Multiple Viral Ligands Naturally Presented by Different Class I Molecules in Transporter Antigen Processing-Deficient Vaccinia Virus-Infected Cells

Lorente, Elena; Infantes, Susana; Barnea, Eilon; Beer, Ilan; García, Ruth; Lasala, Fátima; Jiménez, Mercedes; Vilches, Carlos; Lefrère, François; Admon, Arie; López, Daniel

doi:10.1128/jvi.05737-11

Cited by 18 publications

(52 citation statements)

References 73 publications

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“…The tip was then washed with an additional volume of 0.1% TFA, and the peptides were eluted with 80% acetonitrile in 0.1% TFA. The peptide samples were then concentrated to ϳ20 l using vacuum centrifugation (13,15).…”

Section: Methodsmentioning

confidence: 99%

“…The HLA class II peptides recovered from immunoprecipitated HLA-DR-specific mAb, were analyzed by LC-MS/MS using an Orbitrap XL mass spectrometer (Thermo Scientific, San Jose, CA) that was fitted with a capillary HPLC (Eksigent, Dublin, CA) (13,15). The peptides were resolved on homemade Reprosil C18-Aqua capillary columns (75 micron inner diameter) (16) with a 7-40% acetonitrile gradient for 2 h in the presence of 0.1% formic acid.…”

Section: Methodsmentioning

confidence: 99%

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Structural and Nonstructural Viral Proteins Are Targets of T-Helper Immune Response against Human Respiratory Syncytial Virus

Lorente

Barriga

Barnea

et al. 2016

Molecular & Cellular Proteomics

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Newly synthesized HLA class II molecules from antigenpresenting cells associate with the class II invariant chain (Ii). These complexes are eventually transported to specialized endosomal compartments where the Ii is progressively proteolyzed until only a fragment known as the class-II-associated invariant chain peptide (CLIP) 1 remains bound in the HLA class II peptide-binding groove to prevent it from binding to cellular peptides or pathogen peptides from the endogenous pathways. Interaction of HLA class II/CLIP complexes with the accessory molecule HLA-DM induces conformational changes in HLA class II molecules. Additionally, the release of CLIP results in peptide-receptive HLA class II molecules. This compartment fuses with a late endosome that contains exogenous proteins and/or viral particles that were previously endocytosed. Thus, the binding of antigen-processed peptides of different lengths, but with specific major anchor residues that can be deeply accommodated into specific pockets of the antigen recognition site of the HLA class II molecule, produces the stabilization of the nascent HLA class II/peptide complexes and allows for their subsequent transport to the cell membrane where they are exposed for T cell recognition (1).Human respiratory syncytial virus (HRSV) (2), which is included in the Paramyxoviridae family of the Mononegavirales order, presents a single-stranded, negative-sense RNA genome that codes for 11 proteins. This enveloped pneumovirus causes repeat infections throughout life, and although in healthy adults mild infections are generally reported, the health risk in infected pediatric, immunocompromised, and elderly populations is much more serious. HRSV is the main cause of hospitalization for bronchiolitis and pneumonia in infants and young children, with infection rates approaching 70% in the first year of life (3). Worldwide, at least 3.4 million hospital admissions each year are associated with severe HRSV disease, and the global mortality rate was estimated at more than a quarter of a million deaths in 2010, mainly in developing countries (4).The immune mechanisms involved in HRSV disease and protection are not completely understood; however, it is known that infection induces mucosal and systemic humoral and cellular responses. Studies evaluating CD4 ϩ and CD8 ϩ T-lymphocyte subsets individually or together showed that both effector MHC class I-and helper MHC class II-restricted cellular responses are particularly important in clearing infections (5). Previously, some HRSV epitopes that are restricted by different HLA class II molecules were identified using T cells from seropositive individuals (6 -9). However, these experiments were performed with overlapping synthetic pepFrom the ‡Centro Nacional

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Structural and Nonstructural Viral Proteins Are Targets of T-Helper Immune Response against Human Respiratory Syncytial Virus

Lorente

Barriga

Barnea

et al. 2016

Molecular & Cellular Proteomics

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“…4). The haplotype of the cell line used in the immunoprecipitation was HLA-A*02:01, -B*07:02, and -C*07:02, and thus the G [25][26][27][28][29][30][31][32][33] peptide was most likely a HLA-C*07:02 ligand.…”

Section: Resultsmentioning

confidence: 99%

“…of 0.1% TFA, and the peptides were eluted with 80% acetonitrile in 0.1% TFA. The peptide samples were then concentrated to ϳ20 l using vacuum centrifugation (17,28).…”

mentioning

confidence: 99%

“…The HLA class I peptides that were immunoprecipitated with each HLA-specific mAb were analyzed by LC-MS/MS using an Orbitrap XL mass spectrometer (Thermo Scientific, San Jose, CA) that was fitted with a capillary HPLC column (Eksigent, Dublin, CA) (17,28). The peptides were resolved on homemade Reprosil C18-Aqua capillary columns (75 micron ID) (29) with a 7-40% acetonitrile gradient for 2 h in the presence of 0.1% formic acid.…”

mentioning

confidence: 99%

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The Viral Transcription Group Determines the HLA Class I Cellular Immune Response Against Human Respiratory Syncytial Virus*

Johnstone

Lorente

Barriga

et al. 2015

Molecular & Cellular Proteomics

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The cytotoxic T-lymphocyte-mediated killing of virus-infected cells requires previous recognition of short viral antigenic peptides bound to human leukocyte antigen class I molecules that are exposed on the surface of infected cells. The cytotoxic T-lymphocyte response is critical for the clearance of human respiratory syncytial virus infection. In this study, naturally processed viral human leukocyte antigen class I ligands were identified with mass spectrometry analysis of complex human leukocyte antigen-bound peptide pools isolated from large amounts of human respiratory syncytial virus-infected cells. Acute antiviral T-cell response characterization showed that viral transcription determines both the immunoprevalence and immunodominance of the human leukocyte antigen class I response to human respiratory syncytial virus.

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The HLA-DP peptide repertoire from human respiratory syncytial virus is focused on major structural proteins with the exception of the viral polymerase

Lorente¹,

Barnea

Mir³

et al. 2020

Journal of Proteomics

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Multiple Viral Ligands Naturally Presented by Different Class I Molecules in Transporter Antigen Processing-Deficient Vaccinia Virus-Infected Cells

Abstract: The transporter associated with antigen processing (TAP) delivers the viral proteolytic products generated by the proteasome in the cytosol to the endoplasmic reticulum lumen that are subsequently recognized by cytotoxic T lymphocytes (CTLs).

Cited by 18 publications

References 73 publications

Structural and Nonstructural Viral Proteins Are Targets of T-Helper Immune Response against Human Respiratory Syncytial Virus

Structural and Nonstructural Viral Proteins Are Targets of T-Helper Immune Response against Human Respiratory Syncytial Virus

The Viral Transcription Group Determines the HLA Class I Cellular Immune Response Against Human Respiratory Syncytial Virus*

The HLA-DP peptide repertoire from human respiratory syncytial virus is focused on major structural proteins with the exception of the viral polymerase

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