scholarly journals The VP2/VP3 Minor Capsid Protein of Simian Virus 40 Promotes thein VitroAssembly of the Major Capsid Protein VP1 into Particles

2006 ◽  
Vol 281 (15) ◽  
pp. 10164-10173 ◽  
Author(s):  
Masa-aki Kawano ◽  
Takamasa Inoue ◽  
Hiroko Tsukamoto ◽  
Tatsuya Takaya ◽  
Teruya Enomoto ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Minor Capsid Protein ◽  
Capsid Protein Vp1

scholarly journals Analysis of a nuclear localization signal of simian virus 40 major capsid protein Vp1.

1996 ◽  
Vol 70 (2) ◽  
pp. 1317-1322 ◽  
Author(s):  
N Ishii ◽  
N Minami ◽  
E Y Chen ◽  
A L Medina ◽  
M M Chico ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Major Capsid Protein ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Localization Signal ◽  
Capsid Protein Vp1

The coordinating role of the human norovirus minor capsid protein VP2 is essential to functional change and nuclear localization of the major capsid protein VP1

2019 ◽  
Vol 164 (4) ◽  
pp. 1173-1180 ◽  
Author(s):  
Zhili Liu ◽  
Min Zhang ◽  
Zhen Shen ◽  
Huifen Chen ◽  
Wanju Zhang ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Nuclear Localization ◽  
Major Capsid Protein ◽  
Functional Change ◽  
Human Norovirus ◽  
Minor Capsid Protein ◽  
Capsid Protein Vp1

scholarly journals The Abundant Nuclear Enzyme PARP Participates in the Life Cycle of Simian Virus 40 and Is Stimulated by Minor Capsid Protein VP3

2003 ◽  
Vol 77 (7) ◽  
pp. 4273-4282 ◽  
Author(s):  
Ariela Gordon-Shaag ◽  
Yael Yosef ◽  
Mahmoud Abd El-Latif ◽  
Ariella Oppenheim
Keyword(s):  
Amino Acids ◽  
Life Cycle ◽  
Capsid Protein ◽  
Membrane Integrity ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Capsid Proteins ◽  
Dependent Manner ◽  
Minor Capsid Protein ◽  
Stimulation Of

ABSTRACT The abundant nuclear enzyme poly(ADP-ribose) polymerase (PARP) functions in DNA damage surveillance and repair and at the decision between apoptosis and necrosis. Here we show that PARP binds to simian virus 40 (SV40) capsid proteins VP1 and VP3. Furthermore, its enzymatic activity is stimulated by VP3 but not by VP1. Experiments with purified mutant proteins demonstrated that the PARP binding domain in VP3 is localized to the 35 carboxy-terminal amino acids, while a larger peptide of 49 amino acids was required for full stimulation of its activity. The addition of 3-aminobenzamide (3-AB), a known competitive inhibitor of PARP, demonstrated that PARP participates in the SV40 life cycle. The titer of SV40 propagated on CV-1 cells was reduced by 3-AB in a dose-dependent manner. Additional experiments showed that 3-AB did not affect viral DNA replication or capsid protein production. PARP did not modify the viral capsid proteins in in vitro poly(ADP-ribosylation) assays, implying that it does not affect SV40 infectivity. On the other hand, it greatly reduced the magnitude of the host cytopathic effects, a hallmark of SV40 infection. Additional experiments suggested that the stimulation of PARP activity by VP3 leads the infected cell to a necrotic pathway, characterized by the loss of membrane integrity, thus facilitating the release of mature SV40 virions from the cells. Our studies identified a novel function of the minor capsid protein VP3 in the recruitment of PARP for the SV40 lytic process.

scholarly journals Cell-Free Translation of Messenger RNA of Simian Virus 40: Synthesis of the Major Capsid Protein

1974 ◽  
Vol 71 (2) ◽  
pp. 302-306 ◽  
Author(s):  
C. L. Prives ◽  
H. Aviv ◽  
B. M. Paterson ◽  
B. E. Roberts ◽  
S. Rozenblatt ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Messenger Rna ◽  
Major Capsid Protein ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Free Translation

scholarly journals Simian Virus 40 Assembly, Studied by Temperature-Induced Conformational Changes in Capsid Protein VP1

1986 ◽  
Vol 49 (1) ◽  
pp. 38-40 ◽  
Author(s):  
Minou Bina ◽  
Veronica Blasquez ◽  
Christine Ambrose
Keyword(s):  
Capsid Protein ◽  
Conformational Changes ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Capsid Protein Vp1

Synthesis of the tumour antigen and the major capsid protein of simian virus 40 in a cell-free system derived from Escherichia coli

1976 ◽  
Vol 108 (2) ◽  
pp. 361-379 ◽  
Author(s):  
Jack F. Greenblatt ◽  
Bernard Allet ◽  
Roger Weil ◽  
Cyrus Ahmad-Zadeh
Keyword(s):  
Escherichia Coli ◽  
Capsid Protein ◽  
Major Capsid Protein ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Tumour Antigen ◽  
Free System ◽  
Cell Free System ◽  
A Cell

Simian virus 40 structural proteins: Amino-terminal sequence of the major capsid protein

Virology ◽  
1974 ◽  
Vol 60 (2) ◽  
pp. 584-587 ◽  
Author(s):  
Elias Lazarides ◽  
James G Files ◽  
Klaus Weber
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Structural Proteins ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Amino Terminal Sequence

scholarly journals Cytomegalovirus Assembly Protein Precursor and Proteinase Precursor Contain Two Nuclear Localization Signals That Mediate Their Own Nuclear Translocation and That of the Major Capsid Protein

1998 ◽  
Vol 72 (10) ◽  
pp. 7722-7732 ◽  
Author(s):  
Scott M. Plafker ◽  
Wade Gibson
Keyword(s):  
Capsid Protein ◽  
Nuclear Localization ◽  
Major Capsid Protein ◽  
Nuclear Translocation ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Protein Precursor ◽  
Nuclear Localization Signals ◽  
Carboxy Terminal

ABSTRACT The cytomegalovirus (CMV) assembly protein precursor (pAP) interacts with the major capsid protein (MCP), and this interaction is required for nuclear translocation of the MCP, which otherwise remains in the cytoplasm of transfected cells (L. J. Wood et al., J. Virol. 71:179–190, 1997). We have interpreted this finding to indicate that the CMV MCP lacks its own nuclear localization signal (NLS) and utilizes the pAP as an NLS-bearing escort into the nucleus. The CMV pAP amino acid sequence has two clusters of basic residues (e.g., KRRRER [NLS1] and KARKRLK [NLS2], for simian CMV) that resemble the simian virus 40 large-T-antigen NLS (D. Kalderon et al., Cell 39:499–509, 1984) and one of these (NLS1) has a counterpart in the pAP homologs of other herpesviruses. The work described here establishes that NLS1 and NLS2 are mutually independent NLS that can act (i) in cisto translocate pAP and the related proteinase precursor (pNP1) into the nucleus and (ii) in trans to transport MCP into the nucleus. By using combinations of NLS mutants and carboxy-terminal deletion constructs, we demonstrated a self-interaction of pAP and cytoplasmic interactions of pAP with pNP1 and of pNP1 with itself. The relevance of these findings to early steps in capsid assembly, the mechanism of MCP nuclear transport, and the possible cytoplasmic formation of protocapsomeric substructures is discussed.

scholarly journals Epitopes on the major capsid protein of simian virus 40

1989 ◽  
Vol 264 (5) ◽  
pp. 2665-2671
Author(s):  
L M Babé ◽  
K Brew ◽  
S E Matsuura ◽  
W A Scott
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
Simian Virus 40 ◽  
Simian Virus
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