Peritrophic matrix proteins of Anopheles gambiae and Aedes aegypti
- 1 November 1996
- journal article
- Published by Wiley in Insect Molecular Biology
- Vol. 5 (4) , 261-268
- https://doi.org/10.1111/j.1365-2583.1996.tb00100.x
Abstract
Little is known about the composition and function of the mosquito peritrophic matrix (PM), a physical barrier that pathogens must traverse to complete their life cycles. Anopheies gambiae and Aedes aegypti PM proteins induced by blood or by a protein-free meal have been characterized by the use of 2-D gel electrophoresis and lectin-binding affinity assays. More than forty proteins have been identified in both species. Over half of the PM proteins of both mosquitoes migrate identically. Many PM proteins appear to be giycosylated, primarily by high mannose N-linked glycosyi groups.Keywords
This publication has 41 references indexed in Scilit:
- Feeding behaviour of female Aedes aegypti: effects of diet temperature, bicarbonate and feeding technique on the response to ATPPhysiological Entomology, 1994
- Structure, function, and intracellular localization of glycoprotein B of herpesvirus simian agent 8 expressed in insect and mammalian cellsArchiv für die gesamte Virusforschung, 1993
- The Midgut Ultrastructure Of Hematophagous InsectsAnnual Review of Entomology, 1990
- Maturation of Japanese encephalitis virus glycoproteins produced by infected mammalian and mosquito cellsVirology, 1989
- GLYCOBIOLOGYAnnual Review of Biochemistry, 1988
- GlycobiologyAnnual Review of Biochemistry, 1988
- Extracellular Matrix AssemblyAnnual Review of Cell and Developmental Biology, 1988
- Proteoglycan metabolism associated with mouse metanephric development: Morphologic and biochemical effects of β-d-xylosideDevelopmental Biology, 1987
- Peritrophic membranes and protease activity in the midgut of the malaria mosquito, Anopheles stephensi (Liston) (Insecta: Diptera) under normal and experimental conditionsJournal of Ultrastructure Research, 1983
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970