Journal
VIRUSES-BASEL
Volume 14, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/v14020340
Keywords
HIV; maturation; gag processing; fluorescence lifetime; single virus tracking
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Funding
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [201269156-SFB 1032]
- LMU via the Center for NanoScience (CeNS)
- BioImaging Network (BIN)
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Researchers used fluorescence lifetime imaging microscopy and single virus tracking to study the processing of Gag protein in HIV-1 particles. They found that, in the majority of viral particles, processing of Gag protein occurs with a delay after particle assembly.
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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