Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production

Varthakavi, Vasundhara; Smith, Rita M.; Bour, Stephan; Strebel, Klaus; Spearman, Paul

doi:10.1073/pnas.2433165100

Cited by 152 publications

(158 citation statements)

References 34 publications

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“…HIV‐1 Viral protein U (Vpu) 59, 60 is renowned for its role in proteasomal degradation of CD4 61, 62 and enhancement of HIV‐1 release from infected cells 63, 64, 65 in a cell type‐dependent manner 66. In 2008, two independent laboratories showed that cell type‐specific expression of BST‐2 correlates with Vpu‐dependent release of HIV‐1.…”

Section: Viral Antagonists Of Bst‐2 and Neutralization Of Bst‐2 Antivmentioning

confidence: 99%

The role of BST‐2/Tetherin in host protection and disease manifestation

Mahauad‐Fernandez

Okeoma

2015

Immunity, Inflammation and Disease

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Host cells respond to viral infections by activating immune response genes that are not only involved in inflammation, but may also predispose cells to cancerous transformation. One such gene is BST‐2, a type II transmembrane protein with a unique topology that endows it tethering and signaling potential. Through this ability to tether and signal, BST‐2 regulates host response to viral infection either by inhibiting release of nascent viral particles or in some models inhibiting viral dissemination. However, despite its antiviral functions, BST‐2 is involved in disease manifestation, a function linked to the ability of BST‐2 to promote cell‐to‐cell interaction. Therefore, modulating BST‐2 expression and/or activity has the potential to influence course of disease.

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Section: Viral Antagonists Of Bst‐2 and Neutralization Of Bst‐2 Antivmentioning

confidence: 99%

The role of BST‐2/Tetherin in host protection and disease manifestation

Mahauad‐Fernandez

Okeoma

2015

Immunity, Inflammation and Disease

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“…Experimental evidence has also been obtained that Vpu enhances viral budding by interfering with the endogenous potassium channel TASK-1, 34 with sequence homology suggesting that HIV-1 Vpu may have evolved from the Nterminal TM domain of TASK-1 and may function by forming hetero-oligomers with TASK-1 in host cell membranes. Recent experiments indicate that Vpu facilitates viral budding through interactions with host cell proteins that otherwise inhibit viral budding, 35 in particular an integral membrane protein dubbed tetherin, CD317, or BST-2. 36,37 Tetherin tethers budding virions to host cells by linking the viral and host cell membranes.…”

Section: Introductionmentioning

confidence: 99%

Oligomerization state and supramolecular structure of the HIV‐1 Vpu protein transmembrane segment in phospholipid bilayers

et al. 2010

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HIV-1 Vpu is an 81-residue protein with a single N-terminal transmembrane (TM) helical segment that is involved in the release of new virions from host cell membranes. Vpu and its TM segment form ion channels in phospholipid bilayers, presumably by oligomerization of TM helices into a pore-like structure. We describe measurements that provide new constraints on the oligomerization state and supramolecular structure of residues 1-40 of Vpu (Vpu 1-40 ), including analytical ultracentrifugation measurements to investigate oligomerization in detergent micelles, photo-induced crosslinking experiments to investigate oligomerization in bilayers, and solid-state nuclear magnetic resonance measurements to obtain constraints on intermolecular contacts between and orientations of TM helices in bilayers. From these data, we develop molecular models for Vpu TM oligomers. The data indicate that a variety of oligomers coexist in phospholipid bilayers, so that a unique supramolecular structure can not be defined. Nonetheless, since oligomers of various sizes have similar intermolecular contacts and orientations, molecular models developed from our data are most likely representative of Vpu TM oligomers that exist in host cell membranes.

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“…The ability of Vpu to increase progeny virus secretion from infected cells had been attributed initially to ion conductive membrane pore formation characteristic to cells over-expressing Vpu [8]. However, a later report [9] showed that the requirement for Vpu is host…”

Section: Viral Protein U (Vpu)mentioning

confidence: 99%

Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions

Pauza

et al. 2005

Cell Res

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Active host-pathogen interactions take place during infection of human immunodeficiency virus type 1 (HIV-1). Outcomes of these interactions determine the efficiency of viral infection and subsequent disease progression. HIVinfected cells respond to viral invasion with various defensive strategies such as innate, cellular and humoral immune antiviral mechanisms. On the other hand, the virus has also developed various offensive tactics to suppress these host cellular responses. Among many of the viral offensive strategies, HIV-1 viral auxiliary proteins (Tat, Rev, Nef, Vif, Vpr and Vpu) play important roles in the host-pathogen interaction and thus have significant impacts on the outcome of HIV infection. One of the best examples is the interaction of Vif with a host cytidine deaminase APOBEC3G. Although specific roles of other auxiliary proteins are not as well described as Vif-APOBEC3G interaction, it is the goal of this brief review to summarize some of the preliminary findings with the hope to stimulate further discussion and investigation in this exhilarating area of research.

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Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production

Cited by 152 publications

References 34 publications

The role of BST‐2/Tetherin in host protection and disease manifestation

The role of BST‐2/Tetherin in host protection and disease manifestation

Oligomerization state and supramolecular structure of the HIV‐1 Vpu protein transmembrane segment in phospholipid bilayers

Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions

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