The structural proteins of a porcine paramyxovirus (LPMV)

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Abstract
The porcine paramyxovirus is a newly identified agent of a fatal disease in piglets, endemic in Mexico since 1980, where it was seen around the town of La Piedad, Michoacan, Mexico (hence LPM virus). At least six [35S]methionine-labelled proteins could be resolved by SDS-PAGE and five of them were clearly immuno-precipitated. Selective labelling of LPMV-infected cells with [3H]glucosamine revealed two bands with an M r of about 66K and 59K, corresponding to the two viral glycoproteins, the haemagglutinin—neuraminidase protein and the fusion protein. Labelling of virus with [32P]orthophosphate disclosed one band with an M r of 52K, corresponding to the phosphoprotein. Analysis of nucleocapsids obtained from purified virus or from a permanently infected cell line revealed one major band with an M r of 68K, the nucleoprotein. Two other proteins were also identified, the large protein and the matrix protein, with apparent M r of about 200K and 40K, respectively. The protein migration pattern of LPMV was compared, by SDS-PAGE, with that of Newcastle disease virus, bovine parainfluenza 3 virus and Sendai virus. Differences in the M r of LPMV proteins and the proteins of these paramyxoviruses were observed. We propose that LPMV should be classified as a novel member of the genus Paramyxovirus.

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