Sequence analysis of the cloned streptococcal cell surface antigen I/II.

نویسندگان

  • C Kelly
  • P Evans
  • L Bergmeier
  • S F Lee
  • A Progulske-Fox
  • A C Harris
  • A Aitken
  • A S Bleiweis
  • T Lehner
چکیده

The gene spa P (formerly designated as spa P1) encoding the Mr 185,000 surface antigen (I/II) of Streptococcus mutans, serotype c (NG5), has been sequenced. The gene (4683 bp) encodes a protein of 1561 amino acid residues including putative signal peptide (residues 1-38) and transmembrane (residues 1537-1556) sequences. The N-terminal region (60-550) has alanine-rich repeats and is predicted to be alpha-helical. However, the C-terminal region (800-1540) is proline-rich and favours an extended structure. Except for a short central variable region the sequences appear to be highly conserved for S. mutans serotype c. N-Terminal sequencing of separated antigen I and antigen II polypeptides suggests that the former represents the N-terminal and the latter the C-terminal portions of the intact antigen.

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عنوان ژورنال:
  • FEBS letters

دوره 258 1  شماره 

صفحات  -

تاریخ انتشار 1989