The cytoplasmic tail of herpes simplex virus envelope glycoprotein D binds to the tegument protein VP22 and to capsids.
Herpes simplex virus (HSV) capsids assemble, mature and package their viral genome in the nucleoplasm. They then exit the nucleus into the cytoplasm, where they acquire their final tegument and envelope. The molecular mechanism of cytoplasmic envelopment is unclear, but evidence suggests that the viral glycoprotein tails play an important role in the recruitment of tegument and capsids at the final envelopment site. However, due to redundancy in protein-protein interactions among the viral glycoproteins, genetic analysis of the role of individual glycoproteins in assembly has been difficult. To overcome this problem, a glutathione S-transferase fusion protein-binding assay was used in this study to test the interaction between the cytoplasmic tail of one specific viral glycoprotein, gD, and tegument proteins. The study demonstrated that the 38 kDa tegument protein VP22 bound specifically to the gD tail. This association was dependent on arginine and lysine residues at positions 5 and 6 in the gD tail. In addition, HSV-1 capsids bound the gD tail and exhibited a similar sequence dependence. It is concluded that VP22 may serve as a linker protein, mediating the interaction of the HSV capsid with gD.
Chi
Jung Hee I
JHI
Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Harley
Carol A
CA
Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Mukhopadhyay
Aparna
A
Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Wilson
Duncan W
DW
Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000235:genetics; D019556:COS Cells; D002213:Capsid / Q000378:metabolism* / Q000648:ultrastructure; D002522:Chlorocebus aethiops; D003593:Cytoplasm / Q000821:virology; D008239:Lysine / Q000235:genetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009154:Mutation; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D018139:Simplexvirus / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000737:chemistry / Q000378:metabolism*; D019065:Virus Assembly
D011993:Recombinant Fusion Proteins; D014759:Viral Envelope Proteins; D015678:Viral Structural Proteins; C039447:glycoprotein D, Human herpesvirus 1; C073413:herpes simplex virus type 1 protein VP22; D001120:Arginine; D008239:Lysine