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Journal of Virology, December 2009, p. 12301-12313, Vol. 83, No. 23
0022-538X/09/$08.00+0     doi:10.1128/JVI.01329-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The Amino Terminus of Herpes Simplex Virus Type 1 Glycoprotein K (gK) Modulates gB-Mediated Virus-Induced Cell Fusion and Virion Egress{triangledown}

Vladimir N. Chouljenko, Arun V. Iyer, Sona Chowdhury, Dmitry V. Chouljenko, and Konstantin G. Kousoulas*

Division of Biotechnology and Molecular Medicine and Department of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana 70803

Received 28 June 2009/ Accepted 21 September 2009

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 gK{Delta}31-47, gK{Delta}31-68, and gK{Delta}31-117, 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 gK{Delta}31-47 and gK{Delta}31-117 exhibited a gK-null ({Delta}gK) 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 gK{Delta}31-68 mutant virus formed substantially larger plaques and produced 1-log-higher titers than the gK{Delta}31-47 and gK{Delta}31-117 mutant virions at low multiplicities of infection. Deletion of 28 aa from the carboxyl terminus of gB (gB{Delta}28syn) caused extensive virus-induced cell fusion. However, the gB{Delta}28syn mutation was unable to cause virus-induced cell fusion in the presence of the gK{Delta}31-68 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), gK{Delta}31-68, {Delta}gK, or UL20-null virus. The gKa peptide complemented the gK{Delta}31-47 and gK{Delta}31-68 mutant viruses for infectious-virus production and for gK{Delta}31-68/gB{Delta}28syn-mediated cell fusion. These data show that the amino terminus of gK modulates gB-mediated virus-induced cell fusion and virion egress.

* Corresponding author. Mailing address: Division of Biotechnology and Molecular Medicine and Department of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803. Phone: (225) 578-9682. Fax: (225) 578-9701. E-mail: vtgusk{at}lsu.edu

{triangledown} Published ahead of print on 30 September 2009.

Journal of Virology, December 2009, p. 12301-12313, Vol. 83, No. 23
0022-538X/09/$08.00+0     doi:10.1128/JVI.01329-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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