Sequence and type-specific immunogenicity of the amino-terminal region of type 1 streptococcal M protein

W. Kraus, E. Haanes-Fritz, P. P. Cleary, J. M. Seyer, James Dale, E. H. Beachey

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Abstract

The NH2-terminal sequence of type 1 M protein was determined by automated Edman degradation of purified polypeptide fragments extracted from whole streptococci by limited digestion with pepsin. Three polypeptide fragments were purified by slab gel electrophoresis on sodium dodecyl sulfate (SDS) polyacrylamide followed by electroelution. The purified fragments migrated as 28-, 25-, and 23.5-kDa fragments, respectively. Each of the fragments inhibited opsonization of a diluted antiserum prepared in rabbits by immunization with whole type 1 streptococci. The amino-terminal sequences of the peptide fragments were confirmed by comparison with the primary structure predicted from the nucleotide sequence of the type 1 M protein structural gene. The 28-kDa fragment contained the NH2-terminal asparagine residue of the processed type 1 M protein, whereas the NH2-terminal sequences of the 25- and 23.5-kDa peptides began at residues 27 and 36, respectively. A seven-residue periodicity with respect to polar and nonpolar residues was observed beginning at residue 22 and, therefore, the secondary structural potential of type 1 M protein is similar to that reported for other M proteins. In contrast to the other M proteins, however, identical repeats were rare, the longest sequence identity consisting of a three-amino acid sequence Lys-Asp-Leu positions 30-32 repeated once at positions 65-67. A 23-residue synthetic peptide of the amino-terminus of the type 1 M protein evoked opsonic antibodies against type 1 streptococci. These results indicate that the NH2-terminal region of type 1 M protein retains the secondary structural characteristics of other M serotypes. Moreover, it contains epitopes that evoke protective immune responses. Our studies may have bearing in the development of safe and effective vaccines against group A streptococcal infections.

Original languageEnglish (US)
Pages (from-to)3084-3090
Number of pages7
JournalJournal of Immunology
Volume139
Issue number9
StatePublished - Jan 1 1987

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Proteins
Streptococcus
Peptides
Streptococcal Infections
Peptide Fragments
streptococcal M protein
Pepsin A
Asparagine
Periodicity
Sodium Dodecyl Sulfate
Electrophoresis
Immune Sera
Epitopes
Digestion
Amino Acid Sequence
Immunization
Vaccines
Gels
Rabbits
Antibodies

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

Kraus, W., Haanes-Fritz, E., Cleary, P. P., Seyer, J. M., Dale, J., & Beachey, E. H. (1987). Sequence and type-specific immunogenicity of the amino-terminal region of type 1 streptococcal M protein. Journal of Immunology, 139(9), 3084-3090.

Sequence and type-specific immunogenicity of the amino-terminal region of type 1 streptococcal M protein. / Kraus, W.; Haanes-Fritz, E.; Cleary, P. P.; Seyer, J. M.; Dale, James; Beachey, E. H.

In: Journal of Immunology, Vol. 139, No. 9, 01.01.1987, p. 3084-3090.

Research output: Contribution to journalArticle

Kraus, W, Haanes-Fritz, E, Cleary, PP, Seyer, JM, Dale, J & Beachey, EH 1987, 'Sequence and type-specific immunogenicity of the amino-terminal region of type 1 streptococcal M protein', Journal of Immunology, vol. 139, no. 9, pp. 3084-3090.
Kraus W, Haanes-Fritz E, Cleary PP, Seyer JM, Dale J, Beachey EH. Sequence and type-specific immunogenicity of the amino-terminal region of type 1 streptococcal M protein. Journal of Immunology. 1987 Jan 1;139(9):3084-3090.
Kraus, W. ; Haanes-Fritz, E. ; Cleary, P. P. ; Seyer, J. M. ; Dale, James ; Beachey, E. H. / Sequence and type-specific immunogenicity of the amino-terminal region of type 1 streptococcal M protein. In: Journal of Immunology. 1987 ; Vol. 139, No. 9. pp. 3084-3090.
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