Summary
Aujeszky’s disease virus (ADV), also known as pseudorabies virus (PrV), is an alphaherpesvirus that causes fatal infections in a wide range of animal species. The virus shares a variety of biological properties with human pathogenic herpesviruses like herpes simplex virus or varicella-zoster virus. Although only limited data are available, it seems unlikely that PrV causes disease in immunocompetent humans, but may pose a risk for immunocom-promised patients.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Cheung AK (1989) DNA nucleotide sequence analysis of the immediate-early gene of the Indiana-Funkhauser strain of Pseudorabies virus. J Virol 62: 4763–4766
Dubin G, Socolof E, Frank I, Friedman HM (1991) Herpes simplex virus type 1 Fc receptor protects infected cells from antibody-dependent cellular cytotoxicity. J Virol 65: 7046–7050
Enquist LW (1994) Infection of the mammalian nervous system by Pseudorabies virus (PRV). Semin Virol 5: 221–231
Flynn SJ, Ryan P (1996) The receptor-binding domain of Pseudorabies virus glycoprotein gC is composed of multiple discrete units that are functionally redundant. J Virol 70: 1355–1364
Herold BC, Gerber SI, Belval BJ, Siston AM, Shulman N (1996) Differences in the susceptibility of herpes simplex virus types 1 and 2 to modified heparin compounds suggest serotype differences in viral entry. J Virol 70: 3461–3469
Huemer HP, Larcher C, Coe NE (1992) Pseudorabies virus glycoprotein III derived from virions and infected cells bind to the third component of complement. Virus Res 23: 271–280
Ihara S, Feldman L, Watanabe S, Ben-Porat T (1983) Characterization of the immediate-early functions of Pseudorabies virus. Virology 131: 437–454
Kohl S (1989) The neonatal human’s immune response to herpes simplex virus infection: a critical review. Pediatr Infect Dis J 8: 67–74
Mann SL, Meyers JD, Holmes EX, Corey L (1984) Prevalence and incidence of herpesvirus infections among homosexuelly active men. J Infect Dis 149: 1026
Matthews REF (1982) Classification and nomenclature of viruses. Intervirology 17: 1–200
McNearny TA, Odell C, Holers VM, Spear PG, Atkinson JP (1987) Herpes simplex virus glycoprotein gC-1 and gC-2 bind to the third component of complement and provide protection against complement-mediated neutralization of viral infection. J Exp Med 166: 1525–1535
Morgan C, Rose HM, Mednis B (1968) Electron microscopy of herpes simplex virus I. Entry. J Virol 2: 507–516
Mravak S, Bienzle U, Feldmeier H, Hampl H, Habermehl KO (1987) Lancet 1: 501–502
Nara PL (1982) Porcine herpesvirus 1. In: Olson JR, Krakown S, Blakesless Jr JR (eds) Comparative pathobiology of viral disease. CRC Press, Boca Raton, pp 90–113
Nii S, Morgan C, Rose HM (1968) Electron microscopy of herpes simplex virus II. Sequence of development. J Virol 2: 517–536
Robbins AK, Watson RJ, Whealy ME, Hays WW, Enquist LW (1986) Characterization of a Pseudorabies virus glycoprotein gene with homology to herpes simplex virus type 1 and type 2 glycoprotein C. J Virol 58: 339–347
Sabin AB (1934) The immunological relationships of Pseudorabies (infectious bulbar paralysis, mad itch). Br J Exp Pathol 15: 372–380
Sawitzky D, Hampl H, Habermehl KO (1990) Comparison of heparin-sensitive attachment of Pseudorabies virus and herpes simplex virus type 1 and identification of heparin-binding PrV-glycoproteins. J Gen Virol 71: 1221–1225
Sawitzky D, Hampl H, Habermehl KO (1990) Entry of Pseudorabies virus into CHO cells is blocked at the level of penetration. Arch Virol 115: 309–316
Sawitzky D, Voigt A, Habermehl KO (1993) A peptide-model for the heparin-binding property of Pseudorabies virus glycoprotein III. Med Microbiol Immunol 182: 285–292
Schreurs C, Mettenleiter TC, Zuckermann F, Sugg N, Ben-Porat T (1988) Glycoprotein gIII of Pseudorabies virus is multifunctional. J Virol 62: 2251–2257
Trybala E, Bergström T, Spillmann D, Svennerholm B, Olofsson S, Flynn SJ, Ryan P (1996) Mode of interaction between Pseudorabies virus and heparan sulfate heparin. Virology 218: 35–42
Trybala E, Bergström T, Svennerholm B, Jeansson S, Glorioso JC, Olofsson S (1994) Localization of a functional site on herpes simplex virus type 1 glycoprotein C involved in binding to cell surface heparan sulfate. J Gen Virol 75: 743–752
Whealy ME, Robbins AK, Enquist LW (1988) Pseudorabies virus glycoprotein gIII Is required for efficient virus growth in tissue culture. J Virol 62: 2512–2515
WuDunn D, Spear PG (1989) Initial interaction of herpes simplex virus with cells is binding to heparan sulfate. J Virol 63: 52–58
Zsak L, Mettenleiter TC, Sugg N, Ben-Porat T (1989) Release of Pseudorabies virus from infected cells is controlled by several viral functions and is modulated by cellular components. J Virol 63: 5475–5477
Zuckermann FA, Mettenleiter TC, Schreuers C, Sugg N, Ben-Porat T (1988) Complex between glycoprotein gl and gp63 of Pseudorabies virus: its effect on virus replication. J Virol 62: 4622–4626
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1997 Springer-Verlag Wien
About this paper
Cite this paper
Sawitzky, D. (1997). Transmission, species specificity, and pathogenicity of Aujeszky’s disease virus. In: Kaaden, OR., Czerny, CP., Eichhorn, W. (eds) Viral Zoonoses and Food of Animal Origin. Springer, Vienna. https://doi.org/10.1007/978-3-7091-6534-8_19
Download citation
DOI: https://doi.org/10.1007/978-3-7091-6534-8_19
Publisher Name: Springer, Vienna
Print ISBN: 978-3-211-83014-7
Online ISBN: 978-3-7091-6534-8
eBook Packages: Springer Book Archive