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Sequence analysis of the cloned streptococcal cell surface antigen I/II
Author(s) -
Kelly C.,
Evans P.,
Bergmeier L.,
Lee S.F.,
Progulske-Fox A.,
Hams A.C.,
Aitken A.,
Bleiweis A.S.,
Lehner T.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81632-1
Subject(s) - antigen , gene , streptococcus mutans , peptide sequence , serotype , biology , microbiology and biotechnology , transmembrane protein , transmembrane domain , alanine , signal peptide , amino acid , chemistry , genetics , bacteria , receptor
The gene spa P (formerly designated as spa P1) encoding the M r 185,000 surface antigen (I/II) of Streptococcus mutons , 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 α‐helical. However, the C‐ternunal 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‐Tenninal 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.