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Review
. 2014 Jan;10(1):e1003851.
doi: 10.1371/journal.ppat.1003851. Epub 2014 Jan 23.

HIV-1 accessory proteins adapt cellular adaptors to facilitate immune evasion

David R Collins  1 , Kathleen L Collins  1
Affiliations
Review

HIV-1 accessory proteins adapt cellular adaptors to facilitate immune evasion

David R Collins et al. PLoS Pathog. 2014 Jan.
No abstract available

PubMed Disclaimer

Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Figure 1
Figure 1. Diagrammatic representation of HIV-1 Nef serving as an adaptor of clathrin adaptor proteins in cellular trafficking pathways.
A. The AP-1 µ1 subunit interacts with a tyrosine residue in the cytoplasmic tail of MHC-I via a tyrosine-binding pocket. This interaction is stabilized by electrostatic interactions between a poly-glutamic acid motif of Nef (− −) and a positively charged patch in AP-1 µ1 (++). A polyproline repeat of Nef (PxxP) further stabilizes the complex by forming a wall of the groove that contains the MHC-I tail. These interactions lead to down-modulation of MHC-I from the cell surface. B. AP complexes interact with Nef via a dileucine motif (ExxLL) in the Nef C-terminal loop. AP complexes bind dileucine motifs at an interface between the AP complex σ and heavy chain subunits (α, β, or γ in AP-2, AP-3, and AP-1 respectively) . Nef utilizes the dileucine trafficking signal to down-modulate a number of host proteins, including CD4.
Figure 2
Figure 2. Diagrammatic representations of HIV-1 Vif, Vpu, and Vpr functioning as adaptors of substrate adaptors in cellular ubiquitination pathways.
A. Vif, in complex with and stabilized by cellular CBF-β, binds to the EloBC/Rbx2/Cullin5 E3 ubiquitin ligase complex and to APOBEC3G to induce its polyubiquitination and degradation. B. Vpu interacts with the Skp1/Cullin/F-Box (SCF) ubiquitin ligase complex via β-TrCP and with target proteins BST-2 or CD4 to induce their ubiquitination and mislocalization. C. Vpr interacts with the DCAF1/DDB1/Rbx1/Cullin4A E3 ubiquitin ligase complex and with UNG2 to induce its polyubiquitination and degradation.
See this image and copyright information in PMC

References

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