Abstract
The first interaction of the host and pathogen is initiated by receptor binding, which is mediated by the hemagglutination-neuraminidase (HN) protein of Peste des Petits Ruminants Virus (PPRV) and sialic acid on the host cell membrane. A siRNA-mediated study has confirmed that signal lymphocyte activating molecules (SLAM) could be a putative co-receptor for PPRV. As in all paramyxoviruses, RNA-dependent-RNA polymerase (RdRp) binds to the genome promoter, which is a stretch of the nucleotides before the nucleocapsid open reading frame that initiates transcription in a “stop-start” fashion with the contribution of other viral proteins such as matrix, nucleocapsid, and phosphoprotein. Viral budding occurs through the neuraminidase activity, which cleaves sialic acid residues from the carbohydrate moieties of glycoproteins. Some of these steps in the replication of PPRV are not fully defined yet. However, among morbilliviruses, PPRV is unique in which the HN protein performs both hemagglutination and neuraminidase actions, so better reflected as an HN protein instead of H protein. The virus propagation and pathogenicity is directly proportional to that of the host’s immune response, parasitic infection, the nutritional level of host, and the age of the animal. This chapter highlights recent studies on PPRV replication, transmission, and the factors, both host and non-host, affecting virus propagation in the host.
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Munir, M., Zohari, S., Berg, M. (2013). Replication and Virulence Determinants of Peste des Petits Ruminants Virus. In: Molecular Biology and Pathogenesis of Peste des Petits Ruminants Virus. SpringerBriefs in Animal Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-31451-3_2
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