Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae

The gene Ag-Aper14 encodes a novel peritrophic matrix (or peritrophic membrane; PM) protein in the mosquito Anopheles gambiae. The Ag-Aper14 protein is merely 89 amino acids long and has a single putative chitin-binding domain. Prior to blood feeding, the Ag-Aper14 protein is stored in secretory ves...

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Bibliographic Details
Published in:Cell and tissue research 2005-04, Vol.320 (1), p.175-185
Main Authors: Devenport, M, Fujioka, H, Donnelly-Doman, M, Shen, Z, Jacobs-Lorena, M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
amino acids
Animals
Anopheles - metabolism
Anopheles gambiae
Antibodies - metabolism
Base Sequence
blood
Digestive System - metabolism
Digestive System - secretion
Digestive System - ultrastructure
epithelial cells
Epithelium - metabolism
Epithelium - secretion
Female
genes
Insect Proteins - chemistry
Insect Proteins - genetics
Insect Proteins - metabolism
Insect Proteins - secretion
Larva
microscopy
Molecular Sequence Data
peritrophic membrane
Protein Structure, Tertiary
secretion
secretory granules
Sequence Homology, Amino Acid
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Summary:The gene Ag-Aper14 encodes a novel peritrophic matrix (or peritrophic membrane; PM) protein in the mosquito Anopheles gambiae. The Ag-Aper14 protein is merely 89 amino acids long and has a single putative chitin-binding domain. Prior to blood feeding, the Ag-Aper14 protein is stored in secretory vesicles next to the epithelial cell lumenal surface. Immunoelectron microscopy has revealed that Ag-Aper14 co-localizes to the same secretory vesicles as another PM protein, Ag-Aper1, indicating a common mode of regulated secretion. Conversely, Ag-Muc1, an epithelial cell-surface protein, does not co-localize to these secretory vesicles and is detected only on the cell surface. After blood feeding, Ag-Aper14 is secreted and incorporated into the PM that surrounds the ingested blood.
ISSN:0302-766X
1432-0878
DOI:10.1007/s00441-004-1067-3