Surface and bulk modulation in photoreflectance from undoped GaAs.
Explore the source record for details and available documents.
Biomedical subjects
Publications and source records attributed to M Sydor.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Pertussis toxin (PT) is a major virulence factor of Bordetella pertussis, and also an important protective antigen. PT is an oligomeric A-B type toxin in which the S1 subunit has the ADP-ribosyltransferase activity whereas the B-oligomer mediates its binding to target cell receptors. To analyze the immunological properties of S1 and to generate probes to localize and characterize S1 functional domains, we synthesized four sets of peptides and peptide analogs corresponding to potentially critical regions of the S1 subunit. Two peptide-KLH conjugates were found to be capable of inducing PT-neutralizing antibodies in rabbits as judged by the CHO cell clustering assay. These peptides comprise residues 1-18 (N18-S1) and 121-138 (NAD-S1), respectively. Immunization with the unconjugated C-terminal peptide C35-S1 (residues 201-235) in the presence of Freund's adjuvant also elicited PT-neutralizing antibodies, indicating that the C-terminal region of S1 contains a potent functional T-helper cell epitope. Using truncated peptide analogs of N18-S1, we have demonstrated that the first three N-terminal residues are essential for inducing neutralizing antibodies. The NAD-S1 peptide elicited a neutralizing antibody response when coupled to KLH via its N-terminal end but not via its C-terminal residue. Identification of these B-cell neutralization epitopes represents a first step towards the rational design of a synthetic vaccine against whooping cough.
Recent studies indicate that the gag gene products may play a crucial role in the immune response against HIV infection since clinical progression to AIDS is associated with a reduction in the level of circulating antibodies to gag p24 and antibodies raised against p17 peptide can inhibit HIV1 infection in vitro. Using conventional structure prediction algorithms for T-cell and B-cell epitopes, we have selected and chemically synthesized several gag peptides. In particular, an unconjugated HIV1-p24 peptide containing both B- and T-cell epitopes in tandem plus Freund's adjuvant induced a strong antibody response in both mice and rabbits against p24 and its precursor p55 as judged by immunoblotting. In addition, the peptide presented in the appropriate MHC context was shown to be highly stimulatory for p24 specific murine T-cell clones.
Explore the source record for details and available documents.