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J Biol Chem, Vol. 273, Issue 21, 12960-12966, May 22, 1998
,,
From the Detailed analysis of various heparan sulfate (HS)
species is seriously hampered by a lack of appropriate tools, such as
antibodies. We adopted phage display technology to generate anti-HS
antibodies. A "single pot" semisynthetic human antibody phage
display library was subjected to four rounds of selection on HS from
bovine kidney using panning methodology. Three different phage clones
expressing anti-HS single chain variable fragment antibodies (HS4C3,
HS4D10, and HS3G8) were isolated, with an amino acid sequence of the
complementarity-determining region 3 of GRRLKD (VH3
gene, DP-38), SLRMNGCGAHQ (VH3 gene,
DP-42), and YYHYKVN (VH1 gene,
DP-8), respectively. The antibodies react with HS and
heparin, but not with DNA or other glycosaminoglycans. Kd values for HS are about 0.1 µM.
The three antibodies react differently toward various HS preparations
and show different staining patterns on rat kidney sections, indicating
recognition of different HS molecules. This also holds for two
described mouse anti-HS IgMs (JM403 and 10E4; both generated by
conventional hybridoma technique) and indicates the presence of at
least 5 different HS species in the kidney. O- and
N-sulfation are important for binding of HS to HS4C3 and
HS3G8. The three single chain antibodies, but not JM403, block a basic
fibroblast growth factor binding site of HS. It is concluded that phage
display technology presents a powerful technique to generate antibodies
specific for HS epitopes. This is the first time this technique has
been successfully applied to obtain directly antibodies to
(poly)saccharides.
Department of Biochemistry,
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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