An immunologically active chimaeric protein containing herpes simplex virus type 1 glycoprotein D
| Autor: | Roger J. Watson, J H Weis, Lynn W. Enquist, John S. Salstrom |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
viruses
medicine.disease_cause Virus Single-stranded binding protein Viral Proteins Viral Envelope Proteins medicine Escherichia coli Simplexvirus Antigens Viral Infectivity chemistry.chemical_classification Multidisciplinary biology Chemistry Viral Vaccines beta-Galactosidase Herpesvirus glycoprotein B Virology Bacteriophage lambda Herpes simplex virus biology.protein Antibody Glycoprotein Genetic Engineering Plasmids |
| Zdroj: | Nature. 302(5903) |
| ISSN: | 0028-0836 |
| Popis: | Herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2) cause both persistent and latent infections, including recurrent cutaneous disease, lethal neonatal disease, central nervous system disease and other clinical syndromes. Modified live vaccines or conventionally prepared subunit vaccines have generally been unsuccessful in the treatment of HSV-1 and HSV-2 infections from the standpoints of safety and efficacy. It has been established that HSV-1 and HSV-2 infectivity may be neutralized in vitro with antisera directed specifically against each of the four major glycoproteins of the virus (gA/gB, gC, gD and gE) and antisera against glycoprotein gD, of either HSV-1 or HSV-2, are capable of neutralizing both HSV-1 and HSV-2 infectivity in vitro and in vivo. We have previously reported on the identification, DNA sequence and expression at low level in Escherichia coli of the gD gene of HSV-1 strain Patton. Here we describe construction of a hybrid gene encoding a chimaeric protein containing HSV-1 gD, bacteriophage lambda Cro and E. coli beta-galactosidase (gD-beta-gal) protein, which is expressed at high level in E. coli. Moreover, the chimaeric protein elicits antibodies in rabbits that not only immunoprecipitate gD from cells infected with HSV-1 and HSV-2 but also neutralize HSV-1 and HSV-2 infectivity in vitro. |
| Databáze: | OpenAIRE |
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