What question did this study set out to answer?

Investigate the presentation, structural stability, and CD8+ T cell immunogenicity of the influenza B virus homologue peptide PB1177-B presented by HLA-B*18:01.

June 30, 2025Biochemical JournalOpen Access

Characterisation of an influenza B virus-derived peptide presented by HLA-B*18:01

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Authors

LMLawton D. MurdoloLa Trobe University SLSamuel Liwei LeongLa Trobe University JMJanesha C. MaddumageLa Trobe University

Discussion

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Implication

Laboratory study uncovers structural instability in an influenza B peptide presented by HLA-B*18:01, indicating impaired CD8+ T cell activation and cross-reactivity.

Key Points

Investigate the presentation, structural stability, and CD8+ T cell immunogenicity of the influenza B virus homologue peptide PB1177-B presented by HLA-B*18:01.
Assessed CD8+ T cell activation against PB1177-B in HLA-B*18:01-positive biological samples using intracellular cytokine staining assays.
Analyzed the crystal structure and conducted molecular dynamics simulations of the HLA-B*18:01-PB1177-B complex compared with the homologous influenza A virus peptide (PB1177-A).
PB1177-B failed to stimulate CD8+ T cells from multiple HLA-B*18:01-positive donor samples.
The PB1177-B peptide exhibited distinct conformational differences, lower complex stability, and a flexible central region with a hydrophobic patch formed by two phenylalanine residues not found in PB1177-A, likely preventing T cell receptor binding.

Cite This Study

Murdolo et al. (2025) studied this question.

synapsesocial.com/papers/6a1b3dfe8b4bc479d4c40dcd https://doi.org/10.1042/bcj20240739

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June 30, 2025Biochemical JournalOpen Access

Characterisation of an influenza B virus-derived peptide presented by HLA-B*18:01

View Full Paper

Ask AI

Bookmark

Authors

LMLawton D. MurdoloLa Trobe University SLSamuel Liwei LeongLa Trobe University JMJanesha C. MaddumageLa Trobe University

Discussion

Member takes

Implication

Laboratory study uncovers structural instability in an influenza B peptide presented by HLA-B*18:01, indicating impaired CD8+ T cell activation and cross-reactivity.

Key Points

Investigate the presentation, structural stability, and CD8+ T cell immunogenicity of the influenza B virus homologue peptide PB1177-B presented by HLA-B*18:01.
Assessed CD8+ T cell activation against PB1177-B in HLA-B*18:01-positive biological samples using intracellular cytokine staining assays.
Analyzed the crystal structure and conducted molecular dynamics simulations of the HLA-B*18:01-PB1177-B complex compared with the homologous influenza A virus peptide (PB1177-A).
PB1177-B failed to stimulate CD8+ T cells from multiple HLA-B*18:01-positive donor samples.
The PB1177-B peptide exhibited distinct conformational differences, lower complex stability, and a flexible central region with a hydrophobic patch formed by two phenylalanine residues not found in PB1177-A, likely preventing T cell receptor binding.

Cite This Study

Murdolo et al. (2025) studied this question.

synapsesocial.com/papers/6a1b3dfe8b4bc479d4c40dcd https://doi.org/10.1042/bcj20240739

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