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Title: Growth Determination for Genetic Engineered SAT Type Foot-and-Mouth Disease Viruses

item THERON, J
item Rieder, Aida - Elizabeth

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 11/1/2006
Publication Date: 11/26/2006
Citation: Blignaut, B., Maree, F., Theron, J., Rieder, A.E., Vosloo, W. 2006. Growth Determination for Genetic Engineered SAT Type Foot-and-Mouth Disease Viruses.European Study Group on the Molecular Biology of Picornaviruses (EUROPIC) 2006 Meeting, page B10.

Interpretive Summary:

Technical Abstract: Foot-and-mouth disease virus (FMDV) is endemic throughout large parts of Africa where six of the seven serotypes, viz. A, C, O, SAT (South Africa Territories) 1, 2, 3, occur. The SAT types, usually confined to sub-Saharan Africa, show marked genomic and antigenic variation, with the ID-coding sequence appearing inherently more variable. The replication of FMDV is dependent on several factors, including cell entry via receptors, replication of the RNA genome, translation, the correct polyprotein processing by viral encoded proteases, and packaging of the RNA into virions. FMDV utilizes several cellular receptors including four members of the integrin family via a conserved RGD sequence located within the external G-H loop in protein 1D and heparin sulfate proteoglycans. A study of the heterogeneity of the FMDV 3C proteases revealed 32% variant amino acid positions, whilst 57% , 65% and 75% variant amino acids were observed for impact on the ability of the 3C protease to recognize different cleavage sites within the P1 protein, several chimeric viruses were engineered. The external capsid-coding region (1B-1D) of a SAT2 genome length clone was substituted with that of various SAT1, 2 and 3 field isolates. The growth kinetics of these SAT type chimeras were determined in BHK-21 cells and the intergrins expressed by these cells were investigated. Despite the heterogeneity of the 3C-coding region of the SAT viruses, the protease could successfully process the external capsid proteins of the individual chimeras.