Jembrana Disease Virus Tat Can Regulate Human Immunodeficiency Virus (HIV) Long Terminal Repeat-Directed Gene Expression and Can Substitute for HIV Tat in Viral Replication

Chen, Hexin; He, Jun; Fong, Steven E.; Wilcox, G. E.; Wood, Charles

doi:10.1128/jvi.74.6.2703-2713.2000

Cited by 19 publications

(15 citation statements)

References 57 publications

(55 reference statements)

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“…Here we have shown that the JDV Tat domain also supports viral replication through both TAR elements, consistent with a previous report showing that the full-length JDV Tat protein can substitute for HIV-1 Tat in viral replication (12). We have also shown that a hybrid TAR composed of the HIV-1 loop and BIV bulge region (H/B TAR) that is able to bind the HIV-1 and BIV domains in the two binding modes (50) supports replication with any of the Tat proteins.…”

Section: Discussionsupporting

confidence: 78%

“…Another bovine lentivirus, Jembrana disease virus (JDV), encodes a Tat protein closely related to that of BIV (10,13), and interestingly, its RNAbinding domain exhibits chameleon-like behavior that allows recognition of BIV TAR in the ␤-hairpin binding mode or of HIV-1 TAR in the loop-and cyclin T1-dependent binding mode (49). Consistent with this observation is the finding that JDV Tat is able to activate the HIV-1 LTR in addition to its own LTR (12).…”

supporting

confidence: 62%

“…For the TAR replacements, the lower portion of the HIV-1 stem, which is not directly involved in Tat binding, was maintained. By placing the Tat-TAR interactions within the same HIV-1 background and making only small changes to Tat and TAR, we attempted to focus directly on how the mode of RNA binding influences viral replication and to minimize the possible effects of using different, albeit related, viral LTRs or Tat activation domains (12).…”

Section: Resultsmentioning

confidence: 99%

“…1) activated the HIV-1 LTR only when HIV-1 TAR was replaced by BIV TAR (14). The JDV Tat RNA-binding domain is a chameleon that is able to bind to both HIV-1 and BIV TAR elements with high affinity, in cyclin T1-dependent and ␤-hairpin modes, respectively (49), and consequently is able to activate both LTRs (12).…”

Section: Resultsmentioning

confidence: 99%

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Replication of Human Immunodeficiency Viruses Engineered with Heterologous Tat-Transactivation Response Element Interactions

Xie

Wainberg

Frankel

2003

J Virol

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Section: Discussionsupporting

confidence: 78%

supporting

confidence: 62%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Replication of Human Immunodeficiency Viruses Engineered with Heterologous Tat-Transactivation Response Element Interactions

Xie

Wainberg

Frankel

2003

J Virol

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“…We previously described a ''chameleon'' Tat peptide from Jembrana disease virus (JDV) (31,32) that is related to the BIV ARM and is able to bind not only to its cognate JDV TAR but also to HIV and BIV TARs (33). This ARM domain is particularly interestingly for two reasons: first, it behaves as a structural chameleon that binds to HIV and BIV TARs in the HIV Tat and BIV Tat respective binding modes and, second, it binds BIV TAR with even higher affinity than the cognate BIV peptide because of amino acid differences at its C terminus (33).…”

mentioning

confidence: 99%

A single intermolecular contact mediates intramolecular stabilization of both RNA and protein

Calabro

Daugherty

Frankel

2005

Proc. Natl. Acad. Sci. U.S.A.

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An arginine-rich peptide from the Jembrana disease virus (JDV) Tat protein is a structural ''chameleon'' that binds bovine immunodeficiency virus (BIV) or HIV TAR RNAs in two different binding modes, with an affinity for BIV TAR even higher than the cognate BIV peptide. We determined the NMR structure of the JDV Tat-BIV TAR high-affinity complex and found that the C-terminal tyrosine in JDV Tat forms a network of inter-and intramolecular hydrogen bonding and stacking interactions that simultaneously stabilize the ␤-hairpin conformation of the peptide and a base triple in the RNA. A neighboring histidine also appears to help stabilize the peptide conformation. Induced fit binding is recurrent in protein-protein and protein-nucleic acid interactions, and the JDV Tat complex demonstrates how high affinity can be achieved not only by optimization of the binding interface but also by inducing new intramolecular contacts that stabilize each binding partner. Comparison to the cognate BIV Tat peptide-TAR complex shows how such a costabilization mechanism can evolve with only small changes to the peptide sequence. In addition, the bound structure of BIV TAR in the chameleon peptide complex is strikingly similar to the bound conformation of HIV TAR, suggesting new strategies for the development of HIV TAR binding molecules.NMR ͉ RNA structure ͉ RNA-binding domain T he ability of macromolecules to interact with high affinity and specificity is often accompanied by conformational changes in the binding partners (1-4). Flexibility of one or both molecules can contribute to optimization of the binding surfaces and allow binding to multiple partners (5, 6). Numerous examples of conformational adaptability have been observed in protein-protein and protein-nucleic acid interactions, including Ig proteins, which can accommodate a remarkably wide range of binding partners, and the ribosome, where induced-fit binding helps direct its ordered assembly (7-9).In RNA-protein interactions, the arginine-rich motif (ARM) has served as a model system for examining structural mechanisms that underlie induced fit binding (10-12). Studies of ARM peptide-RNA complexes, including the Tat ARM-TAR RNA interactions of several lentiviruses, have shown that the unbound ARMs generally are unfolded and can adopt a variety of conformations upon RNA binding, often with a concomitant change in RNA structure. In the case of HIV Tat, a relatively weak binding ARM peptide remains in an extended conformational when bound to HIV TAR but causes a large conformational change in the RNA, inducing stacking between the two helical stems and formation of a U-A:U base triple (13-23). In the case of bovine immunodeficiency virus (BIV) Tat, a conformational change in BIV TAR also is observed upon binding, but the cognate ARM peptide undergoes a large conformational rearrangement, forming a ␤-hairpin structure that facilitates high-affinity binding through a large set of specific contacts to the RNA (24-29). Despite the striking difference in binding modes of these two...

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Novel bovine lentiviral vectors based on Jembrana disease virus

et al. 2000

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Jembrana Disease Virus Tat Can Regulate Human Immunodeficiency Virus (HIV) Long Terminal Repeat-Directed Gene Expression and Can Substitute for HIV Tat in Viral Replication

Cited by 19 publications

References 57 publications

Replication of Human Immunodeficiency Viruses Engineered with Heterologous Tat-Transactivation Response Element Interactions

Replication of Human Immunodeficiency Viruses Engineered with Heterologous Tat-Transactivation Response Element Interactions

A single intermolecular contact mediates intramolecular stabilization of both RNA and protein

Novel bovine lentiviral vectors based on Jembrana disease virus

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