The Amino Terminus of Herpes Simplex Virus Type 1 Glycoprotein K (gK) Modulates gB-Mediated Virus-Induced Cell Fusion and Virion Egress
| Autor: | Vladimir N. Chouljenko, Konstantin G. Kousoulas, Dmitry V. Chouljenko, Sona Chowdhury, Arun V. Iyer |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Gene Expression Regulation
Viral Signal peptide viruses Immunology Mutant Herpesvirus 1 Human Viral Plaque Assay Biology medicine.disease_cause Microbiology Virus Cell Line Cell Fusion Viral Proteins Viral Envelope Proteins Virology Chlorocebus aethiops medicine Animals Sequence Deletion chemistry.chemical_classification Mutation Cell fusion Genetic Complementation Test Molecular biology Genome Replication and Regulation of Viral Gene Expression Amino acid Herpes simplex virus chemistry Insect Science Glycoprotein |
| Zdroj: | Journal of Virology. 83:12301-12313 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.01329-09 |
| Popis: | Herpes simplex virus type 1 (HSV-1)-induced cell fusion is mediated by viral glycoproteins and other membrane proteins expressed on infected cell surfaces. Certain mutations in the carboxyl terminus of HSV-1 glycoprotein B (gB) and in the amino terminus of gK cause extensive virus-induced cell fusion. Although gB is known to be a fusogenic glycoprotein, the mechanism by which gK is involved in virus-induced cell fusion remains elusive. To delineate the amino-terminal domains of gK involved in virus-induced cell fusion, the recombinant viruses gKDelta31-47, gKDelta31-68, and gKDelta31-117, expressing gK carrying in-frame deletions spanning the amino terminus of gK immediately after the gK signal sequence (amino acids [aa] 1 to 30), were constructed. Mutant viruses gKDelta31-47 and gKDelta31-117 exhibited a gK-null (DeltagK) phenotype characterized by the formation of very small viral plaques and up to a 2-log reduction in the production of infectious virus in comparison to that for the parental HSV-1(F) wild-type virus. The gKDelta31-68 mutant virus formed substantially larger plaques and produced 1-log-higher titers than the gKDelta31-47 and gKDelta31-117 mutant virions at low multiplicities of infection. Deletion of 28 aa from the carboxyl terminus of gB (gBDelta28syn) caused extensive virus-induced cell fusion. However, the gBDelta28syn mutation was unable to cause virus-induced cell fusion in the presence of the gKDelta31-68 mutation. Transient expression of a peptide composed of the amino-terminal 82 aa of gK (gKa) produced a glycosylated peptide that was efficiently expressed on cell surfaces only after infection with the HSV-1(F), gKDelta31-68, DeltagK, or UL20-null virus. The gKa peptide complemented the gKDelta31-47 and gKDelta31-68 mutant viruses for infectious-virus production and for gKDelta31-68/gBDelta28syn-mediated cell fusion. These data show that the amino terminus of gK modulates gB-mediated virus-induced cell fusion and virion egress. |
| Databáze: | OpenAIRE |
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