Antibody recognition of synthetic peptides mimicking immunodominant regions of HIV-1 p24 and p17 proteins.
作者： J Lottersberger , L M Beltramini , G Tonarelli , J L Salvetti
DOI:
关键词: Group-specific antigen 、 Open reading frame 、 Chemistry 、 Epitope 、 Peptide sequence 、 Molecular mimicry 、 Capsid 、 Protein structure 、 Biochemistry 、 Circular dichroism
摘要: The gag gene of HIV-1 encodes a single open reading frame 55 kDa that contains three subdomains: the matrix domain (p17), capsid (p24) and nucleocapsid (p15). p24 p17 proteins have predominant alpha-helical structure perform important functions throughout viral life-cycle. determination gag-specific antibodies is because declining titers these herald clinical deterioration. In this work we present results obtained on immunoreactiviy synthetic peptides mimic immunogenic regions p17. influence immunoreactivity structural modifications in native sequences, including addition non side chains: AAAC- -CAAA both minimal epitopes was evaluated indirect competitive enzyme immunoassays. conformational characteristcs to were analysed by circular dichroism correlated with It shown reactivity mimicking short improved adding chains N- C-terminus. These enhanced immobilization onto solid support allowed more accessibility specific antibodies, solution.
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