Abstract
Accurate antiviral humoral and cellular immune responses require prior recognition of antigenic peptides presented by human leukocyte antigen (HLA) class I and II molecules on the surface of antigen-presenting cells. Both the helper and the cytotoxic immune responses are critical for the control and the clearance of human respiratory syncytial virus (HRSV) infection, which is a significant cause of morbidity and mortality in infected pediatric, immunocompromised and elderly populations. In this article we review the immunoproteomics studies which have defined the general antigen processing and presentation rules that determine both the immunoprevalence and the immunodominance of the cellular immune response to HRSV. Mass spectrometry and functional analyses have shown that the HLA class I and II cellular immune responses against HRSV are mainly focused on three viral proteins: fusion, matrix, and nucleoprotein. Thus, these studies have important implications for vaccine development against this virus, since a vaccine construct including these three relevant HRSV proteins could efficiently stimulate the major components of the adaptive immune system: humoral, helper, and cytotoxic effector immune responses.
Highlights
Human respiratory syncytial virus (HRSV) [1], a member of the Pneumoviridae family of the order Mononegavirales, is the major cause of severe lower respiratory tract illnesses, such as pneumonia and bronchiolitis, in newborns and young children [2,3,4]
Several immunoproteomics studies performed in our laboratory have identified the target viral proteins and the ligands and epitopes presented by several common human leukocyte antigen (HLA) class I and II alleles against which the cellular immune responses are focused during HRSV infection
This virus remains one of the pathogens deemed most important for vaccine development [57], as is shown by the fact that in the last 50 years several efforts have been made toward HRSV vaccine design using different experimental approaches
Summary
Human respiratory syncytial virus (HRSV) [1], a member of the Pneumoviridae family of the order Mononegavirales, is the major cause of severe lower respiratory tract illnesses, such as pneumonia and bronchiolitis, in newborns and young children [2,3,4]. Proteolytic degradation by cytosol proteases, mainly proteasomes, of the newly synthesized viral or cellular proteins, some of which synthesis or folding are defective generates 8–10 residues long peptides These short peptides, after translocation to the endoplasmic reticulum (ER) lumen by transporters associated with antigen processing, bind to the newly synthesized HLA class I molecules. In absence of appropriate HLA class I and II-restricted T cell recognition both cellular and humoral immune responses cannot be efficiently activated and the infective virus could spread within the whole organism with fatal results for the host In this context, several immunoproteomics studies performed in our laboratory have identified the target viral proteins and the ligands and epitopes presented by several common human leukocyte antigen (HLA) class I and II alleles against which the cellular immune responses are focused during HRSV infection
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