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Varicella zoster virus ORF25 gene product: an essential hub protein linking encapsidation proteins and the nuclear egress complex

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Varicella zoster virus ORF25 gene product: an essential hub protein linking encapsidation proteins and the nuclear egress complex. / Vizoso Pinto, Maria G; Pothineni, Venkata R; Haase, Rudolf; Woidy, Mathias; Lotz-Havla, Amelie S; Gersting, Søren W; Muntau, Ania C; Haas, Jürgen; Sommer, Marvin; Arvin, Ann M; Baiker, Armin.

in: J PROTEOME RES, Jahrgang 10, Nr. 12, 02.12.2011, S. 5374-82.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Vizoso Pinto, MG, Pothineni, VR, Haase, R, Woidy, M, Lotz-Havla, AS, Gersting, SW, Muntau, AC, Haas, J, Sommer, M, Arvin, AM & Baiker, A 2011, 'Varicella zoster virus ORF25 gene product: an essential hub protein linking encapsidation proteins and the nuclear egress complex', J PROTEOME RES, Jg. 10, Nr. 12, S. 5374-82. https://doi.org/10.1021/pr200628s

APA

Vizoso Pinto, M. G., Pothineni, V. R., Haase, R., Woidy, M., Lotz-Havla, A. S., Gersting, S. W., Muntau, A. C., Haas, J., Sommer, M., Arvin, A. M., & Baiker, A. (2011). Varicella zoster virus ORF25 gene product: an essential hub protein linking encapsidation proteins and the nuclear egress complex. J PROTEOME RES, 10(12), 5374-82. https://doi.org/10.1021/pr200628s

Vancouver

Vizoso Pinto MG, Pothineni VR, Haase R, Woidy M, Lotz-Havla AS, Gersting SW et al. Varicella zoster virus ORF25 gene product: an essential hub protein linking encapsidation proteins and the nuclear egress complex. J PROTEOME RES. 2011 Dez 2;10(12):5374-82. https://doi.org/10.1021/pr200628s

Bibtex

@article{111139ce7d4e49feacebe10308a2edb5,
title = "Varicella zoster virus ORF25 gene product: an essential hub protein linking encapsidation proteins and the nuclear egress complex",
abstract = "Varicella zoster virus (VZV) ORF25 is a 156 amino acid protein belonging to the approximately 40 core proteins that are conserved throughout the Herpesviridae. By analogy to its functional orthologue UL33 in Herpes simplex virus 1 (HSV-1), ORF25 is thought to be a component of the terminase complex. To investigate how cleavage and encapsidation of viral DNA links to the nuclear egress of mature capsids in VZV, we tested 10 VZV proteins that are predicted to be involved in either of the two processes for protein interactions against each other using three independent protein-protein interaction (PPI) detection systems: the yeast-two-hybrid (Y2H) system, a luminescence based MBP pull-down interaction screening assay (LuMPIS), and a bioluminescence resonance energy transfer (BRET) assay. A set of 20 interactions was consistently detected by at least 2 methods and resulted in a dense interaction network between proteins associated in encapsidation and nuclear egress. The results indicate that the terminase complex in VZV consists of ORF25, ORF30, and ORF45/42 and support a model in which both processes are closely linked to each other. Consistent with its role as a central hub for protein interactions, ORF25 is shown to be essential for VZV replication.",
keywords = "Animals, Base Sequence, Bioluminescence Resonance Energy Transfer Techniques, Capsid, Cell Nucleus, Cloning, Molecular, Cosmids, DNA, Viral, Escherichia coli, Gene Deletion, Genes, Viral, HeLa Cells, Herpesvirus 3, Human, Humans, Immune Sera, Open Reading Frames, Protein Interaction Mapping, Protein Structure, Tertiary, Rabbits, Transfection, Two-Hybrid System Techniques, Viral Proteins, Virus Replication",
author = "{Vizoso Pinto}, {Maria G} and Pothineni, {Venkata R} and Rudolf Haase and Mathias Woidy and Lotz-Havla, {Amelie S} and Gersting, {S{\o}ren W} and Muntau, {Ania C} and J{\"u}rgen Haas and Marvin Sommer and Arvin, {Ann M} and Armin Baiker",
year = "2011",
month = dec,
day = "2",
doi = "10.1021/pr200628s",
language = "English",
volume = "10",
pages = "5374--82",
journal = "J PROTEOME RES",
issn = "1535-3893",
publisher = "American Chemical Society",
number = "12",

}

RIS

TY - JOUR

T1 - Varicella zoster virus ORF25 gene product: an essential hub protein linking encapsidation proteins and the nuclear egress complex

AU - Vizoso Pinto, Maria G

AU - Pothineni, Venkata R

AU - Haase, Rudolf

AU - Woidy, Mathias

AU - Lotz-Havla, Amelie S

AU - Gersting, Søren W

AU - Muntau, Ania C

AU - Haas, Jürgen

AU - Sommer, Marvin

AU - Arvin, Ann M

AU - Baiker, Armin

PY - 2011/12/2

Y1 - 2011/12/2

N2 - Varicella zoster virus (VZV) ORF25 is a 156 amino acid protein belonging to the approximately 40 core proteins that are conserved throughout the Herpesviridae. By analogy to its functional orthologue UL33 in Herpes simplex virus 1 (HSV-1), ORF25 is thought to be a component of the terminase complex. To investigate how cleavage and encapsidation of viral DNA links to the nuclear egress of mature capsids in VZV, we tested 10 VZV proteins that are predicted to be involved in either of the two processes for protein interactions against each other using three independent protein-protein interaction (PPI) detection systems: the yeast-two-hybrid (Y2H) system, a luminescence based MBP pull-down interaction screening assay (LuMPIS), and a bioluminescence resonance energy transfer (BRET) assay. A set of 20 interactions was consistently detected by at least 2 methods and resulted in a dense interaction network between proteins associated in encapsidation and nuclear egress. The results indicate that the terminase complex in VZV consists of ORF25, ORF30, and ORF45/42 and support a model in which both processes are closely linked to each other. Consistent with its role as a central hub for protein interactions, ORF25 is shown to be essential for VZV replication.

AB - Varicella zoster virus (VZV) ORF25 is a 156 amino acid protein belonging to the approximately 40 core proteins that are conserved throughout the Herpesviridae. By analogy to its functional orthologue UL33 in Herpes simplex virus 1 (HSV-1), ORF25 is thought to be a component of the terminase complex. To investigate how cleavage and encapsidation of viral DNA links to the nuclear egress of mature capsids in VZV, we tested 10 VZV proteins that are predicted to be involved in either of the two processes for protein interactions against each other using three independent protein-protein interaction (PPI) detection systems: the yeast-two-hybrid (Y2H) system, a luminescence based MBP pull-down interaction screening assay (LuMPIS), and a bioluminescence resonance energy transfer (BRET) assay. A set of 20 interactions was consistently detected by at least 2 methods and resulted in a dense interaction network between proteins associated in encapsidation and nuclear egress. The results indicate that the terminase complex in VZV consists of ORF25, ORF30, and ORF45/42 and support a model in which both processes are closely linked to each other. Consistent with its role as a central hub for protein interactions, ORF25 is shown to be essential for VZV replication.

KW - Animals

KW - Base Sequence

KW - Bioluminescence Resonance Energy Transfer Techniques

KW - Capsid

KW - Cell Nucleus

KW - Cloning, Molecular

KW - Cosmids

KW - DNA, Viral

KW - Escherichia coli

KW - Gene Deletion

KW - Genes, Viral

KW - HeLa Cells

KW - Herpesvirus 3, Human

KW - Humans

KW - Immune Sera

KW - Open Reading Frames

KW - Protein Interaction Mapping

KW - Protein Structure, Tertiary

KW - Rabbits

KW - Transfection

KW - Two-Hybrid System Techniques

KW - Viral Proteins

KW - Virus Replication

U2 - 10.1021/pr200628s

DO - 10.1021/pr200628s

M3 - SCORING: Journal article

C2 - 21988664

VL - 10

SP - 5374

EP - 5382

JO - J PROTEOME RES

JF - J PROTEOME RES

SN - 1535-3893

IS - 12

ER -