The pattern of tegument-capsid interaction in the herpes simplex virus type 1 virion is not influenced by the small hexon-associated protein VP26.
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.
Chen
D H
DH
Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030, USA.
Jakana
J
J
McNab
D
D
Mitchell
J
J
Zhou
Z H
ZH
Dougherty
M
M
Chiu
W
W
Rixon
F J
FJ
D001483:Base Sequence; D002213:Capsid / Q000502:physiology*; D036022:Capsid Proteins; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D018259:Herpesvirus 1, Human / Q000502:physiology*; D014771:Virion / Q000737:chemistry / Q000502:physiology*
D036022:Capsid Proteins; D017931:DNA Primers; C077409:capsid protein VP26, herpes simplex virus type 1