28 Rue du Dr. Roux, 75724 Paris Cedex 15, France,
e Theodor Kocher Institute, University of Bern,
CH3000 Bern 9, Switzerland, f Laboratoire d'Immunologie
Cellulaire, CNRS URA 625, Cervi, Paris, France, and
i Institut de Biologie Structurale, 41 Avenue des Martyrs,
38027 Grenoble, Cedex 01, France
Biological properties of chemokines are believed
to be influenced by their association with glycosaminoglycans. Surface
plasmon resonance kinetic analysis shows that the CXC chemokine stromal cell-derived factor-1
(SDF-1), which binds the CXCR4 receptor, associates with heparin with an affinity constant of 38.4 nM (kon = 2.16 × 106 M
1 s1 and
koff = 0.083 × s1). A
modified SDF-1 (SDF-1 3/6) was generated by combined substitution of
the basic cluster of residues Lys24, His25, and
Lys27 by Ser. SDF-1 3/6 conserves the global native
structure and functional properties of SDF-1, but it is unable to
interact with sensor chip-immobilized heparin. The biological relevance
of these in vitro findings was investigated. SDF-1 was
unable to bind in a CXCR4-independent manner on epithelial cells that
were treated with heparan sulfate (HS)-degrading enzymes or
constitutively lack HS expression. The inability of SDF-1 3/6 to bind
to cells underlines the importance of the identified basic cluster for the physiological interactions of SDF-1 with HS. Importantly, the
amino-terminal domain of SDF-1 which is required for binding to, and
activation of, CXCR4 remains exposed after binding to HS and is
recognized by a neutralizing monoclonal antibody directed against the
first residues of the chemokine. Overall, these findings indicate that
the Lys24, His25, and Lys27 cluster
of residues forms, or is an essential part of, the HS-binding site
which is distinct from that required for binding to, and signaling
through, CXCR4.
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