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Identification of Linear HLA Class II Amino Acid Sequences Recognized by Rabbit Antisera against Native Molecules
Author(s) -
CHERSI A.,
MORGANTI M. C.,
HOUGHTEN R.,
CHILLEMI F.,
MURATTI E.
Publication year - 1987
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1987.tb02309.x
Subject(s) - antiserum , identification (biology) , biology , human leukocyte antigen , amino acid , rabbit (cipher) , computational biology , chemistry , microbiology and biotechnology , biochemistry , immunology , antigen , mathematics , botany , statistics
A rabbit was immunized with B lymphoblastoid cells, and subsets of the antibodies produced were isolated on affinity columns made from synthetic peptides corresponding to known amino acid sequences from the human class II antigens DQ and DP. Those peptides for which specific antibodies were isolated could be assumed to contribute to the antigenic properties of the intact antigen. The antibody subsets were tested for binding to synthetic peptides, to glycoprotein fractions isolated from cells with different DR and DQ specificities, and to the cells used for immunization of the rabbit. The isolation of those antibodies directed against well‐defined amino acid stretches of the histocompatibility antigens is proof of the role of those regions in determining the antigenic properties of these molecules.