This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Oyan, A M Articles by Crumpacker, C S Search for Related Content PubMed PubMed Citation Articles by Oyan, A M Articles by Crumpacker, C S

Resistance of herpes simplex virus type 2 to neomycin maps to the N-terminal portion of glycoprotein C.

Department of Microbiology and Immunology, Gade Institute, University of Bergen, Norway.

ABSTRACT

Entry of herpes simplex virus (HSV) into cells is believed to be mediated by specific binding of envelope proteins to a cellular receptor. Neomycin specifically blocks this initial step in infection by HSV-1 but not HSV-2. Resistance of HSV-2 to this compound maps to a region of the genome encoding glycoprotein C (gC-2). We have studied the function of gC-2 in the initial interaction of the virus with the host cell, using HSV-2 mutants deleted for gC-2 and gC-2-rescued recombinants. Resistance to neomycin was directly linked to the presence of gC-2 within the viral genome. In addition, deletion of the gC-2 gene caused a marked delay in adsorption to cells relative to the wild-type virus. HSV-1 recombinants containing chimeric gC genes composed of HSV-1 and HSV-2 sequences were used to localize neomycin resistance within the N-terminal 223 amino acids of gC-2. This region of the glycoprotein comprises an important domain responsible for binding of HSV-2 to cell receptors in the presence of neomycin. A gC-2-negative mutant is still infectious, indicating that HSV-2 also has an alternative pathway of adsorption.

This article has been cited by other articles:

• Adamiak, B., Ekblad, M., Bergstrom, T., Ferro, V., Trybala, E. (2007). Herpes Simplex Virus Type 2 Glycoprotein G Is Targeted by the Sulfated Oligo- and Polysaccharide Inhibitors of Virus Attachment to Cells. J. Virol. 81: 13424-13434 [Abstract] [Full Text]  
• Cheshenko, N., Herold, B. C. (2002). Glycoprotein B plays a predominant role in mediating herpes simplex virus type 2 attachment and is required for entry and cell-to-cell spread. J. Gen. Virol. 83: 2247-2255 [Abstract] [Full Text]  
• Trybala, E., Liljeqvist, J.-A., Svennerholm, B., Bergström, T. (2000). Herpes Simplex Virus Types 1 and 2 Differ in Their Interaction with Heparan Sulfate. J. Virol. 74: 9106-9114 [Abstract] [Full Text]