Membrane Attack Complex/Perforin domain-containing proteins in a dual-species transcriptome of caenogastropoda Littorina littorea and its trematode parasite Himasthla elongata.
The MACPF domain-containing proteins potentially able to build a transmembrane pore structure are found in the transcriptome of a common periwinkle kidney loaded with trematode rediae. Two homologs of mammalian Macrophage expressed gene 1 (Mpeg1), LlMpeg1-1 and LIMpeg1-2, share similar domain structure with the only difference such as LIMpeg1-2 transcript lacks of a C-terminal transmembrane helix. Expression of membrane-anchored protein LlMpeg1-1 is similar in kidneys of naturally infected with trematode Himasthla elongata and uninfected snails. The expression of the second soluble LIMpeg1-2 protein is 4-fold upregulated under infection. The third MACPF protein found in Littorina littorea kidney is homologous with Perivitellin - 2 67 kDa subunit named LlPV2-67 and the expression of the transcript is 3-fold upregulated in the kidney of infected snails. The last two molecules are candidate effectors that may participate in the immune response of common periwinkles to trematode infestation. A single parasite-expressed MACPF-like protein was recorded from the transcriptome of Himasthla elongata.
Institute of Evolutionary Physiology and Biochemistry of the Russian Academy of Sciences (IEPhB RAS), St-Petersburg, Russia. Electronic address: agorbushin@gmail.com.
Alexander M
AM
Gorbushin
D000818:Animals; D015938:Complement Membrane Attack Complex / Q000235:genetics* / Q000378:metabolism; D054353:Perforin / Q000235:genetics* / Q000378:metabolism; D000072417:Protein Domains; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D012908:Snails / Q000235:genetics* / Q000469:parasitology*; D059467:Transcriptome; D014200:Trematoda / Q000235:genetics / Q000502:physiology*
D015938:Complement Membrane Attack Complex; D054353:Perforin
Effector immune molecules; Innate immunity; Mollusk/trematode interactions; Proto-complement system