Summary
Electrophoretic analysis of the polypeptides present in foot-and-mouth disease virus (FMDV) infected cells indicates that the viral ribonucleic acid (RNA), as with other picornaviruses is translated to produce large polypeptide products which are subsequently cleaved into the smaller stable virus proteins (VP) and non-capsid virus proteins (NCVP). The stable genome products and their estimated molecular weights are: NCVP5 (57,000 daltons), NCVP9 (37,500 daltons), NCVP11. (15,500 daltons), VP0 (40,000 daltons), and VP1–3 (each, 28,300 daltons). The similarities of these products compared to poliovirus and encephalomyocarditis virus genome products are discussed.
The presence of guanidine delays the rate of appearance of NCVP5 and reduces the relative amounts of NCVP9 and VP0. Moreover, some genome products show a predilection for the membrane-free 105 ×g cytoplasmic supernatant fraction as compared with the membrane associated 105 ×g pellet fraction. Thus, during a short pulse, NCVP5 appears predominantly in the supernatant fraction before appearing as a major component in both fractions. NCVP2, 3, 5, 6 and VP0 emerge as major components of the 105 ×g supernatant fraction, while the major products associated with the membranous pellet are NCVP5, 9, 10, 11 and the larger polypeptides in the region of NCVP1.
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Vande Woude, G.F., Ascione, R. Translation products of foot-and-mouth disease virus-infected baby hamster kidney cells. Archiv f Virusforschung 45, 259–271 (1974). https://doi.org/10.1007/BF01249689
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DOI: https://doi.org/10.1007/BF01249689