Phosphorylation of ribosomal proteins by the vaccinia virus B1R protein kinase

Banham, Alison H.; Leader, David P.; Smith, Geoffrey L.

doi:10.1016/0014-5793(93)80614-z

Cited by 33 publications

(28 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, these data strongly suggest that B1R plays an important role in the reduction of CD1d1-mediated antigen presentation following a VV infection. It has been shown that B1R phosphorylates one VVencoded and three host cell proteins [19,20]. The former is the product of the VV H5R gene product, a transcription factor expressed both early and late in the virus life cycle, and is involved in the transcription of VV late genes [14,21].…”

Section: Resultsmentioning

confidence: 99%

Inhibition of CD1d1‐mediated antigen presentation by the vaccinia virus B1R and H5R molecules

et al. 2006

View full text Add to dashboard Cite

Vaccinia virus (VV) has been most commonly used as the vaccine to protect individuals against the causative agent of smallpox (variola virus), but it also uses a number of strategies meant to evade or blunt the host's antiviral immune response. Natural killer T (NKT) cells are a subset of immunoregulatory CD1d‐restricted T lymphocytes believed to bridge the innate and adaptive immune responses. It is shown here that the VV‐encoded molecules, B1R and H5R, play a role in the ability of VV to inhibit CD1d‐mediated antigen presentation to NKT cells. These are the first poxvirus‐encoded molecules identified that can play such a role in the evasion of an important component of the innate immune response.

show abstract

Section: Resultsmentioning

confidence: 99%

Inhibition of CD1d1‐mediated antigen presentation by the vaccinia virus B1R and H5R molecules

et al. 2006

View full text Add to dashboard Cite

show abstract

“…Besides the effects of B1 on BAF and H5, the viral kinase has been shown to phosphorylate two ribosomal proteins, Sa and S2, which may have consequences on the efficiency of viral versus cellular translation (13). In vitro kinase assays have shown that the A30 protein, which is involved in virion morphogenesis, may also be a B1 substrate (139).…”

Section: Poxvirusesmentioning

confidence: 99%

Viral Serine/Threonine Protein Kinases

Jacob

Broeke

Favoreel

2011

J Virol

107

View full text Add to dashboard Cite

Phosphorylation represents one the most abundant and important posttranslational modifications of proteins, including viral proteins. Virus-encoded serine/threonine protein kinases appear to be a feature that is unique to large DNA viruses. Although the importance of these kinases for virus replication in cell culture is variable, they invariably play important roles in virus virulence. The current review provides an overview of the different viral serine/threonine protein kinases of several large DNA viruses and discusses their function, importance, and potential as antiviral drug targets.

show abstract

“…Also, it was impossible to generate a virus lacking the B1R open reading frame, which shows that it is an essential gene even without kinase activity (2), probably because of its ability to modulate other proteins by a direct interaction. So far, the identification of B1R substrates, either viral or cellular, is very limited; among its viral protein substrates is H5R (3), and among the cellular substrates are ribosomal proteins (1,4), BAF (30), and p53, which is hyperphosphorylated, triggering a downregulation of apoptotic signals (37) that could contribute to the survival of infected cells by transiently interfering with the cellular stress response and thus allowing the course of the infection to progress.…”

mentioning

confidence: 99%

Vaccinia Virus B1R Kinase Interacts with JIP1 and Modulates c-Jun-Dependent Signaling

Santos

Blanco

Sevilla

et al. 2006

J Virol

View full text Add to dashboard Cite

Viruses have to adjust to the host cell to guarantee their life cycle and survival. This aspect of the virus-host cell interaction is probably performed by viral proteins, such as serine-threonine kinases, that are present early during infection. Vaccinia virus has an early Ser-Thr kinase, B1R, which, although required for successful viral infection, is poorly characterized regarding its effects on cellular proteins, and thus, its potential contribution to pathogenesis is not known. Signaling by mitogen-activated protein kinase (MAPK) is mediated by the assembly of complexes between these kinases and the JIP scaffold proteins. To understand how vaccinia virus B1R can affect the host, its roles in the cellular signaling by MAPK complexes and c-Jun activation have been studied. Independently of its kinase activity, B1R can interact with the central region of the JIP1 scaffold protein. The B1R-JIP1 complex increases the amount of MAPK bound to JIP1; thus, MKK7 and TAK1 either bind with higher affinity or bind more stably to JIP1, while there is an increase in the phosphorylation state of JNK bound to JIP1. The functional consequence of these more stable interactions is an increase in the activity of transcription factors, such as c-Jun, that respond to these complexes. Furthermore, B1R is also able to directly phosphorylate c-Jun in residues different from those targeted by JNK and, thus, B1R can also cooperate by an independent route in c-Jun activation. Vaccinia virus B1R can thus modulate the signaling of pathways that respond to cellular stress.

show abstract

Phosphorylation of ribosomal proteins by the vaccinia virus B1R protein kinase

Cited by 33 publications

References 34 publications

Inhibition of CD1d1‐mediated antigen presentation by the vaccinia virus B1R and H5R molecules

Inhibition of CD1d1‐mediated antigen presentation by the vaccinia virus B1R and H5R molecules

Viral Serine/Threonine Protein Kinases

Vaccinia Virus B1R Kinase Interacts with JIP1 and Modulates c-Jun-Dependent Signaling

Contact Info

Product

Resources

About