Herpes simplex virus type 1 glycoprotein L mutants that fail to promote trafficking of glycoprotein H and fail to function in fusion can induce binding of glycoprotein L-dependent anti-glycoprotein H antibodies

The Journal of General Virology
Yuri KlyachkinRobert J Geraghty

Abstract

The herpes simplex virus type 1 (HSV-1) glycoproteins H (gH) and L (gL) form a heterodimer and efficient expression of gH at the virion or cell surface is dependent upon gL. Five carboxy-terminal deletion mutants of gL were created and their ability to interact with and mediate cell-surface expression of gH, to promote binding of gL-dependent anti-gH antibodies and to contribute to cell fusion was analysed. All of the gL mutants bound gH, but only two mutants, containing the amino-terminal 161 or 168 aa of gL, mediated cell-surface expression of gH, and only gL161 and gL168 functioned in cell fusion. The binding of gL to gH, therefore, was not sufficient to ensure gH cell-surface expression and it was not possible to separate the gH-trafficking role of gL from gL function in fusion. Co-expression of gH with any gL mutant conferred binding of the anti-gH mAbs 53S and LP11. If the acquisition of 53S and LP11 binding to gH reflects a gL-induced conformational change, such a change is not sufficient to mediate trafficking of the gH-gL heterodimer.

References

May 28, 2003·Journal of Virology·Tina M CairnsRoselyn J Eisenberg
Jun 7, 2005·The Journal of Biological Chemistry·Stefania GaldieroMassimiliano Galdiero

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Citations

Jul 6, 2010·Nature Structural & Molecular Biology·Tirumala K ChowdaryEkaterina E Heldwein
Feb 15, 2007·Proceedings of the National Academy of Sciences of the United States of America·Ravi P Subramanian, Robert J Geraghty
Dec 15, 2012·The Journal of General Virology·Gen TakahashiYoshiaki Yura
Nov 14, 2014·Journal of Virology·Sebastian W BöhmWalter Fuchs
Jun 23, 2015·Molecular and Biochemical Parasitology·Jean-Philippe SemblatJ Alexandra Rowe

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