Open AccessMolecular cloning and characterization of a novel leptospiral lipoprotein with OmpA domain
Author(s) -
Koizumi Nobuo,
Watanabe Haruo
Publication year - 2003
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 - 10.1016/s0378-1097(03)00619-0
Subject(s) - leptospira , virulence , biology , bacterial outer membrane , microbiology and biotechnology , pathogenic bacteria , antigen , fusion protein , virulence factor , cloning (programming) , virology , gene , recombinant dna , bacteria , genetics , escherichia coli , serotype , computer science , programming language
Abstract A novel antigenic protein of pathogenic Leptospira , Loa22, was identified by using the PhoA fusion method followed by immunoblotting with convalescent mouse sera. Loa22 was shown to be a lipoprotein having a C‐terminal OmpA consensus domain. Loa22 was detected among pathogenic leptospires but not among non‐pathogenic leptospires, suggesting the possible involvement of this protein in virulence. The results of three different experiments suggested that Loa22 is located in the outer membrane and a small portion is exposed on the cell surface. Thus, Loa22 may be a candidate for a novel vaccine against infection with pathogenic leptospires.