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Differential expression of proteins in the midgut of Anopheles albimanus infected with Plasmodium berghei
Authors:Vania Serrano-Pinto  Maribel Acosta-Pérez  Darwin Luviano-Bazán  Gerardo Hurtado-Sil  Cesar VF Batista  Jesús Martínez-Barnetche  Humberto Lánz-Mendoza
Institution:2. Laboratoire de Spectrométrie de Masse Bioorganique (LSMBO), Université de Strasbourg, CNRS-UMR7178, 25 rue Becquerel, 67087 Strasbourg Cedex 2, France;3. Plate-forme Protéomique, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris cedex 15, France;4. Laboratoire de Génétique Moléculaire, Génomique et Microbiologie, Université de Strasbourg, CNRS-UMR7156, Equipe Ecophysiologie Moléculaire des Microorganismes 28, rue Goethe, 67083 Strasbourg Cedex, France;5. INRA, UMR 1300 BioEpAR, ENVN, Atlanpole La Chantrerie, BP 40706, F 44307 Nantes Cedex 03, France;6. Unité Interactions Moléculaires Flavivirus-Hôtes, 25 rue du Dr Roux, 75724 Paris cedex 15, France;1. Mosquito Control Laboratory, QIMR Berghofer Medical Research Institute, Brisbane, Queensland, Australia;2. Environmental Research Institute and Griffith School of Environment, Griffith University, Brisbane, Queensland, Australia;3. Environmental Health and Ecological Sciences Thematic Group, Ifakara Health Institute, Ifakara, United Republic of Tanzania;4. Vector Biology Department, Liverpool School of Tropical Medicine, Liverpool, United Kingdom;5. The Protein Discovery Centre, QIMR Berghofer Medical Research Institute, Brisbane, Australia
Abstract:The main vector for transmission of malaria in Mexico is the Anopheles albimanus mosquito. The midgut of disease-transmitting mosquitoes carries out a variety of functions that are related to blood feeding. We analyzed the midgut of A. albimanus infected with Plasmodium berghei (resistant mosquito) using a proteomic approach to identify putative short peptides that are enriched in the midgut after blood feeding. Mosquito midguts were analyzed by two-dimensional electrophoresis to determine the changes in protein profiles. We identified 21 spot proteins that are differentially expressed in the blood of mosquitoes during the immune challenge. Molecular weight of the spots varied from 13 to 36 kDa, with a broad isoelectric point range of 3.92–8.90. We identified the differentially expressed proteins using mass spectrometry and constructed a proteomic data base of the A. albimanus midgut with diverse functions, some of them proteins with digestive and immunologic functions. Identification of these proteins may have important implications for understanding the blood meal digestion process, as well as developing novel vector control strategies and understanding parasite vector interactions.
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