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Volume 270,
Number 49,
Issue of December 8, 1995 pp. 29307-29313
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Identification of
a Novel Giardia lamblia Cyst Wall Protein with Leucine-rich
Repeats
IMPLICATIONS FOR SECRETORY GRANULE FORMATION AND PROTEIN ASSEMBLY
INTO THE CYST WALL
(Received for publication, August 22,
1995; and in revised form, October 4, 1995)
Hugo
D.
Luján
,
Michael R.
Mowatt
,
John
T.
Conrad
,
Blair
Bowers
,
Theodore E.
Nash
Giardia lamblia trophozoites, like most intestinal
parasitic protozoa, undergo fundamental biological changes to survive
outside the intestine of their mammalian host by differentiating into
infective cysts. This complex process entails the coordinated
production, processing, and transport of cyst wall constituents for
assembly into a protective cyst wall. Yet, little is known about this
process and the identity of cyst wall constituents. We previously
identified a 26-kDa cyst wall protein, CWP1. In the present work, using
monoclonal antibodies to cyst wall antigens, we cloned the gene that
encodes a novel 39-kDa cyst wall protein, CWP2. Expression of CWP1 and
CWP2 was induced during encystation with identical kinetics. Soon after
synthesis, these two proteins combine to form a stable complex, which
is concentrated within the encystation-specific secretory granules
before incorporation into the cyst wall. Both proteins contain five
tandem copies of a 24-residue leucine-rich repeat, a motif implicated
in protein-protein interactions. Unlike CWP1, CWP2 has an extremely
basic 121-residue COOH-terminal extension that might be involved in the
sorting of these proteins to the secretory granules.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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