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.