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Blood, Vol. 92 No. 12 (December 15), 1998:
pp. 4602-4611
The Human Poliovirus Receptor Related 2 Protein Is a New
Hematopoietic/Endothelial Homophilic Adhesion Molecule
Marc Lopez,
Mustapha Aoubala,
François Jordier,
Daniel Isnardon,
Sophie Gomez, and
Patrice Dubreuil
From INSERM U.119, Unité de Cancérologie et
Thérapeutique Expérimentales, Marseille, France; and the
Institut Paoli-Calmettes, Marseille, France.
We have recently described Poliovirus Receptor Related 2 (PRR2), a
new cell surface molecule homologous to the poliovirus receptor
(PVR/CD155). Both molecules are transmembrane glycoproteins belonging
to the Ig superfamily (IgSF). They contain 3 Ig domains of V, C2, and
C2 types in their extracellular regions that share 51% aa identity.
The PRR2 gene encodes two mRNA isoforms of 3.0 kb (hPRR2 [short
form]) and 4.4 kb (hPRR2 [long form]), both widely expressed in
human tissues, including hematopoietic cells. To further characterize
PRR2 expression during hematopoiesis and to analyze its function, we
have developed a monoclonal antibody (MoAb) directed against its
extracellular region (R2.477). PRR2 was expressed in 96% of the
CD34+, 88% of the CD33+, and 95% of the
CD14+ hematopoietic lineages and faintly in the CD41
compartment. Ectopic expression of both PRR2 cDNAs induced marked cell
aggregation. A soluble chimeric receptor construct with the Fc fragment
of human IgG1 (PRR2-Fc) as well as a fab fragment of the anti-PRR2 MoAb
(R2.477) inhibit aggregation. PRR2-Fc binds specifically to
PRR2-expressing cells. These results suggest that PRR2 is a homophilic
adhesion receptor. PRR2 was also expressed at the surface of
endothelial cells at the intercellular junctions of adjacent cells but
not at the free cellular edges. Homophilic interactions are associated
with dimerization of isoforms of PRR2 and lead to the tyrosine
phosphorylation of PRR2. Altogether, these results suggest that
homophilic properties of PRR2 could participate to the regulation of
hematopoietic/endothelial cell functions.
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