The CLIP-domain serine protease homolog SPCLIP1 regulates complement recruitment to microbial surfaces in the malaria mosquito Anopheles gambiae.
The complement C3-like protein TEP1 of the mosquito Anopheles gambiae is required for defense against malaria parasites and bacteria. Two forms of TEP1 are present in the mosquito hemolymph, the full-length TEP1-F and the proteolytically processed TEP1(cut) that is part of a complex including the le...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS Pathogens |
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24039584/pdf/?tool=EBI |
| _version_ | 1818403976161263616 |
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| author | Michael Povelones Lavanya Bhagavatula Hassan Yassine Lee Aun Tan Leanna M Upton Mike A Osta George K Christophides |
| author_facet | Michael Povelones Lavanya Bhagavatula Hassan Yassine Lee Aun Tan Leanna M Upton Mike A Osta George K Christophides |
| author_sort | Michael Povelones |
| collection | DOAJ |
| description | The complement C3-like protein TEP1 of the mosquito Anopheles gambiae is required for defense against malaria parasites and bacteria. Two forms of TEP1 are present in the mosquito hemolymph, the full-length TEP1-F and the proteolytically processed TEP1(cut) that is part of a complex including the leucine-rich repeat proteins LRIM1 and APL1C. Here we show that the non-catalytic serine protease SPCLIP1 is a key regulator of the complement-like pathway. SPCLIP1 is required for accumulation of TEP1 on microbial surfaces, a reaction that leads to lysis of malaria parasites or triggers activation of a cascade culminating with melanization of malaria parasites and bacteria. We also demonstrate that the two forms of TEP1 have distinct roles in the complement-like pathway and provide the first evidence for a complement convertase-like cascade in insects analogous to that in vertebrates. Our findings establish that core principles of complement activation are conserved throughout the evolution of animals. |
| first_indexed | 2024-12-14T08:32:48Z |
| format | Article |
| id | doaj.art-8167feeb5f9f4491bd0f7b6d02590f1f |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-12-14T08:32:48Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-8167feeb5f9f4491bd0f7b6d02590f1f2022-12-21T23:09:29ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742013-01-0199e100362310.1371/journal.ppat.1003623The CLIP-domain serine protease homolog SPCLIP1 regulates complement recruitment to microbial surfaces in the malaria mosquito Anopheles gambiae.Michael PovelonesLavanya BhagavatulaHassan YassineLee Aun TanLeanna M UptonMike A OstaGeorge K ChristophidesThe complement C3-like protein TEP1 of the mosquito Anopheles gambiae is required for defense against malaria parasites and bacteria. Two forms of TEP1 are present in the mosquito hemolymph, the full-length TEP1-F and the proteolytically processed TEP1(cut) that is part of a complex including the leucine-rich repeat proteins LRIM1 and APL1C. Here we show that the non-catalytic serine protease SPCLIP1 is a key regulator of the complement-like pathway. SPCLIP1 is required for accumulation of TEP1 on microbial surfaces, a reaction that leads to lysis of malaria parasites or triggers activation of a cascade culminating with melanization of malaria parasites and bacteria. We also demonstrate that the two forms of TEP1 have distinct roles in the complement-like pathway and provide the first evidence for a complement convertase-like cascade in insects analogous to that in vertebrates. Our findings establish that core principles of complement activation are conserved throughout the evolution of animals.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24039584/pdf/?tool=EBI |
| spellingShingle | Michael Povelones Lavanya Bhagavatula Hassan Yassine Lee Aun Tan Leanna M Upton Mike A Osta George K Christophides The CLIP-domain serine protease homolog SPCLIP1 regulates complement recruitment to microbial surfaces in the malaria mosquito Anopheles gambiae. PLoS Pathogens |
| title | The CLIP-domain serine protease homolog SPCLIP1 regulates complement recruitment to microbial surfaces in the malaria mosquito Anopheles gambiae. |
| title_full | The CLIP-domain serine protease homolog SPCLIP1 regulates complement recruitment to microbial surfaces in the malaria mosquito Anopheles gambiae. |
| title_fullStr | The CLIP-domain serine protease homolog SPCLIP1 regulates complement recruitment to microbial surfaces in the malaria mosquito Anopheles gambiae. |
| title_full_unstemmed | The CLIP-domain serine protease homolog SPCLIP1 regulates complement recruitment to microbial surfaces in the malaria mosquito Anopheles gambiae. |
| title_short | The CLIP-domain serine protease homolog SPCLIP1 regulates complement recruitment to microbial surfaces in the malaria mosquito Anopheles gambiae. |
| title_sort | clip domain serine protease homolog spclip1 regulates complement recruitment to microbial surfaces in the malaria mosquito anopheles gambiae |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24039584/pdf/?tool=EBI |
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