Dynamics of HIV-1 gag processing as revealed by fluorescence lifetime imaging microscopy and single virus tracking / Chen Qian, Annica Flemming, Barbara Müller and Don C. Lamb
The viral polyprotein Gag plays a central role for HIV-1 assembly, release and maturation. Proteolytic processing of Gag by the viral protease is essential for the structural rearrangements that mark the transition from immature to mature, infectious viruses. The timing and kinetics of Gag processing are not fully understood. Here, fluorescence lifetime imaging microscopy and single virus tracking are used to follow Gag processing in nascent HIV-1 particles in situ. Using a Gag polyprotein labelled internally with eCFP, we show that proteolytic release of the fluorophore from Gag is accompanied by an increase in its fluorescence lifetime. By tracking nascent virus particles in situ and analyzing the intensity and fluorescence lifetime of individual traces, we detect proteolytic cleavage of eCFP from Gag in a subset (6.5%) of viral particles. This suggests that for the majority of VLPs, Gag processing occurs with a delay after particle assembly..
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
8 February 2022 2022 |
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| Erschienen: |
8 February 2022 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:14 |
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| Enthalten in: |
Viruses - 14(2022), 2 vom: Feb., Artikel-ID 340, Seite 1-13 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Qian, Chen [VerfasserIn] |
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| Links: |
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| Themen: |
Fluorescence lifetime |
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| Anmerkungen: |
Gesehen am 14.05.2022 |
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| Umfang: |
13 |
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| doi: |
10.3390/v14020340 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a The viral polyprotein Gag plays a central role for HIV-1 assembly, release and maturation. Proteolytic processing of Gag by the viral protease is essential for the structural rearrangements that mark the transition from immature to mature, infectious viruses. The timing and kinetics of Gag processing are not fully understood. Here, fluorescence lifetime imaging microscopy and single virus tracking are used to follow Gag processing in nascent HIV-1 particles in situ. Using a Gag polyprotein labelled internally with eCFP, we show that proteolytic release of the fluorophore from Gag is accompanied by an increase in its fluorescence lifetime. By tracking nascent virus particles in situ and analyzing the intensity and fluorescence lifetime of individual traces, we detect proteolytic cleavage of eCFP from Gag in a subset (6.5%) of viral particles. This suggests that for the majority of VLPs, Gag processing occurs with a delay after particle assembly. | ||
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