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T‐Cell Recognition of Measles Virus Haemagglutinin Studied in a Mouse Model
Author(s) -
MÄKELÄ M. J.,
SMITH R. H.,
LUND G. A.,
SALMI A. A.
Publication year - 1989
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.1365-3083.1989.tb01163.x
Subject(s) - measles virus , antigen , epitope , priming (agriculture) , microbiology and biotechnology , peptide , virology , t cell , biology , sindbis virus , in vitro , chemistry , immune system , immunology , measles , biochemistry , vaccination , rna , botany , germination , gene
BALB/c mice were pretreated with cyclophosphamide and immunized 2 days later with inactivated, purified measles virus (MV) mixed with dimethyl dioctadecyl ammonium bromide (DDA). Seven days later, lymph nodes (LN) were removed and lymphocytes cultured in the presence of purified MV antigens. MV haemagglutinin (H) was found to be a major antigen responsible for proliferation of the lymphocytes Incorporation of purified H into liposomes significantly enhanced the proliferative response compared with purified H alone. Response to MV nucleocapsid protein was only moderate, and insertion of this protein into liposomes did not improve the response. As un attempt to analyse T‐cell epitopes of MVH, three synthetic peptides previously found to elicit a strong antibody response were used both as priming and stimulating antigens. None of the peptides was able to elicit a secondary response when MV‐primed LN cells were stimulated in vitro. However, each peptide primed T cells for a secondary challenge with purified, inactivated MV, which was demonstrated by proliferation and a delayed‐type hypersensitivity assay and also by transfer experiments with peptide‐primed cells.