The complete amino acid sequence of a biologically active 197-residue fragment of M protein isolated from type 5 group A streptococci.

@article{Manjula1984TheCA,
  title={The complete amino acid sequence of a biologically active 197-residue fragment of M protein isolated from type 5 group A streptococci.},
  author={Belur N. Manjula and A. Seetharama Acharya and Sheenah M Mische and Thomas Fairwell and Vincent A. Fischetti},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 6},
  pages={3686-93}
}
The complete amino acid sequence of a peptic fragment (Pep M5) of the group A streptococcal type 5 M protein, the antiphagocytic cell surface molecule of the bacteria, is described. This fragment, comprising nearly half of the native M molecule, is biologically active in that it has the ability to interact with opsonic antibodies as well as to evoke such an antibody response in rabbits. The sequence of Pep M5 was determined by automated Edman degradations of the uncleaved molecule and its… CONTINUE READING