Identification of an antigenic determinant within the phylogenetically conserved triprolyl region of myelin basic protein

Nicholas Potter, G. A. Hashim, E. D. Day

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Synthetic peptide SP6 (RTPPPSG), comprising amino acid residues 98-103-Gly of myelin basic protein (MBP), and a series of peptide analogs were used to probe the structural requirements for antigenicity of a highly conserved region of a self protein. By means of a liquid-phase radioimmunoassay, antibody responses directed toward this determinant in both multi-specific anti-MBP and monospecific anti-peptide antisera were measured. The specificities of the antibodies present in the anti-MBP and anti-peptide antisera were examined by an equilibrium competitive inhibition radioimmunoassay by using the set of related peptides, as well as intact MBP from different species. Although the fine specificities of the reagent antisera differed, competitive inhibition analyses with intact MBP revealed a cross-reactive determinant involving residues 99-100 (Thr-Pro). This suggests that the neighborhood of the triprolyl region of MBP, despite its strong phylogenetic conservation, serves as an immunogen for humoral responses whether presented as a hapten-carrier conjugate or in the context of intact MBP. The latter supports the contention that the general antigenicity of a protein need not require sequence differences between the immunizing protein and its counterpart in the host.

Original languageEnglish (US)
Pages (from-to)516-520
Number of pages5
JournalJournal of Immunology
Volume136
Issue number2
StatePublished - Jan 1 1986
Externally publishedYes

Fingerprint

Myelin Basic Protein
Epitopes
Peptides
Immune Sera
Radioimmunoassay
Proteins
Antibody Specificity
Haptens
Antibody Formation
Amino Acids

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

Identification of an antigenic determinant within the phylogenetically conserved triprolyl region of myelin basic protein. / Potter, Nicholas; Hashim, G. A.; Day, E. D.

In: Journal of Immunology, Vol. 136, No. 2, 01.01.1986, p. 516-520.

Research output: Contribution to journalArticle

@article{83408c944f174533b5c62e4fd06e0192,
title = "Identification of an antigenic determinant within the phylogenetically conserved triprolyl region of myelin basic protein",
abstract = "Synthetic peptide SP6 (RTPPPSG), comprising amino acid residues 98-103-Gly of myelin basic protein (MBP), and a series of peptide analogs were used to probe the structural requirements for antigenicity of a highly conserved region of a self protein. By means of a liquid-phase radioimmunoassay, antibody responses directed toward this determinant in both multi-specific anti-MBP and monospecific anti-peptide antisera were measured. The specificities of the antibodies present in the anti-MBP and anti-peptide antisera were examined by an equilibrium competitive inhibition radioimmunoassay by using the set of related peptides, as well as intact MBP from different species. Although the fine specificities of the reagent antisera differed, competitive inhibition analyses with intact MBP revealed a cross-reactive determinant involving residues 99-100 (Thr-Pro). This suggests that the neighborhood of the triprolyl region of MBP, despite its strong phylogenetic conservation, serves as an immunogen for humoral responses whether presented as a hapten-carrier conjugate or in the context of intact MBP. The latter supports the contention that the general antigenicity of a protein need not require sequence differences between the immunizing protein and its counterpart in the host.",
author = "Nicholas Potter and Hashim, {G. A.} and Day, {E. D.}",
year = "1986",
month = "1",
day = "1",
language = "English (US)",
volume = "136",
pages = "516--520",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "2",

}

TY - JOUR

T1 - Identification of an antigenic determinant within the phylogenetically conserved triprolyl region of myelin basic protein

AU - Potter, Nicholas

AU - Hashim, G. A.

AU - Day, E. D.

PY - 1986/1/1

Y1 - 1986/1/1

N2 - Synthetic peptide SP6 (RTPPPSG), comprising amino acid residues 98-103-Gly of myelin basic protein (MBP), and a series of peptide analogs were used to probe the structural requirements for antigenicity of a highly conserved region of a self protein. By means of a liquid-phase radioimmunoassay, antibody responses directed toward this determinant in both multi-specific anti-MBP and monospecific anti-peptide antisera were measured. The specificities of the antibodies present in the anti-MBP and anti-peptide antisera were examined by an equilibrium competitive inhibition radioimmunoassay by using the set of related peptides, as well as intact MBP from different species. Although the fine specificities of the reagent antisera differed, competitive inhibition analyses with intact MBP revealed a cross-reactive determinant involving residues 99-100 (Thr-Pro). This suggests that the neighborhood of the triprolyl region of MBP, despite its strong phylogenetic conservation, serves as an immunogen for humoral responses whether presented as a hapten-carrier conjugate or in the context of intact MBP. The latter supports the contention that the general antigenicity of a protein need not require sequence differences between the immunizing protein and its counterpart in the host.

AB - Synthetic peptide SP6 (RTPPPSG), comprising amino acid residues 98-103-Gly of myelin basic protein (MBP), and a series of peptide analogs were used to probe the structural requirements for antigenicity of a highly conserved region of a self protein. By means of a liquid-phase radioimmunoassay, antibody responses directed toward this determinant in both multi-specific anti-MBP and monospecific anti-peptide antisera were measured. The specificities of the antibodies present in the anti-MBP and anti-peptide antisera were examined by an equilibrium competitive inhibition radioimmunoassay by using the set of related peptides, as well as intact MBP from different species. Although the fine specificities of the reagent antisera differed, competitive inhibition analyses with intact MBP revealed a cross-reactive determinant involving residues 99-100 (Thr-Pro). This suggests that the neighborhood of the triprolyl region of MBP, despite its strong phylogenetic conservation, serves as an immunogen for humoral responses whether presented as a hapten-carrier conjugate or in the context of intact MBP. The latter supports the contention that the general antigenicity of a protein need not require sequence differences between the immunizing protein and its counterpart in the host.

UR - http://www.scopus.com/inward/record.url?scp=0022631512&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022631512&partnerID=8YFLogxK

M3 - Article

VL - 136

SP - 516

EP - 520

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 2

ER -