A conserved carboxy-terminal domain in the major tegument structural protein VP22 facilitates virion packaging of a chimeric protein during productive herpes simplex virus 1 infection.
Recombinant virus HSV-1(RF177) was previously generated to examine tegument protein VP22 function by inserting the GFP gene into the gene encoding VP22. During a detailed analysis of this virus, we discovered that RF177 produces a novel fusion protein between the last 15 amino acids of VP22 and GFP, termed GCT-VP22. Thus, the VP22 carboxy-terminal specific antibody 22-3 and two anti-GFP antibodies reacted with an approximately 28 kDa protein from RF177-infected Vero cells. GCT-VP22 was detected at 1 and 3 hpi. Examination of purified virions indicated that GCT-VP22 was incorporated into RF177 virus particles. These observations imply that at least a portion of the information required for virion targeting is located in this domain of VP22. Indirect immunofluorescence analyses showed that GCT-VP22 also localized to areas of marginalized chromatin during RF177 infection. These results indicate that the last fifteen amino acids of VP22 participate in virion targeting during HSV-1 infection.
Schlegel
Elisabeth F M
EF
Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10029-6574, USA.
Blaho
John A
JA
D000595:Amino Acid Sequence; D000818:Animals; D002522:Chlorocebus aethiops; D017124:Conserved Sequence; D006561:Herpes Simplex / Q000821:virology*; D018259:Herpesvirus 1, Human / Q000235:genetics / Q000502:physiology*; D017434:Protein Structure, Tertiary / Q000502:physiology; D011995:Recombination, Genetic; D014709:Vero Cells; D015678:Viral Structural Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D019065:Virus Assembly
D015678:Viral Structural Proteins; C073413:herpes simplex virus type 1 protein VP22