Abstract
Polypeptide constructs containing up to four copies of the T cell epitope 306-318 of influenza virus haemagglutinin have been synthesized on solid phase. Between the copies, a non-natural PEG-based spacer amino acid has been introduced. The oligomeric epitopes were analysed by RP-HPLC and ES-MS. The arrangement of the epitopes within the peptide constructs was either linear or comb-like. The proliferative response in a T helper cell assay induced by these oligomerized epitopes has been tested, showing that the linearly arranged epitopes are more effective than the comb-like oligomers.
MeSH terms
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Amino Acid Sequence
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Antigens, Viral / chemistry
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Antigens, Viral / immunology
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CD4-Positive T-Lymphocytes / cytology
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CD4-Positive T-Lymphocytes / immunology*
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Cell Division
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Cell Line
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Chromatography, High Pressure Liquid
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Epitopes, T-Lymphocyte / chemistry*
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Epitopes, T-Lymphocyte / immunology*
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Hemagglutinin Glycoproteins, Influenza Virus / chemistry
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Hemagglutinin Glycoproteins, Influenza Virus / immunology*
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Humans
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Leukocytes, Mononuclear / cytology
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Leukocytes, Mononuclear / immunology
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Mass Spectrometry
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Peptides / chemical synthesis*
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Peptides / chemistry
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Peptides / immunology*
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Protein Conformation
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Repetitive Sequences, Amino Acid / immunology*
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Structure-Activity Relationship
Substances
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Antigens, Viral
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Epitopes, T-Lymphocyte
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Hemagglutinin Glycoproteins, Influenza Virus
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Peptides