Premium
A 29.5 KDA Heat‐modifiable Major Outer Membrane Protein of Rickettsia Prowazekii, Putative Virulence Factor, is a Peptidyl‐Prolyl Cis/trans Isomerase
Author(s) -
Emelyanov Victor V.,
Loukianov Evgeny V.
Publication year - 2004
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540410001699321
Subject(s) - rickettsia prowazekii , virulence , bacterial outer membrane , biology , recombinant dna , gene , virulence factor , strain (injury) , escherichia coli , microbiology and biotechnology , biochemistry , rickettsia , genetics , virus , anatomy
Allelic genes from three Rickettsia prowazekii strains encoding parvulin‐like protein (Plp), a heat‐modifiable 29.5 kDa major outer membrane protein, were earlier cloned into expression vector pQE 30. In this work, recombinant proteins were overproduced in E. coli, purified, and found to exhibit an expected peptidyl‐prolyl cis/trans isomerase activity of a parvulin type in vitro with oligopeptide substrates. Native polypeptide of prototype virulent Breinl strain is known to differ by SDS ‐ PAGE mobility from those of both vaccine Madrid E and virulent EVir isolates. Being different in electrophoretic behavior, heat‐unmodified forms of the three strains were shown to migrate apart from lipopolysaccharides. A EVir Plp gene was sequenced, and deduced protein sequence was found to be identical to previously published Breinl and Madrid E. Present data indicate that unknown post‐translational modification(s) in rickettsiae are responsible for both interstrain difference and heat‐modifiability of Plp.IUBMB Life, 56: 215‐219, 2004