Influenza A M1 13-21 (HLA-A*11:01)(HLA-A*03:01)(HLA-A*31:01)(HLA-A*68:01) SIIPSGPLK

The Influenza A M1 125–132 epitope (amino acid sequence: ASCMGLIY) is a CD8⁺ T cell epitope derived from Matrix Protein 1 (M1) of the Influenza A virus (UniProt ID: P03485). This 8-mer linear peptide is located within the membrane-binding domain of M1 and is known to be presented on the HLA class I molecules HLA-B27 and HLA-B35. This epitope has been referenced under IEDB Epitope ID: 4349. Human cytotoxic T lymphocyte (CTL) responses to Influenza A virus are known to target multiple epitopes, with a dominant response frequently observed against the HLA-A2-restricted epitope M1 58–66. ASCMGLIY was used in a study that investigated the influence of HLA makeup on the overall CTL response against influenza viruses. CTL responses were analyzed in groups of individuals who shared identical HLA-A and HLA-B alleles, with each group having two or three of the same four alleles. [1; under Tab References] Following in vitro stimulation of PBMCs with influenza virus, the strongest CTL activity was observed in HLA-A2-positive donors. CTL activity and precursor frequency (CTLp) were assessed for specific influenza-derived epitopes. Notably, the CTLp frequency for the HLA-B8-restricted epitope NP 380–388 was found to be threefold lower in HLA-B27-positive individuals compared to HLA-B27-negative individuals. Importantly, a threefold increase in CTLp frequency for the HLA-A1-restricted epitope NP 44–52 was observed in individuals who were positive for HLA-A1, HLA-A2, HLA-B8, and HLA-B35. This elevated response was further confirmed by in vitro CTL assays. These results suggest that CTL epitope specificity is influenced not only by the presenting HLA allele, but also by the broader HLA-A and HLA-B genotype. Moreover, the overall strength of the CTL response to influenza appears to be modulated by an individual’s HLA phenotype, highlighting the immunological relevance of HLA-B27/B35-positive donors in the context of specific epitope responses.

RMVLASTTAK is a linear peptidic epitope (epitope ID54953) studied as part of Matrix protein 1 from Influenza A virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays

The Influenza A M1 58-66 peptide is a linear peptidic epitope (epitope ID 20354) that has the amino acid sequence GILGFVFTL and is located at positions 58-66 of the Matrix Protein 1 (UniProt:P03485) from Influenza A virus.  The M1 58-66 peptide is highly conserved across many strains of influenza, T cells primed to recognize this peptide can potentially recognize and respond to a variety of influenza infections. This makes the M1 58-66 peptide valuable in vaccine research and in the study of cross-protection against different strains of influenza. The Influenza A M1 58-66 peptide is well-known for its role in being presented by HLA-A*02:01 (a class I MHC molecule) to cytotoxic CD8+ T cells. It is a well-characterized epitope, making it an ideal tool for studying how T cells recognize viral peptides and initiate an immune response. It is used as a model antigen to study T cell function, activation, and the mechanics of antigen presentation. Understanding how immune cells recognize and target antigens also helps improve T cell-based therapies for cancer.  The Influenza A M1 58-66 peptide has been tested in T cell assays, B cell assays and MHC ligand assays. It is frequently used as a positive control, especially in ELISPOT and tetramer staining, ensuring that the immune cells are functioning as expected. The M1 58-66 peptide is also a prime example of an immunodominant epitope. In people with the HLA-A*02:01 type, a significant portion of the immune response to influenza focuses on this peptide, making it a key target for understanding immune system priorities in viral infections.See also an example comparison of our prices with the prices of other peptide manufacturers.

The ILGFVFTLTV peptide (epitope ID 27066) overlaps with the well-known immunodominant epitope GILGFVFTL from Influenza A Matrix Protein 1 (M1; UniProt:P03485). Influenza A MP 59-68 is used for the development of more broadly protective influenza vaccines and as a control peptide in immunological studies.Researchers investigated the immunogenicity and protective efficacy of Modified Vaccinia Virus Ankara (MVA) vectors encoding internal influenza antigens in HLA-A2.1 transgenic mice. Following vaccination with recombinant MVAs expressing peptides derived from Influenza A Matrix Protein 1 (M1), the induced CD8⁺ T cell responses were primarily directed against the immunodominant epitope M1 58-66. However, consistent T cell responses were also observed against the overlapping peptide M1 59-68. CD8⁺ T cell activity was assessed using an IFN-γ ELISPOT assay.

The Influenza A M1 Peptide Pool is a carefully designed mix of 61 overlapping 15-mer peptides (11-amino-acid overlap) that span the full-length Matrix protein 1 (UniProt ID: P03485) of Influenza A virus. This peptide pool enables robust stimulation of influenza-specific CD4⁺ and CD8⁺ T cells in various immunomonitoring assays, including: ELISPOT   Intracellular cytokine staining (ICS)   Flow cytometry   Activation-Induced Marker (AIM) assays The peptide pool is suitable for infection models, vaccine evaluation, and cellular immune response profiling. One unit allows the stimulation of 2,5 x 108 cells. Key Features: Covers the entire M1 protein (252 amino acids) of Influenza A Virus Tested for endotoxin-free performance     Lyophilized, ready for reconstitution   Suitable for both in vitro stimulation and ex vivo detection of T cell responses Applications: Monitoring influenza-specific cellular immunity Evaluation of vaccine candidates or adjuvants Detection of memory T cell responses post-infection or vaccination Use in longitudinal studies or clinical immunology research Background Matrix protein 1 (M1) is the most abundant structural protein in Influenza A virions and plays a crucial role in multiple steps of the viral life cycle – from genome uncoating during host cell entry to assembly and budding. It forms a protein shell beneath the lipid envelope and mediates interactions with ribonucleoprotein complexes (vRNPs), membrane proteins, and the M2 ion channel. Due to its high conservation and immunogenicity, M1 is a well-established target for T cell-mediated immunity and a valuable component in vaccine and infection research.