ArticleDevelopmental and comparative immunology2017
Hemolymph proteins of Anopheles gambiae larvae infected by Escherichia coli.
Article in Developmental and comparative immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Partial reconstitution of the prophenoloxidase activation system inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Fluctuating Warm and Humid Conditions Differentially Impact Immunity and Development in the Malaria Vector Anopheles stephensi.Global change biology · 2025Article
- CLIPA protein pairs function as cofactors for prophenoloxidase activation in Anopheles gambiae.Insect biochemistry and molecular biology · 2025Article
- Serine protease homolog pairs CLIPA4-A6, A4-A7Δ, and A4-A12 act as cofactors for proteolytic activation of prophenoloxidase-2 and -7 in Anopheles gambiae.Insect biochemistry and molecular biology · 2024Article
- Integrative Proteomic and Phosphoproteomic Analyses Revealed Complex Mechanisms Underlying Reproductive Diapause inInsects · 2022Article
- Trained Immunity inFrontiers in microbiology · 2021Article
- Changes in composition and levels of hemolymph proteins during metamorphosis of Manduca sexta.Insect biochemistry and molecular biology · 2020Article
- When Appearance Misleads: The Role of the Entomopathogen Surface in the Relationship with Its Host.Insects · 2020Review
- Mosquito Hemocytes Associate With Circulatory Structures That Support Intracardiac Retrograde Hemolymph Flow.Frontiers in physiology · 2018Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Anopheles gambiae is a major vector of human malaria and its immune system in part determines the fate of ingested parasites. Proteins, hemocytes and fat body in hemolymph are critical components of this system, mediating both humoral and cellular defenses. Here we assessed differences in the hemolymph proteomes of water- and E. coli-pricked mosquito larvae by a gel-LC-MS approach. Among the 1756 proteins identified, 603 contained a signal peptide but accounted for two-third of the total protein amount on the quantitative basis. The sequence homology search indicated that 233 of the 1756 may be related to defense. In general, we did not detect substantial differences between the control and induced plasma samples in terms of protein numbers or levels. Protein distributions in the gel slices suggested post-translational modifications (e.g. proteolysis) and formation of serpin-protease complexes and high Mr immune complexes. Based on the twenty-five most abundant proteins, we further suggest that major functions of the larval hemolymph are storage, transport, and immunity. In summary, this study provided first data on constitution, levels, and possible functions of hemolymph proteins in the mosquito larvae, reflecting complex changes occurring in the fight against E. coli infection.
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