Dynamics of HIV-1 gag processing as revealed by fluorescence lifetime imaging microscopy and single virus tracking

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 processin...

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Hauptverfasser: Qian, Chen (VerfasserIn) , Flemming, Annica (VerfasserIn) , Müller, Barbara (VerfasserIn) , Lamb, Don C. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 8 February 2022
In: Viruses
Year: 2022, Jahrgang: 14, Heft: 2, Pages: 1-13
ISSN:1999-4915
DOI:10.3390/v14020340
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.3390/v14020340
Verlag, lizenzpflichtig, Volltext: https://www.mdpi.com/1999-4915/14/2/340
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Verfasserangaben:Chen Qian, Annica Flemming, Barbara Müller and Don C. Lamb
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Zusammenfassung: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.
Beschreibung:Gesehen am 14.05.2022
Beschreibung:Online Resource
ISSN:1999-4915
DOI:10.3390/v14020340