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J Biol Chem, Vol. 273, Issue 28, 17665-17670, July 10, 1998
From the Case Western Reserve University, School of Medicine,
Department of Genetics, Cleveland, Ohio 44106-4955
Upon feeding, mosquito midguts secrete the
peritrophic matrix (PM), an extracellular chitin-containing envelope
that completely surrounds the blood meal. Because the malaria parasite
must cross the PM to complete its life cycle in the mosquito, the PM is
a potential barrier for malaria transmission. By antibody screening of
an expression library we have identified and partially characterized a
cDNA encoding a putative PM protein, termed Anopheles
gambiae adult peritrophin 1 (Ag-Aper1).
Ag-Aper1 is the first cloned PM gene from a disease vector.
Northern analysis detected an abundant Ag-Aper1 transcript
only in the adult gut, and not in any other tissues or at any other
stages of development. The predicted amino acid sequence indicates that
it has two tandem chitin-binding domains that share high sequence
similarity with each other and also with the chitin-binding domain of
an adult gut-specific chitinase from the same organism. The presumed
ability of Ag-Aper1 to bind chitin was verified by a
functional assay with the baculovirus-expressed recombinant protein.
Ag-Aper1 did bind to chitin but not to cellulose, indicating that
Ag-Aper1 binds chitin specifically. The double chitin-binding domain
organization of Ag-Aper1 suggests that each protein
molecule is able to link two chitin polymer chains. Hence, this protein
is likely to act as a molecular linker that connects PM chitin fibrils
into a three-dimensional network.
A Type I Peritrophic Matrix Protein from the Malaria Vector
Anopheles gambiae Binds to Chitin
CLONING, EXPRESSION, AND CHARACTERIZATION
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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