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.
From: University of Kentucky, Department of Microbiology, Immunology, and Molecular Genetics, 800 Rose Street, UKMC MS415, Lexington, KY 40536-0298, USA.
The Journal of general virology
- Publish Date: Apr 2006
- ISSN: 0022-1317
- Volume: 87
- Issue: Pt 4
- Pages: 759-67
- Medium: Print
- Language: English
- Citation (JAMA): Klyachkin Yuri M, Stoops Krista D, Geraghty Robert J, et al. 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.. J. Gen. Virol. Apr 2006;87:759-67
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.
Mesh Headings (Keywords): Amino Acid Sequence, Animals, Antibodies, Monoclonal, Antibodies, Viral, Cell Fusion, Cricetinae, Dimerization, Gene Expression Regulation, Viral, Herpesvirus 1, Human, Membrane Fusion, Mice, Molecular Sequence Data, Mutation, Rats, Sequence Deletion, Viral Envelope Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 16528023
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