| Range |
≈0.002-0.003 µm^2/sec
|
| Organism |
HIV |
| Reference |
Chojnacki J et al., Envelope glycoprotein mobility on HIV-1 particles depends on the virus maturation state. Nat Commun. 2017 Sep 15 8(1):545. doi: 10.1038/s41467-017-00515-6 p.7 right column top paragraphPubMed ID28916807
|
| Method |
Abstract: "Here, [investigators] determine molecular dynamics of Env on the surface of individual HIV-1 particles using scanning fluorescence correlation spectroscopy on a super-resolution STED [Stimulated emission depletion] microscope." |
| Comments |
P.7 left column bottom paragraph: "HIV-1 surface protein mobility was found to be two orders of magnitude slower than in the plasma membrane where diffusion coefficients of tested proteins were similar to that of many other proteins in the plasma membrane environment [ref 32]. This trend was found to be true irrespective of whether the protein is the essential HIV-1 surface protein Env, externally supplied membrane GPI [glycophosphatidylinositol]-anchored protein GPI-SNAP or host cell protein MHC-I. The general difference between plasma membrane and HIV-1 surface mobility and lack of dependence on virus maturation status for GPI-SNAP and MHC-I indicates that the observed very slow protein diffusion on the virus surface is not caused by direct interactions with underlying virus proteins but rather due to the properties of the viral membrane itself. Thus D ≈ 0.002-0.003 µm^2/s appears to represent a general intrinsic mobility that may be shared by all HIV-1 surface proteins present on the wild-type mature particle." |
| Entered by |
Uri M |
| ID |
114190 |