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Originally published In Press as doi:10.1074/jbc.M105235200 on June 29, 2001

J. Biol. Chem., Vol. 276, Issue 40, 37431-37435, October 5, 2001
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N-terminal Residues of Plasmatocyte-spreading Peptide Possess Specific Determinants Required for Biological Activity*

Kevin D. ClarkDagger , Brian F. Volkman§, Honglada ThoetkiattikulDagger , Yoichi Hayakawa, and Michael R. StrandDagger ||

From the Dagger  Department of Entomology, University of Wisconsin-Madison, Madison, Wisconsin 53706, the § Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, and the  Biochemical Laboratory, Institute of Low Temperature Science, Hokkaido University, Sapporo 060-0819, Japan

Plasmatocyte-spreading peptide (PSP) is a 23-amino acid cytokine that activates a class of insect immune cells called plasmatocytes. The tertiary structure of PSP consists of an unstructured N terminus (residues 1-6) and a well structured core (residues 7-23). A prior study indicated that deletion of the N terminus from PSP eliminated all biological activity. Alanine substitution of the first three residues (Glu1-Asn2-Phe3) further indicated that only replacement of Phe3 resulted in a loss of activity equal to the N-terminal deletion mutant. Here, we characterized structural determinants of the N terminus. Adding a hydroxyl group to the aromatic ring of Phe3 (making a Tyr) greatly reduced activity, whereas the addition of a fluorine (p-fluoro) did not. Substitutions that changed the chirality or replaced the aromatic ring of Phe3 with a branched aliphatic chain (making a Val) also greatly decreased activity. The addition of a methylene group to Val (making a Leu) partially restored activity, whereas the removal of a methylene group from Phe (phenyl-Gly) eliminated all activity. These results indicated that a branched carbon chain with a methylene spacer at the third residue is the minimal structural motif required for activity. The deletion of Glu1 also eliminated activity. Additional experiments identified the charged N-terminal amine and backbone of Glu1 as key determinants for activity.

* This work was supported by National Institutes of Health Grant AI32917 and Wisconsin Hatch Grant WIS044436 (to M. R. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and structure factors of PSP can be accessed through NCBI Protein Data base under NCBI accession 6729988 (8). The deduced amino acid sequence of the PSP precursor protein can also be accessed through the NCBI Protein Data base under NCBI accession JE0359 or the GenBankTM accession number AF062489 (7).

|| To whom correspondence should be addressed: Dept. of Entomology, 237 Russell Laboratories, University of Wisconsin, Madison, WI 53706. Tel.: 608-262-6902; Fax: 608-262-3322; E-mail: mrstrand@facstaff. wisc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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