Minute virus of mice small non-structural protein NS2 localizes within, but is not required for the formation of, Smn-associated autonomous parvovirus-associated replication bodies.

@article{Young2005MinuteVO,
  title={Minute virus of mice small non-structural protein NS2 localizes within, but is not required for the formation of, Smn-associated autonomous parvovirus-associated replication bodies.},
  author={Philip J. Young and A Newman and Klaus Thorleif Jensen and Lisa R. Burger and David J. Pintel and Christian L. Lorson},
  journal={The Journal of general virology},
  year={2005},
  volume={86 Pt 4},
  pages={
          1009-14
        }
}
The non-structural proteins NS1 and NS2 of the parvovirus minute virus of mice (MVM) are required for efficient virus replication. It has previously been shown that NS1 and NS2 interact and colocalize with the survival motor neuron (Smn) gene product in novel nuclear structures that are formed late in infection, termed Smn-associated APAR (autonomous parvovirus-associated replication) bodies (SAABs). It is not clear what molecular viral intermediate(s) contribute to SAAB formation. The current… 
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Recruitment of DNA replication and damage response proteins to viral replication centers during infection with NS2 mutants of Minute Virus of Mice (MVM).
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Differential roles for the C-terminal hexapeptide domains of NS2 splice variants during MVM infection of murine cells.
Dynamics and interactions of parvoviral NS1 protein in the nucleus
TLDR
Time‐lapse imaging of infected cells revealed that the intranuclear distribution of NS1‐EYFP evolves dramatically starting from the formation ofNS1 foci and proceeding to a homogenous distribution extending throughout the nucleus.
Mosquito densonucleosis virus non-structural protein NS2 is necessary for a productive infection.
Replication Initiator Protein NS1 of the Parvovirus Minute Virus of Mice Binds to Modular Divergent Sites Distributed throughout Duplex Viral DNA
TLDR
It is shown that NS1 specifically binds to many internal sites, so that all viral fragments of more than ∼170 nucleotides effectively compete for NS1, often binding with higher affinity to these internal sites than to sites in the origins.
Mutations in the Non-Structural Protein-Coding Sequence of Protoparvovirus H-1PV Enhance the Fitness of the Virus and Show Key Benefits Regarding the Transduction Efficiency of Derived Vectors
TLDR
It is hypothesize that the NS2 protein—modified in H1-PM-I, H-1- PM-II, and H 1-DM—may result in the stimulation of some maturation step(s) of the capsid and facilitate virus entry into subsequently infected cells.
An In-Frame Deletion in the NS Protein-Coding Sequence of Parvovirus H-1PV Efficiently Stimulates Export and Infectivity of Progeny Virions
TLDR
It is hypothesized that the internal deletion within the NS2 and/or NS1 protein expressed by Del H-1PV results in the stimulation of some step of the viral life cycle, in particular, a maturation step(s), leading to more efficient nuclear export of infectious viral particles and increased fitness of the virus produced.
Characterising the role of the Cajal Body during a productive adenovirus infection
TLDR
This investigation uncovered the involvement of two CB proteins in two very distinct roles during Ad infection, the first report suggesting a role for CBs in mRNA export and the first reports indicating that SMN may be involved in splicing of virus mRNAs.
Distribution and Dynamics of Transcription-Associated Proteins during Parvovirus Infection
TLDR
Fluorescence recovery after photobleaching showed that the recovery kinetics of nuclear transcription-associated proteins, TATA binding protein, TBP, transcription factor IIB, and poly(A) binding protein nuclear 1 (PABPN1) were different in infected and noninfected cells, pointing to virus-induced alterations in binding dynamics of these proteins.
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References

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TLDR
It is shown that SMN can directly interact in vitro and in vivo with the large nonstructural protein NS1 of the autonomous parvovirus minute virus of mice (MVM), a protein essential for viral replication and a potent transcriptional activator.
The NS2 Proteins of Parvovirus Minute Virus of Mice Are Required for Efficient Nuclear Egress of Progeny Virions in Mouse Cells
TLDR
Analysis of two MVM mutant genomic clones generating NS2 proteins that are unable to interact with Crm1 as a result of amino acid substitutions within their nuclear export signal (NES) sequences indicates that the interaction of MVMpNS2 proteins with the nuclear export receptor Crm 1 plays a critical role at a late stage of the parvovirus life cycle involved in release of progeny viruses.
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TLDR
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TLDR
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TLDR
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ABSTRACT A mutation that disrupts the interaction between the NS2 protein of minute virus of mice and the nuclear export factor Crm1 results in a block to egress of mutant-generated full virions from…
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