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 Blood, 15 September 2005, Vol. 106, No. 6, pp. 1982-1987.
Prepublished online as a Blood First Edition Paper on June 2, 2005; DOI 10.1182/blood-2005-02-0514.

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Submitted February 7, 2005
Accepted May 22, 2005

Gain of von Willebrand Factor-binding function by mutagenesis of a species-conserved residue within the leucine-rich repeat region of platelet glycoprotein Ib{alpha}

Yuandong Peng, Corie N Shrimpton, Jing-fei Dong, and Jose A Lopez*

Thrombosis Research Section, Department of Medicine, Baylor College of Medicine, Houston, TX, USA

* Corresponding author; email: josel{at}bcm.tmc.edu.

Glycoprotein (GP) Ib{alpha}, a member of the leucine-rich repeat (LRR) protein family, mediates platelet adhesion to immobilized von Willebrand factor (VWF). We investigated the role in VWF binding of charged residues in the LRR region of GP Ib{alpha} that are conserved in the human, dog, and mouse proteins. Substitution of His86 with either Ala or Glu resulted in a gain of VWF-binding function as judged by increased VWF binding in the presence of the modulators ristocetin and botrocetin, and by enhanced adhesion of CHO cells expressing the mutant GPIb{alpha} to immobilized VWF under conditions of flow. This is the first report of a gain-of-function phenotype resulting from mutations in the LRR region of GP Ib{alpha}. Because His86 is 20 angstrom away from the region of GP Ib{alpha} with the largest surface of contact with VWF, the data suggest that the LRRs regulate GP Ib{alpha} affinity for VWF allosterically.


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