Apolipophorin-III mediates antiplasmodial epithelial responses in Anopheles gambiae (G3) mosquitoes

• Published in: PloS one 2010-11, Vol.5 (11), p.e15410-e15410
• Main Authors: Gupta, Lalita, Noh, Ju Young, Jo, Yong Hun, Oh, Seung Han, Kumar, Sanjeev, Noh, Mi Young, Lee, Yong Seok, Cha, Sung-Jae, Seo, Sook Jae, Kim, Iksoo, Han, Yeon Soo, Barillas-Mury, Carolina
• Format: Article
• Language: English
• Subjects: Agriculture; Amino Acid Sequence; Animals; Anopheles; Anopheles - immunology; Anopheles - parasitology; Anopheles gambiae; Antiprotozoal agents; Apolipoproteins; Apolipoproteins - genetics; Apolipoproteins - immunology; Apolipoproteins - metabolism; Apoptosis; Aquatic insects; Base Sequence; Biology; Blotting, Western; Bombyx mandarina; Culicidae; Cytoplasm; Digestive System - immunology; Digestive System - metabolism; Digestive System - parasitology; Drosophila; Epithelium - immunology; Epithelium - metabolism; Epithelium - parasitology; Female; Fruit flies; Gene Expression; Health aspects; Host-Parasite Interactions; Humidity; Hyphantria cunea; Immune response; Immunity; Immunofluorescence; Infections; Infectious diseases; Innate immunity; Insect Proteins - chemistry; Insect Proteins - classification; Insect Proteins - immunology; Insect Vectors - immunology; Insect Vectors - parasitology; Insects; Laboratories; Lepidoptera; Life sciences; Lipids; Malaria; Manduca sexta; Medicine; Mice; Mice, Inbred BALB C; Midgut; Models, Molecular; Molecular Sequence Data; Mosquitoes; Parasites; Phylogenetics; Phylogeny; Plasmodium; Plasmodium berghei; Plasmodium berghei - immunology; Plasmodium berghei - physiology; Protein Folding; Protein structure; Protein Structure, Secondary; Proteins; Public health; Reverse Transcriptase Polymerase Chain Reaction; RNA; RNA Interference; RNA, Messenger - genetics; RNA, Messenger - metabolism; Sequence Homology, Amino Acid; Tertiary structure; Tobacco
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0015410

Apolipophorin-III (ApoLp-III) is known to play an important role in lipid transport and innate immunity in lepidopteran insects. However, there is no evidence of involvement of ApoLp-IIIs in the immune responses of dipteran insects such as Drosophila and mosquitoes. We report the molecular and functional characterization of An. gambiae apolipophorin-III (AgApoLp-III). Mosquito ApoLp-IIIs have diverged extensively from those of lepidopteran insects; however, the predicted tertiary structure of AgApoLp-III is similar to that of Manduca sexta (tobacco hornworm). We found that AgApoLp-III mRNA expression is strongly induced in the midgut of An. gambiae (G3 strain) mosquitoes in response to Plasmodium berghei infection. Furthermore, immunofluorescence stainings revealed that high levels of AgApoLp-III protein accumulate in the cytoplasm of Plasmodium-invaded cells and AgApoLp-III silencing increases the intensity of P. berghei infection by five fold. There are broad differences in the midgut epithelial responses to Plasmodium invasion between An. gambiae strains. In the G3 strain of An. gambiae AgApoLp-III participates in midgut epithelial defense responses that limit Plasmodium infection.