Antiviral activity of a single-domain antibody immunotoxin binding to glycoprotein D of herpes simplex virus 2.
Antimicrob Agents Chemother
; 59(1): 527-35, 2015 Jan.
Article
en En
| MEDLINE
| ID: mdl-25385102
ABSTRACT
Despite years of research dedicated to preventing the sexual transmission of herpes simplex virus 2 (HSV-2), there is still no protective vaccine or microbicide against one of the most common sexually transmitted infections in the world. Using a phage display library constructed from a llama immunized with recombinant HSV-2 glycoprotein D, we identified a single-domain antibody VHH, R33, which binds to the viral surface glycoprotein D. Although R33 does not demonstrate any HSV-2 neutralization activity in vitro, when expressed with the cytotoxic domain of exotoxin A, the resulting immunotoxin (R33ExoA) specifically and potently kills HSV-2-infected cells, with a 50% neutralizing dilution (IC50) of 6.7 nM. We propose that R33ExoA could be used clinically to prevent transmission of HSV-2 through killing of virus-producing epithelial cells during virus reactivation. R33 could also potentially be used to deliver other cytotoxic effectors to HSV-2-infected cells.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Antivirales
/
Proteínas del Envoltorio Viral
/
Herpesvirus Humano 2
/
Anticuerpos de Dominio Único
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
Antimicrob Agents Chemother
Año:
2015
Tipo del documento:
Article
País de afiliación:
Estados Unidos