Functional Interaction of Human Immunodeficiency Virus Type 1 Vpu and Gag with a Novel Member of the Tetratricopeptide Repeat Protein Family

Callahan, Michael A.; Handley, Mark A.; Lee, Yung-Hui; Talbot, Katrin J.; Wade, Harper, J.; Panganiban, Antonito T.

doi:10.1128/jvi.72.10.8460c-8460c.1998

Cited by 21 publications

(18 citation statements)

References 41 publications

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“…Different levels of TASK-1 expression in various cell lines (Hsu et al, 2004) may explain why Vpu viral enhancement is cell type dependent (Geraghty et al, 1994;Gottlinger et al, 1991;Yao et al, 1992). Furthermore, Vpu and Gag have been shown to bind to viral protein U-binding Protein (Ubp) (Callahan et al, 1998;Geraghty et al, 1994). Ubp may play a role in targeting Gag to the plasma membrane (Handley et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

SARS coronavirus E protein forms cation-selective ion channels

Wilson¹,

Mckinlay²,

et al. 2004

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Severe Acute Respiratory Syndrome (SARS) is caused by a novel coronavirus (SARS-CoV). Coronaviruses including SARS-CoV encode an envelope (E) protein, a small, hydrophobic membrane protein. We report that, in planar lipid bilayers, synthetic peptides corresponding to the SARS-CoV E protein forms ion channels that are more permeable to monovalent cations than to monovalent anions. Affinity-purified polyclonal antibodies recognizing the N-terminal 19 residues of SARS-CoV E protein were used to establish the specificity of channel formation by inhibiting the ion currents generated in the presence of the E protein peptides.

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Section: Discussionmentioning

confidence: 99%

SARS coronavirus E protein forms cation-selective ion channels

Wilson¹,

Mckinlay²,

et al. 2004

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“…The interaction of SGT with the HIV-1 accessory protein vpu and major structural protein gag has previously been reported [25]. The accessory protein vpu has been shown to be essential in regulating viral particle release and viral load [34].…”

Section: A-ha Interacted With Sars-cov M and Ementioning

confidence: 95%

“…Interestingly, both H1-virus infection and transient expression of the NS protein result in modification (most likely phosphorylation) of hSGT [24]. A subsequent study showed that hSGT interacts with HIV-I Vpu and Gag proteins, with Callahan and co-workers postulating that hSGT plays a role in HIV-1 virus assembly or release [25]. Other binding partners of SGT include the growth hormone receptor [26], myostatin [27], heat shock cognate protein [28], and heat shock protein [29], and it has been speculated that SGT could also have a cochaperone function.…”

Section: Identification Of Cellular Proteins Interacting With Sars-comentioning

confidence: 99%

Severe acute respiratory syndrome coronavirus protein 7a interacts with hSGT

Fielding

Gunalan

Tan

et al. 2006

Biochemical and Biophysical Research Communications

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Severe acute respiratory syndrome coronavirus (SARS-CoV) 7a is an accessory protein with no known homologues. In this study, we report the interaction of a SARS-CoV 7a and small glutamine-rich tetratricopeptide repeat-containing protein (SGT). SARS-CoV 7a and human SGT interaction was identified using a two-hybrid system screen and confirmed with interaction screens in cell culture and cellular co-localization studies. The SGT domain of interaction was mapped by deletion mutant analysis and results indicated that tetratricopeptide repeat 2 (aa 125-158) was essential for interaction. We also showed that 7a interacted with SARS-CoV structural proteins M (membrane) and E (envelope), which have been shown to be essential for virus-like particle formation. Taken together, our results coupled with data from studies of the interaction between SGT and HIV-1 vpu indicated that SGT could be involved in the life-cycle, possibly assembly of SARS-CoV.Coronaviruses are members of the Coronaviridae family in the order Nidovirales. This family of viruses contains genomes of ~30 kb that include non-structural (pp1ab) and structural proteins (spike [S], envelope [E], membrane [M], and nucleocapsid [N]), making them the largest known RNA viruses. Interspersed among the structural proteins are group-specific proteins that differ in location and composition between the three coronavirus groups. The group-specific genes are not well characterized and the vast majority has, as yet, no known function. Initial research into the functions of these genes has shown that they are non-essential and dispensable for virus growth in cell culture [1]. However, more recent studies have shown that the accessory genes are required for in vivo infection in the natural host [2-4].Severe acute respiratory syndrome virus (SARS-CoV) encodes for eight potential open reading frames (ORFs), i.e., ORF 3a, 3b,6, 7a, 7b, 8a, 8b, and 9b,. Of these, SARS 3a, 3b, 6, 7a, and 9b have been detected in SARS-CoV infected cells, as well as in clinical samples [8], indicating possible in vivo functions. SARSCoV 7a (previously designated U122 in [9] and X4 in [10]) is the first ORF of subgenomic RNA 7 [6] and has been shown to be expressed inSARS-CoV infected Vero E6 cells [9,11]. It has been shown to localize to the Golgi apparatus and the endoplasmic reticulum (ER) and is recycled between the ER and Golgi complex via the intermediate

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“…Downregulation via interaction with Vpu has also been reported for bTrCP (Margottin et al, 1996) to hand over CD4 to the proteosomal degradation pathway. Also, other host proteins such as Vpu binding protein (UBP) (Callahan et al, 1998), CD74 (Hussain et al, 2008), and CD317 (Bolduan et al, 2011;Neil et al, 2008;van Damme et al, 2008) are "marked" by Vpu for downregulation. Interaction of Vpu with host factors at the site of the plasmamembrane are reported for TASK channels (Hsu et al, 2004) and BST-2/tetherin (also called CD317) (Neil et al, 2008;van Damme et al, 2008).…”

Section: Vpu From Human Immunodeficiency Virus Typementioning

confidence: 99%

Mechanism of Function of Viral Channel Proteins and Implications for Drug Development

Fischer¹,

Wang²,

Schindler³

et al. 2012

International Review of Cell and Molecular Biology

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Viral channel-forming proteins comprise a class of viral proteins which, similar to their host companions, are made to alter electrochemical or substrate gradients across lipid membranes. These proteins are active during all stages of the cellular life cycle of viruses. An increasing number of proteins are identified as channel proteins, but the precise role in the viral life cycle is yet unknown for the majority of them. This review presents an overview about these proteins with an emphasis on those with available structural information. A concept is introduced which aligns the transmembrane domains of viral channel proteins with those of host channels and toxins to give insights into the mechanism of function of the viral proteins from potential sequence identities. A summary of to date investigations on drugs targeting these proteins is given and discussed in respect of their mode of action in vivo.

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Functional Interaction of Human Immunodeficiency Virus Type 1 Vpu and Gag with a Novel Member of the Tetratricopeptide Repeat Protein Family

Cited by 21 publications

References 41 publications

SARS coronavirus E protein forms cation-selective ion channels

SARS coronavirus E protein forms cation-selective ion channels

Severe acute respiratory syndrome coronavirus protein 7a interacts with hSGT

Mechanism of Function of Viral Channel Proteins and Implications for Drug Development

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