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Lipidome and proteome of mumps virus

Introduction Mumps virus belongs to Paramyxoviridae family. Paramyxoviruses are surrounded by a lipid envelope containing two glycoproteins having the lead role in cell infection. After replication viruses bud from the host cell membrane, most probably microdomains. So, virus envelope is completely of host cell origin although may differ in lipid composition from the average cell lipid composition [1, 2]. These virus surface structural elements, glycans and lipids, are not encoded by the virus genome and are therefore variable and to some extent host depended, but obviously have an impact on virus biology (e.g. infectivity) and physico-chemical properties (e.g. stability). The aim of this work was to compare the lipidome of two strains of mumps virus derived from two cell substrates and to analyze mumps virus proteome. Methods Mumps viruses (L-Zagreb and Jeryl Lynn strains) grown in chicken embryo fibroblast or Vero cells were purified using sucrose gradient ultracentrifugation. Virus lipids were extracted and separated by 2D-HPTLC. After extraction high-energy CID MALDI-TOF/RTOF-MS was used for identification. Whole virus samples were denaturated and subjected to SDS-PAGE. Proteins were identified after in-gel digestion by MALDI-TOF-MS. Results and Discussion Results of lipid analysis revealed similarity of two mumps virus strains with lipids from the cell line they were derived from. No significant differences were observed between the strains. Interestingly, in viruses derived from Vero cells glycolipids with up to four glycan units were detected and these lipids are not reported so far in viruses [3]. In addition, it was found that mumps virus proteome contains truncated nucleoprotein forms and currently there are no data indicating that such proteins are incorporated in viral capsids, although they have been detected in cell lysates [4]. Function of glycolipids and truncated nucleoprotein forms remains to be determined. Innovative aspects • Mumps virus lipidome and proteome are described for the first time revealing similarity of mumps virus lipids to lipids from the cell line the virus was derived from • Truncated nucleoprotein forms were identified that are reported for the first time incorporated in mumps virus capsid References [1] T. S. Jardetzky, R. A. Lamb, Activation of paramyxovirus membrane fusion and virus entry, Curr. Opin. Virol. 5 (2014) 24. [2] P. Plattet, R. K. Plemper, Envelope protein dynamics in paramyxovirus entry, mBio 4 (2013). [3] M. Lorizate, T. Sachsenheimer, B. Glass, A. Habermann, M. J. Gerl, H.-G. Kräusslich, B. Brügger, Comparative lipidomics analysis of HIV-1 particles and their producer cell membrane in different cell lines, Cell. Microbiol. 15 (2013) 292. [4] N. Liu, W. Song, P. Wang, K-C. Lee, Z. Cai, H. Chen, Identification of unusual truncated forms of nucleocapsid protein in MDCK cells infected by Avian influenza virus (H9N2), Proteomics 10 (2010) 1875.

Mumps virus; Lipidome; Proteome; Mass spectrometry

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