Paramyxo and Bunyavirus Group

My research group concentrates mainly on the interaction of the virus with the host, the host responses to infection, and how this relates to host-specificity and the disease process. We are studying two groups of viruses, morbilliviruses (a genus of the Paramyxoviridae family) and nairoviruses, a genus of the Bunyaviridae family.

Within the morbilliviruses we have concentrated primarily on rinderpest virus (RPV), a morbillivirus that causes a fatal disease in cattle and buffalo. The morbilliviruses are an important group of viruses, including viruses that infect man (measles virus), dogs and many wild carnivores (canine distemper virus), and sheep and goats (peste des petits ruminants virus). Current research projects include:

  • comparison of the host response to pathogenic and non-pathogenic viruses using bovine microarrays
  • the mechanisms by which viral proteins of RPV and PPRV block specific host defence mechanisms (primarily the induction and actions of interferons)
  • analysis of the roles specific viral and host proteins have in viral genome and mRNA synthesis.

The nairoviruses, like the morbilliviruses, have a genome consisting of negative-stranded RNA. Unlike morbilliviruses, they are spread solely by certain types of tick. The most well-known nairovirus is Crimea-Congo hemorrhagic fever virus (CCHFV), which causes a fatal disease in humans. We are studying the closely related Nairobi sheep disease virus (NSDV); current areas of research include:

  • developing a system for making recombinant NSDV
  • as with our studies on RPV, studying the way NSDV interferes with host defences in an effort to create a weakened virus that may be useful as a vaccine in the field
  • studying the pathogenesis of NSDV in its natural host
  • investigating the species specificity of disease caused by NSDV by comparing host responses to the virus in sheep and cattle.

Selected Publications:

  • Boxer, EL, Nanda, SK, and Baron, MD (2009). The rinderpest virus non-structural C protein blocks the induction of type 1 interferon. Virology 385: 134-42 [Abstract]. 
  • Nanda, SK, and Baron, MD (2006). Rinderpest virus blocks type I and type II interferon action: role of structural and nonstructural proteins. J. Virol. 80: 7555-68 [Abstract]. 
  • Baron, MD (2005). Wild-type rinderpest virus uses SLAM (CD150) as its receptor. J. Gen. Virol. 86: 1753-7 [Abstract]. 
  • Baron, MD, Banyard, AC, Parida, S, and Barrett, T (2005). The Plowright vaccine strain of rinderpest virus has attenuating mutations in most genes. J. Gen. Virol. 86: 1093-101 [Abstract]. 
  • Brown, DD, Rima, BK, Allen, IV, Baron, MD, Banyard, AC, Barrett, T, and Duprex, WP (2005). Rational attenuation of a morbillivirus by modulating the activity of the RNA-dependent RNA polymerase. J. Virol. 79: 14330-8 [Abstract]. 
  • Sleeman, K, and Baron, MD (2005). The polymerase (L) protein of rinderpest virus interacts with the host cell protein striatin. Virology 332: 225-34 [Abstract]. 
  • Barrett, T, Parida, S, Mohapatra, M, Walsh, P, Das, S, and Baron, MD (2003). Development of new generation rinderpest vaccines. Dev. Biol. 114: 89-97. [Abstract]. 
  • Mioulet, V, Barrett, T, and Baron, MD (2001). Scanning mutagenesis identifies critical residues in the rinderpest virus genome promoter. J. Gen. Virol. 82: 2905-11. [Abstract]. 
  • Sweetman, DA, Miskin, J, and Baron, MD (2001). Rinderpest virus C and V proteins interact with the major (L) component of the viral polymerase. Virology 281: 193-204 [Abstract].