HSV-gB2 (498-505) is an immunodominant epitope from herpes simplex virus (HSV) glycoprotein B residues 498-505, acts as H-2Kb-restricted and HSV-1/2-cross-reactive cytotoxic T-lymphocyte (CTL) recognition epitope.
CAT No: R1434
CAS No:149997-91-1
Synonyms/Alias:HSV-gB2 (498-505);HSV-gB2 498-505;149997-91-1;HY-P1862;CS-0096593;G13455;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-amino-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-3-methylpentanoyl]amino]-4-carboxybutanoyl]amino]-3-phenylpropanoyl]amino]propanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-4-methylpentanoic acid;
HSV-gB2 498-505 is a synthetic peptide corresponding to amino acids 498 through 505 of the glycoprotein B (gB2) from herpes simplex virus type 2 (HSV-2). As a well-defined linear peptide fragment, it is frequently utilized in virology and immunology research to investigate viral entry mechanisms, host-pathogen interactions, and epitope mapping. The sequence represents a conserved region within the gB2 protein, which plays a pivotal role in viral membrane fusion and cell infection processes, making it a valuable tool for dissecting molecular events associated with HSV-2 pathogenesis. By providing a precisely defined segment of the viral glycoprotein, this peptide enables researchers to conduct targeted studies on immune recognition and functional domains critical to HSV-2 biology.
Epitope mapping: In immunological studies, HSV-gB2 498-505 serves as a reference peptide for mapping B-cell and T-cell epitopes within the glycoprotein B of HSV-2. Researchers employ this fragment to identify and characterize antigenic determinants recognized by the adaptive immune system, facilitating the development of immunoassays, vaccine design strategies, and the assessment of immune memory following viral exposure. Its defined sequence allows for the systematic evaluation of immune responses at the peptide level, supporting the elucidation of immunodominant regions and their relevance to protective immunity.
Antibody specificity testing: The peptide is widely utilized as a substrate in assays designed to assess the specificity and affinity of antibodies generated against HSV-2 gB2. By incorporating this fragment into enzyme-linked immunosorbent assays (ELISA), Western blotting, or immunofluorescence protocols, researchers can determine the presence and strength of antibody binding to the targeted region, which is essential for validating antibody reagents, screening candidate monoclonal antibodies, and monitoring serological responses in experimental systems.
Functional studies of viral entry: HSV-gB2 498-505 is instrumental in dissecting the functional domains of gB2 involved in viral membrane fusion and entry into host cells. By introducing this peptide into cell-based assays or membrane fusion models, investigators can probe the structural requirements for viral infectivity, assess peptide-mediated inhibition of viral entry, and explore the mechanistic basis of gB2-mediated membrane interactions. Such studies contribute to a deeper understanding of the molecular determinants governing HSV-2 infectivity and may inform the design of novel antiviral strategies.
T-cell activation assays: The defined sequence of this peptide makes it suitable for use in ex vivo and in vitro T-cell activation experiments. Researchers employ it to stimulate peripheral blood mononuclear cells (PBMCs) or isolated T-cell populations to evaluate cellular immune responses specific to HSV-2. These assays enable the quantification of cytokine production, proliferation, or cytotoxic activity in response to the peptide, providing insights into the cellular arm of the host immune defense and supporting studies on immune memory, vaccine efficacy, or immunopathology associated with HSV-2 infection.
Peptide-based assay development: The availability of HSV-gB2 498-505 as a synthetic peptide supports the development and optimization of peptide-based diagnostic and research assays. Its use as a standard or control in various immunoassay formats enhances assay reproducibility, facilitates the calibration of detection systems, and enables comparative studies across different laboratories. By serving as a reliable reagent in peptide-centric analytical workflows, it contributes to the advancement of robust and standardized methodologies for HSV-2 research and related virological investigations.
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