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Development of the Cellular Immune System of Drosophila Requires the Membrane Attack Complex/Perforin-Like Protein Torso-Like
- Publication Year :
- 2016
- Publisher :
- Genetics Society of America, 2016.
-
Abstract
- Pore-forming members of the membrane attack complex/perforin-like (MACPF) protein superfamily perform well-characterized roles as mammalian immune effectors. For example, complement component 9 and perforin function to directly form pores in the membrane of Gram-negative pathogens or virally infected/transformed cells, respectively. In contrast, the only known MACPF protein in Drosophila melanogaster, Torso-like, plays crucial roles during development in embryo patterning and larval growth. Here, we report that in addition to these functions, Torso-like plays an important role in Drosophila immunity. However, in contrast to a hypothesized effector function in, for example, elimination of Gram-negative pathogens, we find that torso-like null mutants instead show increased susceptibility to certain Gram-positive pathogens such as Staphylococcus aureus and Enterococcus faecalis. We further show that this deficit is due to a severely reduced number of circulating immune cells and, as a consequence, an impaired ability to phagocytose bacterial particles. Together these data suggest that Torso-like plays an important role in controlling the development of the Drosophila cellular immune system.
- Subjects :
- 0301 basic medicine
Cellular immunity
Staphylococcus aureus
Complement Membrane Attack Complex
Investigations
03 medical and health sciences
0302 clinical medicine
Immune system
Phagocytosis
Genetics
Enterococcus faecalis
Animals
Drosophila Proteins
MACPF
biology
Effector
Perforin
Cell Membrane
biology.organism_classification
Cell biology
030104 developmental biology
Drosophila melanogaster
Immune System
Larva
biology.protein
Complement membrane attack complex
030217 neurology & neurosurgery
Drosophila Protein
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....bbff3e90fa83cdaf4dfddb992f5d314c