scholarly journals Murine polyomavirus DNA transitions through spatially distinct nuclear replication subdomains during infection

2020 ◽  
Vol 16 (3) ◽  
pp. e1008403
Author(s):  
Douglas K. Peters ◽  
Robert L. Garcea
Keyword(s):  
Murine Polyomavirus

scholarly journals Conformational Changes of Murine Polyomavirus Capsid Proteins Induced by Sialic Acid Binding

2004 ◽  
Vol 279 (40) ◽  
pp. 41573-41579 ◽  
Author(s):  
Michaela Cavaldesi ◽  
Maddalena Caruso ◽  
Olga Sthandier ◽  
Paolo Amati ◽  
Marie Isabelle Garcia
Keyword(s):  
Sialic Acid ◽  
Conformational Changes ◽  
Capsid Proteins ◽  
Sialic Acid Binding ◽  
Murine Polyomavirus

Ganglioside-dependent cell attachment and endocytosis of murine polyomavirus-like particles

FEBS Letters ◽  
2003 ◽  
Vol 555 (2) ◽  
pp. 199-203 ◽  
Author(s):  
Alicia E Smith ◽  
Hauke Lilie ◽  
Ari Helenius
Keyword(s):  
Cell Attachment ◽  
Dependent Cell ◽  
Murine Polyomavirus

scholarly journals A Transformation-Defective Polyomavirus Middle T Antigen with a Novel Defect in PI3 Kinase Signaling

2016 ◽  
Vol 91 (2) ◽  
Author(s):  
Deborah Denis ◽  
Cecile Rouleau ◽  
Brian S. Schaffhausen
Keyword(s):  
Tyrosine Phosphorylation ◽  
Tyrosine Kinases ◽  
T Antigen ◽  
Pi3 Kinase ◽  
Binding Motif ◽  
Wild Type ◽  
Pi3k Activity ◽  
Murine Polyomavirus ◽  
Middle T Antigen

ABSTRACT Middle T antigen (MT), the principal oncoprotein of murine polyomavirus, transforms by association with cellular proteins. Protein phosphatase 2A (PP2A), YAP, Src family tyrosine kinases, Shc, phosphatidylinositol 3-kinase (PI3K), and phospholipase C-γ1 (PLCγ1) have all been implicated in MT transformation. Mutant dl1015, with deletion of residues 338 to 347 in the C-terminal region, has been an enigma, because the basis for its transformation defect has not been apparent. This work probes the dl1015 region of MT. Because the region is proline rich, the hypothesis that it targets Src homology domain 3 (SH3) domains was tested, but mutation of the putative SH3 binding motif did not affect transformation. During this work, two point mutants, W348R and E349K, were identified as transformation defective. Extensive analysis of the E349K mutant is described here. Similar to wild-type MT, the E349K mutant associates with PP2A, YAP, tyrosine kinases, Shc, PI3 kinase, and PLCγ1. The E349K mutant was examined to determine the mechanism for its transformation defect. Assays of cell localization and membrane targeting showed no obvious difference in localization. Src association was normal as assayed by in vitro kinase and MT phosphopeptide mapping. Shc activation was confirmed by its tyrosine phosphorylation. Association of type 1 PI3K with MT was demonstrated by coimmunoprecipitation, showing both PI3K subunits and in vitro activity. Nonetheless, expression of the mutants failed to lead to the activation of two known downstream targets of PI3K, Akt and Rac-1. Strikingly, despite normal association of the E349K mutant with PI3K, cells expressing the mutant failed to elevate phosphatidylinositol (3,4,5)-trisphosphate (PIP3) in mutant-expressing cells. These results indicate a novel unsuspected aspect to PI3K control. IMPORTANCE The gene coding for middle T antigen (MT) is the murine polyomavirus oncogene most responsible for tumor formation. Its study has a history of uncovering novel aspects of mammalian cell regulation. The importance of PI3K activity and tyrosine phosphorylation are two examples of insights coming from MT. This study describes new mutants unable to transform like the wild type that point to novel regulation of PI3K signaling. Previous mutants were defective in PI3K because they failed to bind the enzyme and bring the activity to the membrane. These mutants recruit PI3K activity like the wild type, but fail to elevate the cellular level of PIP3, the product used to signal downstream of PI3K. As a result, they fail to activate either Akt or Rac1, explaining the transformation defect.

scholarly journals NMR Structure of the N-terminal J Domain of Murine Polyomavirus T Antigens

2000 ◽  
Vol 275 (46) ◽  
pp. 36094-36103 ◽  
Author(s):  
Mark V. Berjanskii ◽  
Michael I. Riley ◽  
Anyong Xie ◽  
Valentyna Semenchenko ◽  
William R. Folk ◽  
...  
Keyword(s):  
Nmr Structure ◽  
T Antigens ◽  
Murine Polyomavirus ◽  
J Domain

scholarly journals Murine Polyomavirus Requires the Endoplasmic Reticulum Protein Derlin-2 To Initiate Infection

2006 ◽  
Vol 80 (17) ◽  
pp. 8739-8744 ◽  
Author(s):  
Brendan N. Lilley ◽  
Joanna M. Gilbert ◽  
Hidde L. Ploegh ◽  
Thomas L. Benjamin
Keyword(s):  
Endoplasmic Reticulum ◽  
Viral Genome ◽  
Cellular Membrane ◽  
Dominant Negative ◽  
Hairpin Rna ◽  
Dominant Negative Form ◽  
Endoplasmic Reticulum Protein ◽  
Murine Polyomavirus ◽  
Infection Inhibition ◽  
Negative Form

ABSTRACT The pathways by which viruses enter cells are diverse, but in all cases, infection necessitates the transfer of the viral genome across a cellular membrane. Polyomavirus (Py) particles, after binding to glycolipid and glycoprotein receptors at the cell surface, are delivered to the lumen of the endoplasmic reticulum (ER). The nature and extent of virus disassembly in the ER, how the viral genome is transported to the cytosol and subsequently to the nucleus, and whether any cellular proteins are involved are not known. Here, we identify an ER-resident protein, Derlin-2, a factor implicated in the removal of misfolded proteins from the ER for cytosolic degradation, as a component of the machinery required for mouse Py to establish an infection. Inhibition of Derlin-2 function by expression of either a dominant-negative form of Derlin-2 or a short hairpin RNA that reduces Derlin-2 levels blocks Py infection by 50 to 75%. The block imposed by Derlin-2 inhibition occurs after the virus reaches the ER and can be bypassed by the introduction of Py DNA into the cytosol. These findings suggest a mode of Py entry that involves cytosolic access via the quality control machinery in the ER.

Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment

Nature ◽  
1994 ◽  
Vol 369 (6476) ◽  
pp. 160-163 ◽  
Author(s):  
Thilo Stehle ◽  
Youwei Yan ◽  
Thomas L. Benjamin ◽  
Stephen C. Harrison
Keyword(s):  
Murine Polyomavirus ◽  
Receptor Fragment

Murine polyomavirus-like particles induce maturation of bone marrow-derived dendritic cells and proliferation of T cells

2006 ◽  
Vol 196 (1) ◽  
pp. 31-39 ◽  
Author(s):  
Thomas Bickert ◽  
Gisela Wohlleben ◽  
Marc Brinkman ◽  
Claudia M. Trujillo-Vargas ◽  
Claus Ruehland ◽  
...  
Keyword(s):  
Bone Marrow ◽  
T Cells ◽  
Dendritic Cells ◽  
Murine Polyomavirus

scholarly journals Early Steps of Polyomavirus Entry into Cells

2000 ◽  
Vol 74 (18) ◽  
pp. 8582-8588 ◽  
Author(s):  
Joanna M. Gilbert ◽  
Thomas L. Benjamin
Keyword(s):  
Jc Virus ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Dominant Negative ◽  
Independent Manner ◽  
Caveolin 1 ◽  
Dominant Negative Form ◽  
Murine Polyomavirus ◽  
Dynamin I ◽  
Negative Form

ABSTRACT The mechanism by which murine polyomavirus penetrates cells and arrives at the nucleus, the site of viral replication, is not well understood. Simian virus 40 and JC virus, two closely related members of the polyomavirus subfamily, use caveola- and clathrin-mediated uptake pathways for entry, respectively. The data presented here indicate that compounds that block endocytosis of both caveola- and clathrin-derived vesicles have no effect on polyomavirus infectivity. Polyomavirus does not appear to colocalize with either clathrin light chain or caveolin-1 by immunofluorescence microscopy. Additionally, expression of a dominant-negative form of dynamin I has no effect on polyomavirus uptake and infectivity. Therefore, polyomavirus uptake occurs through a class of uncoated vesicles in a clathrin-, caveolin-1-, and dynamin I-independent manner.

scholarly journals Different roles for two enhancer domains in the organ- and age-specific pattern of polyomavirus replication in the mouse.

1992 ◽  
Vol 12 (8) ◽  
pp. 3628-3635 ◽  
Author(s):  
A Amalfitano ◽  
L G Martin ◽  
M M Fluck
Keyword(s):  
Transcription Factors ◽  
In Situ Hybridization ◽  
Mammary Gland ◽  
Crucial Role ◽  
Specific Pattern ◽  
Neonatal Stage ◽  
Murine Polyomavirus ◽  
A Domains

Viral replication in mice infected with murine polyomavirus strains with novel enhancer rearrangements was analyzed by direct in situ hybridization of whole mouse sections and by hybridization of nucleic acids extracted from a specific set of organs. The enhancer rearrangements included a deletion of the B domain as well as duplications within the A domain. Comparisons between enhancer variants demonstrate that the B domain plays an important role in replication in most organs, in particular in the kidney, at the neonatal stage (days 0 to 7 postbirth). In contrast, the B domain is not required in those organs which can sustain replication in the adult, i.e. mammary gland, skin, and bone (class I organs [J. J. Wirth, A. Amalfitano, R. Gross, M. B. A. Oldstone, and M. M. Fluck, J. Virol. 66:3278-3286, 1992]). Altogether, the results suggest that the B and A domains mediate very different functions in infection of mice, controlling the acute and persistent phases of infection, respectively. A model of mouse infection based on the crucial role of differentially expressed host transcription factors is presented.

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