Abstract:
:Multiple antigen peptides (MAP), consisting of a number of peptide copies synthesized on a branching lysyl core, offer a novel approach for rendering small peptides immunoreactive in solid-phase immunoassays. An octameric MAP, carrying 6 repeats of the sequence -N-A-A-G-, tandem repeated in the immunodominant region of the circumsporozoite (CS) protein of Plasmodium malariae, was used as a model to evaluate the suitability of the MAP system in an indirect enzyme-linked immunosorbent assay (ELISA) for detecting antibodies against a parasite antigen in individuals exposed to natural infection. The reaction of endemic sera in ELISA on MAP8-(NAAG)6 was related to that obtained in immunofluorescence on sporozoites, indicating the specificity of the antibody-MAP interaction. The reactivity of immune sera was found to be directed only against the (NAAG)6 moiety of the MAP and not against the lysyl core, since antibody binding to MAP8-(NAAG)6 was completely inhibited by (NAAG)6-NA monomer, but remained uninfluenced when lysyl core was used as competing ligand. The levels of antibodies to MAP8-(NAAG)6, in two groups of individuals naturally exposed to malaria infection, appeared to be related to their respective exposure to the parasite.
journal_name
Immunol Lettjournal_title
Immunology lettersauthors
Habluetzel A,Pessi A,Bianchi E,Rotigliano G,Esposito Fdoi
10.1016/0165-2478(91)90092-osubject
Has Abstractpub_date
1991-09-01 00:00:00pages
75-80issue
1eissn
0165-2478issn
1879-0542pii
0165-2478(91)90092-Ojournal_volume
30pub_type
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