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The structural proteins of a porcine paramyxovirus (LPMV)
A Sundqvist1, M Berg, P Hernandez-Jauregui
1Department of Veterinary Microbiology, BMC, Uppsala, Sweden.
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 immunoprecipitated. Selective labelling of LPMV-infected cells with [3H]glucosamine revealed two bands with an Mr 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 Mr 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 Mr of 68K, the nucleoprotein. Two other proteins were also identified, the large protein and the matrix protein, with apparent Mr 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 Mr 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.
Insights
A novel porcine paramyxovirus (LPMV) causes fatal disease in piglets. Protein analysis reveals distinct characteristics, suggesting LPMV is a new Paramyxovirus genus member.
Area of Science:
- Virology
- Animal Pathology
Background:
- Porcine paramyxovirus (LPMV) is a newly identified pathogen causing fatal disease in piglets.
- This virus has been endemic in Mexico since 1980, particularly around La Piedad, Michoacan.
Purpose of the Study:
- To characterize the proteins of the porcine paramyxovirus (LPMV).
- To compare LPMV protein profiles with other known paramyxoviruses.
- To propose a classification for LPMV within the Paramyxoviridae family.
Main Methods:
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to resolve viral proteins.
- Metabolic labeling with [35S]methionine, [3H]glucosamine, and [32P]orthophosphate identified specific viral proteins.
- Immunoprecipitation assays were performed to confirm protein identities.
- Comparative analysis of LPMV protein migration patterns with Newcastle disease virus, bovine parainfluenza 3 virus, and Sendai virus.
Main Results:
- SDS-PAGE resolved at least six [35S]methionine-labeled proteins, with five immunoprecipitated.
- Two viral glycoproteins (hemagglutinin-neuraminidase and fusion proteins) were identified using [3H]glucosamine labeling.
- A phosphoprotein (52K) was detected with [32P]orthophosphate labeling.
- Nucleocapsids contained a major nucleoprotein (68K) and identified large (200K) and matrix (40K) proteins.
- Significant differences in protein migration patterns were observed when compared to other paramyxoviruses.
Conclusions:
- The protein composition of LPMV is distinct from other known paramyxoviruses.
- Based on its protein profile, LPMV is proposed as a novel member of the genus Paramyxovirus.