scholarly journals The three-dimensional structure of thymidine kinase from Herpes simplex virus type 1

FEBS Letters ◽  
1995 ◽  
Vol 368 (2) ◽  
pp. 289-292 ◽  
Author(s):  
Klemens Wild ◽  
Thomas Bohner ◽  
André Aubry ◽  
Gerd Folkers ◽  
Georg E. Schulz
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Thymidine Kinase ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Simplex Virus

scholarly journals Visualization of Tegument-Capsid Interactions and DNA in Intact Herpes Simplex Virus Type 1 Virions

1999 ◽  
Vol 73 (4) ◽  
pp. 3210-3218 ◽  
Author(s):  
Z. Hong Zhou ◽  
Dong Hua Chen ◽  
Joanita Jakana ◽  
Frazer J. Rixon ◽  
Wah Chiu
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Cellular Transport ◽  
Capsid Shell ◽  
Simplex Virus

ABSTRACT Herpes simplex virus type 1 virions were examined by electron cryomicroscopy, allowing the three-dimensional structure of the infectious particle to be visualized for the first time. The capsid shell is identical to that of B-capsids purified from the host cell nucleus, with the exception of the penton channel, which is closed. The double-stranded DNA genome is organized as regularly spaced (∼26 Å) concentric layers inside the capsid. This pattern suggests a spool model for DNA packaging, similar to that for some bacteriophages. The bulk of the tegument is not icosahedrally ordered. However, a small portion appears as filamentous structures around the pentons, interacting extensively with the capsid. Their locations and interactions suggest possible roles for the tegument proteins in regulating DNA transport through the penton channel and binding to cellular transport proteins during viral infection.

scholarly journals The Pattern of Tegument-Capsid Interaction in the Herpes Simplex Virus Type 1 Virion Is Not Influenced by the Small Hexon-Associated Protein VP26

2001 ◽  
Vol 75 (23) ◽  
pp. 11863-11867 ◽  
Author(s):  
Dong-Hua Chen ◽  
Joanita Jakana ◽  
David McNab ◽  
Joyce Mitchell ◽  
Z. Hong Zhou ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Binding Properties ◽  
Potential Binding ◽  
Simplex Virus

ABSTRACT Examination of the three-dimensional structure of intact herpes simplex virus type 1 (HSV-1) virions had revealed that the icosahedrally symmetrical interaction between the tegument and capsid involves the pentons but not the hexons (Z. H. Zhou, D. H. Chen, J. Jakana, F. J. Rixon, and W. Chiu, J. Virol. 73:3210–3218, 1999). To account for this, we postulated that the presence of the small capsid protein, VP26, on top of the hexons was masking potential binding sites and preventing tegument attachment. We have now tested this hypothesis by determining the structure of virions lacking VP26. Apart from the obvious absence of VP26 from the capsids, the structures of the VP26 minus and wild-type virions were essentially identical. Notably, they showed the same tegument attachment patterns, thereby demonstrating that VP26 is not responsible for the divergent tegument binding properties of pentons and hexons.

Mechanism of resistance to acyclovir in thymidine kinase mutants from Herpes simplex virus type 1: a computational approach

2019 ◽  
Vol 38 (7) ◽  
pp. 2116-2127 ◽  
Author(s):  
Vitor Won-Held Rabelo ◽  
Nelilma Correia Romeiro ◽  
Izabel Christina Nunes de Palmer Paixão ◽  
Paula Alvarez Abreu
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Thymidine Kinase ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Computational Approach ◽  
Mechanism Of Resistance ◽  
Simplex Virus
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