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Immune signaling pathways regulating bacterial and malaria parasite infection of the mosquito Anopheles gambiae.


ABSTRACT: We show that, in the malaria vector Anopheles gambiae, expression of Cecropin 1 is regulated by REL2, an NF-kappaB-like transcription factor orthologous to Drosophila Relish. Through alternative splicing, REL2 produces a full-length (REL2-F) and a shorter (REL2-S) protein isoform lacking the inhibitory ankyrin repeats and death domain. RNA interference experiments show that, in contrast to Drosophila Relish, which responds solely to Gram-negative bacteria, the Anopheles REL2-F and REL2-S isoforms are involved in defense against the Gram-positive Staphylococcus aureus and the Gram-negative Escherichia coli bacteria, respectively. REL2-F also regulates the intensity of mosquito infection with the malaria parasite, Plasmodium berghei. The adaptor IMD shares the same activities as REL2-F. Microarray analysis identified 10 additional genes regulated by REL2, including CEC3, GAM1, and LRIM1.

SUBMITTER: Meister S 

PROVIDER: S-EPMC1183586 | biostudies-literature | 2005 Aug

REPOSITORIES: biostudies-literature

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Immune signaling pathways regulating bacterial and malaria parasite infection of the mosquito Anopheles gambiae.

Meister Stephan S   Kanzok Stefan M SM   Zheng Xue-Li XL   Luna Coralia C   Li Tong-Ruei TR   Hoa Ngo T NT   Clayton John Randall JR   White Kevin P KP   Kafatos Fotis C FC   Christophides George K GK   Zheng Liangbiao L  

Proceedings of the National Academy of Sciences of the United States of America 20050802 32


We show that, in the malaria vector Anopheles gambiae, expression of Cecropin 1 is regulated by REL2, an NF-kappaB-like transcription factor orthologous to Drosophila Relish. Through alternative splicing, REL2 produces a full-length (REL2-F) and a shorter (REL2-S) protein isoform lacking the inhibitory ankyrin repeats and death domain. RNA interference experiments show that, in contrast to Drosophila Relish, which responds solely to Gram-negative bacteria, the Anopheles REL2-F and REL2-S isoform  ...[more]

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