Genetic control of antibody response to bovine rhodopsin in mice

epitope mapping of rhodopsin structure

Grazyna Adamus, Anatol Arendt, Paul A. Hargrave

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Inbred strains of mice of independent haplotype were immunized with bovine rhodopsin. All mice tested except SJL developed significant titers of specific antibodies 21 days after a single immunization. Anti-rhodopsin antibody level differed among conventional inbred strains. Comparison of the immune response to rhodopsin of congenic mice on two different genetic backgrounds showed that animals with an A background typically produced higher levels of specific antibody than mice with a B10 background. Titer of specific antibodies in antisera of mice of the same H-2 haplotype but different Igh haplotype differed; e.g. for H-2d haplotype, NZB (Ighn) generated the highest level of antibody with BALB/c (Igha), DBA/2 (Ighc), and B10.D2 (Ighb) strains giving successively lower responses. The location of immunodominant regions of bovine rhodopsin was investigated in primary sera among strains of mice. Sera were tested for their binding of anti-rhodopsin antibodies to synthetic peptides covering the entire primary structure of rhodopsin. From direct binding studies with hydrophilic rhodopsin peptides, the majority of the antigenic binding sites were localized in the sequence of the amino terminus, the II-III loop and the carboxyl terminus. Binding to these antigenic peptides was not strain restricted. Application of the overlapping synthetic peptide strategy of Geysen enabled refinement of these epitopes and determination of an additional major epitope in the hydrophobic sequence 304-310.

Original languageEnglish (US)
Pages (from-to)89-97
Number of pages9
JournalJournal of Neuroimmunology
Volume34
Issue number2-3
DOIs
StatePublished - 1991
Externally publishedYes

Fingerprint

Epitope Mapping
Rhodopsin
Antibody Formation
Haplotypes
Peptides
Antibodies
Epitopes
Anti-Idiotypic Antibodies
Congenic Mice
Immunodominant Epitopes
Inbred Strains Mice
Serum
Immune Sera
Immunization
Binding Sites

Keywords

  • (Mouse)
  • Antibody response
  • Epitope mapping
  • Genetic control
  • Major histocompatibility complex
  • Rhodopsin

ASJC Scopus subject areas

  • Immunology
  • Immunology and Allergy
  • Clinical Neurology
  • Neurology

Cite this

Genetic control of antibody response to bovine rhodopsin in mice : epitope mapping of rhodopsin structure. / Adamus, Grazyna; Arendt, Anatol; Hargrave, Paul A.

In: Journal of Neuroimmunology, Vol. 34, No. 2-3, 1991, p. 89-97.

Research output: Contribution to journalArticle

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AB - Inbred strains of mice of independent haplotype were immunized with bovine rhodopsin. All mice tested except SJL developed significant titers of specific antibodies 21 days after a single immunization. Anti-rhodopsin antibody level differed among conventional inbred strains. Comparison of the immune response to rhodopsin of congenic mice on two different genetic backgrounds showed that animals with an A background typically produced higher levels of specific antibody than mice with a B10 background. Titer of specific antibodies in antisera of mice of the same H-2 haplotype but different Igh haplotype differed; e.g. for H-2d haplotype, NZB (Ighn) generated the highest level of antibody with BALB/c (Igha), DBA/2 (Ighc), and B10.D2 (Ighb) strains giving successively lower responses. The location of immunodominant regions of bovine rhodopsin was investigated in primary sera among strains of mice. Sera were tested for their binding of anti-rhodopsin antibodies to synthetic peptides covering the entire primary structure of rhodopsin. From direct binding studies with hydrophilic rhodopsin peptides, the majority of the antigenic binding sites were localized in the sequence of the amino terminus, the II-III loop and the carboxyl terminus. Binding to these antigenic peptides was not strain restricted. Application of the overlapping synthetic peptide strategy of Geysen enabled refinement of these epitopes and determination of an additional major epitope in the hydrophobic sequence 304-310.

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