optosis, tumour immunogenicity and cancer cell death. Consistent with these finding, CDV and MV infections showed promising oncolytic activity in a mouse model of lymphoma carcinomas. The MV-mediated PubMed ID:http://www.ncbi.nlm.nih.gov/pubmed/22189597 anti-tumour response has been characterized as an immune response triggering cell apoptosis in hepatocellular carcinoma and human cutaneous T cell lymphoma. The fact that MV infection in human lymphoma CEM-101 site induces ERresident stress proteins is in line with our own observations linking viral infection-mediated ER stress and CRT exposed at the cell surface. While the molecular mechanisms of oncolytic action mediated by CDV and MV very likely are governed by F/Hinduced syncytium formation and subsequent cell lysis, they are not yet completely elucidated. Thus, it is tempting to speculate that vasostatin on the cell surface of both infected and neighbouring cells may contribute to anti-tumour activity in vivo. In conclusion, we demonstrate that during morbillivirus infection the accumulation of viral surface glycoproteins in the ER induces an ER stress characterized by Ca2+ release, apoptosis and CRT fragmentation. The N-terminal fragment of CRT, vasostatin, is secreted and binds to the cell surface of both infected cells and neighbouring cells. An auto-antibodies response to vasostatin, as described in other disease, might result in neurodegenerative-autoimmunity. Acknowledgments We acknowledge the excellent technical assistance of Liliane Glauser, Arnaud Paradis, Elzbieta Huggler, Catherine Roger and Genevieve ��Metthez. We also thank Professor Daniel Law for the CRT N-terminal antiserum. ~~ The biological function of proteins and cellular metabolism can be significantly modulated through post-translational modifications . Naturally occurring PTMs can either result from enzyme modifications or arise spontaneously. However, PTMs can also be used by bacterial and viral pathogens to compromise critical immune responses and host factors acting against infection. The breakdown of immunological tolerance resulting from such modifications may render endogenous antigens immunogenic. A large array of PTM peptides presented by major histocompatibility complex class I and class II molecules have now been described, and it has been demonstrated that modifications such as cysteinylation, glycosylation or phosphorylation may affect T cell immunoreactivity, resulting in immune escape and/or initiation of autoimmunity. Protein tyrosine nitration is a hallmark of inflammation, and is associated with up-regulated expression of inducible nitric oxide synthase . Nitrotyrosinated proteins are generated in vivo by nitration with peroxynitrite, itself derived from nitric oxide and superoxide which are both released from activated inflammatory cells. NT-proteins may accumulate in apoptotic or inflamed tissues. Indeed, accumulation of the amino acid homolog 39-nitrotyrosine and of NT-proteins has been observed at inflammatory sites in Alzheimer’s disease, arthritis, atherosclerosis, autoimmune diabetes, autoimmune uveitis, celiac disease, ischemiareperfusion injury, multiple sclerosis, Parkinson’s disease, respiratory disease and transplant rejection, as well as in various cancers and infectious diseases. NT self-proteins 
may thus be highly immunogenic, eliciting both humoral and cellular responses. The potential immunogenicity of MHC class II-restricted NT autologous peptides has been previously investigated using the IEk-restricted T cell pigeon/moth cytochrome c as wel