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The Anopheles gambiae adult midgut peritrophic matrix proteome.
- Source :
-
Insect biochemistry and molecular biology [Insect Biochem Mol Biol] 2009 Feb; Vol. 39 (2), pp. 125-34. Date of Electronic Publication: 2008 Nov 11. - Publication Year :
- 2009
-
Abstract
- Malaria is a devastating disease. For transmission to occur, Plasmodium, the causative agent of malaria, must complete a complex developmental cycle in its mosquito vector. Thus, the mosquito is a potential target for disease control. Plasmodium ookinetes, which develop within the mosquito midgut, must first cross the midgut's peritrophic matrix (PM), a thick extracellular sheath that completely surrounds the blood meal. The PM poses a partial, natural barrier against parasite invasion of the midgut and it is speculated that modifications to the PM may lead to a complete barrier to infection. However, such strategies require thorough characterization of the structure of the PM. Here, we describe for the first time, the complete PM proteome of the main malaria vector, Anopheles gambiae. Altogether, 209 proteins were identified by mass spectrometry. Among them were nine new chitin-binding peritrophic matrix proteins, expanding the list from three to twelve peritrophins. Lastly, we provide a model for the putative interactions among the proteins identified in this study.
- Subjects :
- Animals
Anopheles chemistry
Anopheles genetics
Digestive System chemistry
Digestive System metabolism
Extracellular Matrix Proteins chemistry
Extracellular Matrix Proteins genetics
Female
Humans
Insect Proteins chemistry
Insect Proteins genetics
Insect Vectors chemistry
Insect Vectors genetics
Malaria transmission
Molecular Sequence Data
Protein Structure, Tertiary
Proteome chemistry
Proteome genetics
Anopheles metabolism
Extracellular Matrix Proteins metabolism
Insect Proteins metabolism
Insect Vectors metabolism
Proteome metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1879-0240
- Volume :
- 39
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Insect biochemistry and molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 19038338
- Full Text :
- https://doi.org/10.1016/j.ibmb.2008.10.010