Volume 8, Issue 1, Pages (July 2010)

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Volume 8, Issue 1, Pages 55-67 (July 2010) Immune Evasion and Counteraction of Restriction Factors by HIV-1 and Other Primate Lentiviruses  Frank Kirchhoff  Cell Host & Microbe  Volume 8, Issue 1, Pages 55-67 (July 2010) DOI: 10.1016/j.chom.2010.06.004 Copyright © 2010 Elsevier Inc. Terms and Conditions

Figure 1 Genomic Organization of Lentiviruses The organization of the consensus endogenous RELIK and pSIVgml proviral genomes is shown in comparison to that of other infectious lentiviruses. RELIK, rabbit endogenous lentivirus type K; FIV, feline immunodeficiency virus; OMVV, ovine maedi-visna virus; pSIVgml, gray mouse lemur prosimian immunodeficiency virus. Question marks indicate the possible presence of short, spliced Rev and Tat exons. Cell Host & Microbe 2010 8, 55-67DOI: (10.1016/j.chom.2010.06.004) Copyright © 2010 Elsevier Inc. Terms and Conditions

Figure 2 Host Restriction Factors and Their Viral Antagonists As schematically indicated, TRIM5α (T5α) interacts with incoming HIV-1 capsids and may induce accelerated uncoating by proteasomal degradation. Vif binds to a cullin 5-based ubiquitin ligase complex and to APOBEC3G (3G) to induce the degradation of the restriction factor in proteasomes. Without Vif, APOBEC3G is incorporated into budding virions and causes lethal G-to-A hypermutations of the retroviral genome in the next round of infection. Tetherin inhibits the release of mature viral particles from the cell surface and is antagonized by the Vpu protein. The exact mechanism remains to be defined but most likely involves direct interaction and β-TrCP2-dependent degradation of tetherin, leading to its sequestration from budding virions. Cell Host & Microbe 2010 8, 55-67DOI: (10.1016/j.chom.2010.06.004) Copyright © 2010 Elsevier Inc. Terms and Conditions

Figure 3 Schematic Presentation of Selected Nef Functions Nef downmodulates HLA molecules, CD4, CD28, CXCR4, and CD3 from the surface of infected CD4+ T cells by recruiting them to the endocytic machinery via interactions with adaptor protein 2 (AP2) complexes or by rerouting them to endosomes. These Nef functions reduce CTL lysis, suppress cell migration, facilitate virus release, and modulate signal transduction by the immunological synapse. Furthermore, Nef interacts with cellular kinases and induces downstream signaling events to modulate T cell activation; to induce rearrangements of the actin skeleton; to activate NF-AT, NF-κB, and AP-1; and to induce the efficient transcription of the viral LTR promoter, as well as of cellular genes, including those encoding inflammatory cytokines, activation markers, and death receptors. Nef also directly enhances the infectivity of progeny virions. As indicated by green boxes, SIVagm and SIVsmm Nef alleles are more effective than those of HIV-1 in modulating CD28 and CXCR4 and, in addition, also downregulate CD3. Thus, in contrast to HIV-1 Nefs, they prevent the formation of the immune synapse and not just deregulate it. As indicated by the orange box, cells expressing HIV-1 Nefs express higher levels of death receptors and inflammatory cytokines than those expressing SIVsmm or SIVagm Nef proteins. Modified from Arhel and Kirchhoff, 2009. Cell Host & Microbe 2010 8, 55-67DOI: (10.1016/j.chom.2010.06.004) Copyright © 2010 Elsevier Inc. Terms and Conditions

Figure 4 Tetherin-Driven Evolution of Vpu and Nef Function and the Emergence of HIV-1 SIVcpz represents a recombinant of the precursors of viruses nowadays found in red-capped mangabeys and Cercopithecus monkeys and was transmitted to humans and gorillas. Vpu was first acquired by a common precursor of SIVgsn/mus/mon and then transferred from monkeys to apes and to humans by zoonotic primate lentiviral transmissions. The events that led to the emergence of pandemic HIV-1 group M strains are indicated by thick lines. Nef-mediated tetherin antagonism is indicated by blue and Vpu-mediated tetherin antagonism by red lines, respectively. +, active; (+), poorly active; −, inactive; ?, unknown; n.a., not applicable because these viruses do not have a vpu gene. Adapted from Sauter et al., 2009. Cell Host & Microbe 2010 8, 55-67DOI: (10.1016/j.chom.2010.06.004) Copyright © 2010 Elsevier Inc. Terms and Conditions