Open AccessCloning and characterization of a major surface protein (MspTL) of Treponema lecithinolyticum associated with rapidly progressive periodontitis
Author(s) -
Park KwangKyun,
Heuner Klaus,
B. Göbel Ulf,
Yoo YunJung,
Kim ChongKwan,
Choi BongKyu
Publication year - 2002
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2002.tb11049.x
Subject(s) - open reading frame , homology (biology) , treponema , gene , southern blot , microbiology and biotechnology , biology , locus (genetics) , nucleic acid sequence , amino acid , peptide sequence , genetics , molecular cloning , signal peptide , sequence analysis , western blot , protein primary structure , virology , syphilis , human immunodeficiency virus (hiv)
The gene encoding a major surface protein (MspTL) of Treponema lecithinolyticum , a periodontopathogen, was cloned and sequenced. The mspTL gene has a 1770‐bp open reading frame (ORF) encoding a protein of 590 amino acids with a predicted molecular mass of 65 kDa which had a typical prokaryotic signal sequence (19 amino acids). MspTL showed a high level of homology with major sheath protein (MspA) of Treponema maltophilum , phylogenetically the closest relative of T. lecithinolyticum . Southern blot analysis indicated that the mspTL gene exists in a single copy and Northern blot analysis showed that the mspTL transcript is monocistronic. Another ORF located downstream of mspTL was in the same orientation and encoded a putative protein, in which the first N‐terminal 291 amino acids were identified. The homologous region of this protein is also a part on the T. maltophilum mspA locus.