scholarly journals A conserved region of the herpes simplex virus type 1 tegument protein VP22 facilitates interaction with the cytoplasmic tail of glycoprotein E (gE)

Virology ◽  
2007 ◽  
Vol 358 (1) ◽  
pp. 192-200 ◽  
Author(s):  
Kevin J. O'Regan ◽  
Michelle A. Bucks ◽  
Michael A. Murphy ◽  
John W. Wills ◽  
Richard J. Courtney
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Cytoplasmic Tail ◽  
Tegument Protein ◽  
Glycoprotein E ◽  
Simplex Virus ◽  
Protein Vp22

scholarly journals Incorporation of the herpes simplex virus type 1 tegument protein VP22 into the virus particle is independent of interaction with VP16

Virology ◽  
2007 ◽  
Vol 369 (2) ◽  
pp. 263-280 ◽  
Author(s):  
Kevin J. O'Regan ◽  
Michael A. Murphy ◽  
Michelle A. Bucks ◽  
John W. Wills ◽  
Richard J. Courtney
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Particle ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Tegument Protein ◽  
Simplex Virus ◽  
Protein Vp22

scholarly journals Herpes Simplex Virus Type 1 Tegument Protein VP22 Induces the Stabilization and Hyperacetylation of Microtubules

1998 ◽  
Vol 72 (8) ◽  
pp. 6448-6455 ◽  
Author(s):  
Gillian Elliott ◽  
Peter O’Hare
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Tegument Protein ◽  
Microtubule Network ◽  
Animal Virus ◽  
Simplex Virus ◽  
Protein Vp22

ABSTRACT The role of the herpes simplex virus type 1 tegument protein VP22 during infection is as yet undefined. We have previously shown that VP22 has the unusual property of efficient intercellular transport, such that the protein spreads from single expressing cells into large numbers of surrounding cells. We also noted that in cells expressing VP22 by transient transfection, the protein localizes in a distinctive cytoplasmic filamentous pattern. Here we show that this pattern represents a colocalization between VP22 and cellular microtubules. Moreover, we show that VP22 reorganizes microtubules into thick bundles which are easily distinguishable from nonbundled microtubules. These bundles are highly resistant to microtubule-depolymerizing agents such as nocodazole and incubation at 4°C, suggesting that VP22 has the capacity to stabilize the microtubule network. In addition, we show that the microtubules contained in these bundles are modified by acetylation, a marker for microtubule stability. Analysis of infected cells by both immunofluorescence and measurement of microtubule acetylation further showed that colocalization between VP22 and microtubules, and induction of microtubule acetylation, also occurs during infection. Taken together, these results suggest that VP22 exhibits the properties of a classical microtubule-associated protein (MAP) during both transfection and infection. This is the first demonstration of a MAP encoded by an animal virus.

scholarly journals Phosphorylation of the Herpes Simplex Virus Type 1 Tegument Protein VP22

Virology ◽  
1996 ◽  
Vol 226 (1) ◽  
pp. 140-145 ◽  
Author(s):  
Gillian Elliott ◽  
Dawn O'reilly ◽  
Peter O'hare
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Tegument Protein ◽  
Simplex Virus ◽  
Protein Vp22
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