Annales de l'Institut Pasteur. Immunology最新文献

The epitope specificity of antibodies to horse cytochrome c (cyt.c) in the primary and secondary immune response of C57BL mice was studied by means of the ELISA technique with synthetic peptides of cyt.c. It was found that, in the early primary response, N- and C-end fragments of cyt.c (peptides 2–13, 14–22 and 92–104) were preferentially recognized. In the secondary response, more antibodies to the epitopes of the central part of the molecule (peptides 61–69 and 46–56) were found. This was presumed to be due to the mode of cyt.c processing and presentation in the course of immune response: at first, cyt.c was recognized in the native form and then in the processed one. The capacity of cyt.c peptides to stimulate the formation of cyt.c-specific antibody-secreting cells (ASC) was studied in splenocyte culture of C57BL mice. Peptides stimulated more ASC than cyt.c did, but larger molar doses of peptides were required. Comparison of the capacity of related peptides (1–13 and 2–13, 61–69, 61–77 and 57–77) to be recognized by antibodies produced to native cyt.cin vivo and to stimulate anti-cyt.c ASC in vitro suggested certain molecular requirements for cyt.c epitope and agretope formation. These were partially confirmed by computer analysis.

Numerous Plasmodium falciparum antigens contain repetitive amino acid sequences. Two blood stage antigens, Pf11-1 and Pf332, were characterized in our laboratories and present high cross-reactivities, defining a family of cross-reacting antigens. In this report, we show that amino acid sequence homologies might explain these cross-reactivities, but that they extend to polypeptides from the host, namely thymosin-α1 (Tα1). An antiserum raised in chickens and Saimiri monkeys against the synthetic Pf11-1 peptide cross-reacts with synthetic Tα1. Synthetic Pf11-1 and Pf332 peptides share some of the biological activities of Tα1. These results are discussed with respect to the mechanisms devised by malaria parasites for escape from the host immune response.

Genetic polymorphism of the seventh component of complement (C7) was studied in a healthy Caucasian population using polyacrylamide gel isoelectric focusing of neuraminidase-treated plasma samples and an immunoblotting procedure for the specific detection of C7. Among 248 blood donors, three C7-3/1 heterozygotes were identified, resulting in a C7^∗3 allele frequency of 0.0061 ± 0.0035. Neuraminidase treatment of serum or plasma samples is necessary for unequivocal identification of C7^∗3, which is known to be a hypomorphic variant. This observation is discussed with special reference to previous studies on C7 polymorphism in Caucasian populations, where untreated samples have been used for C7 typing.

The network theory predicts that a subpopulation within the antiidiotypic (anti-Id) antibody response will be the internal image of the priming stimulus. In myasthenia gravis, a portion of the anti-acetylcholine-receptor (anti-AChR) antibody repertoire is directed against the ligand-binding site. These antibodies would be expected to elicit an «anti-idiotypeå which is the internal image of the receptor-binding site and hence may also bind cholinergic ligands. We have utilized this theoretical specificity to isolate anti-Id antibodies with AChR-like ligand-binding properties from the serum of 4 myasthenia gravis patients using a choline affinity column. Affinity-purified antibodies from one patient were characterized and found to exhibit binding properties similar to the AChR for various cholinergic ligands.