Structural and functional characterization of Aedes aegypti pupal cuticle protein that controls dengue virus infection
© 2023 The Protein Society..
The pupal cuticle protein from Aedes aegypti (AaPC) inhibits dengue virus (DENV) infection; however, the underlying mechanism of this inhibition remains unknown. Here, we report that AaPC is an intrinsically disordered protein and interacts with domain I/II of the DENV envelope protein via residues Asp59, Asp61, Glu71, Asp73, Ser75, and Asp80. AaPC can directly bind to and cause the aggregation of DENV, which in turn blocks virus infection during the virus-cell fusion stage. AaPC may also influence viral recognition and attachment by interacting with human immune receptors DC-SIGN and CD4. These findings enhance our understanding of the role of AaPC in mitigating viral infection and suggest that AaPC is a potential target for developing inhibitors or antibodies to control dengue virus infection.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:32 |
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| Enthalten in: |
Protein science : a publication of the Protein Society - 32(2023), 10 vom: 18. Okt., Seite e4761 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Huang, Qingqing [VerfasserIn] |
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| Links: |
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| Themen: |
Aggregation |
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| Anmerkungen: |
Date Completed 23.10.2023 Date Revised 01.11.2023 published: Print Citation Status MEDLINE |
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| doi: |
10.1002/pro.4761 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM360927092 |
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| 245 | 1 | 0 | |a Structural and functional characterization of Aedes aegypti pupal cuticle protein that controls dengue virus infection |
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| 500 | |a Date Revised 01.11.2023 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © 2023 The Protein Society. | ||
| 520 | |a The pupal cuticle protein from Aedes aegypti (AaPC) inhibits dengue virus (DENV) infection; however, the underlying mechanism of this inhibition remains unknown. Here, we report that AaPC is an intrinsically disordered protein and interacts with domain I/II of the DENV envelope protein via residues Asp59, Asp61, Glu71, Asp73, Ser75, and Asp80. AaPC can directly bind to and cause the aggregation of DENV, which in turn blocks virus infection during the virus-cell fusion stage. AaPC may also influence viral recognition and attachment by interacting with human immune receptors DC-SIGN and CD4. These findings enhance our understanding of the role of AaPC in mitigating viral infection and suggest that AaPC is a potential target for developing inhibitors or antibodies to control dengue virus infection | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Cuticular proteins | |
| 650 | 4 | |a aggregation | |
| 650 | 4 | |a dengue virus | |
| 650 | 4 | |a intrinsically disordered | |
| 650 | 4 | |a structure | |
| 700 | 1 | |a Gavor, Edem |e verfasserin |4 aut | |
| 700 | 1 | |a Tulsian, Nikhil Kumar |e verfasserin |4 aut | |
| 700 | 1 | |a Fan, Jingsong |e verfasserin |4 aut | |
| 700 | 1 | |a Lin, Qingsong |e verfasserin |4 aut | |
| 700 | 1 | |a Mok, Yu Keung |e verfasserin |4 aut | |
| 700 | 1 | |a Kini, R Manjunatha |e verfasserin |4 aut | |
| 700 | 1 | |a Sivaraman, J |e verfasserin |4 aut | |
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