Cold temperature-induced modifications to the composition and structure of the lipopolysaccharide of Yersinia pestis
Graphical abstract
Introduction
The natural environmental temperatures for Y. pestis, the cause of bubonic and pneumonic plague, may vary from 0 to 42 °C. Significant variations in the lipopolysaccharide (LPS) structure were observed when the bacteria are cultivated at 25–28 or 37 °C, including alternation of terminal core monosaccharides [d-glycero-d-manno-heptose (ddHep) vs d-galactose; 3-deoxy-d-manno-oct-2-ulosonic acid (Kdo) vs d-glycero-d-talo-octulosonic acid (Ko)]1 and change in the content of 4-amino-4-deoxy-l-arabinose (l-Ara4N) and the degree of acylation in lipid A.1, 2, 3 These variations were accompanied by alteration in the LPS bioactivity suggesting a role for overcoming the defense systems of both warm-blooded mammals (host) and cold-blooded insects (vector). We now studied the LPS structure in a Y. pestis strain grown at 6 °C (LPS-6) to mimic the conditions in animals during winter hibernation, and compared it with those of the LPS from the same strain cultivated at 25 and 37 °C (LPS-25 and LPS-37, respectively).
Section snippets
Results and discussion
LPS-6 was isolated by phenol/chloroform/light petroleum extraction from Y. pestis KM218 grown at 6 °C in a casein hydrolysate medium. In SDS-PAGE, the electrophoretic mobility of LPS-6 was practically the same as that for the previously described LPS-251 (data not shown).
The electrospray ionization Fourier transform ion-cyclotron resonance (ESI FTICR) mass spectrum of LPS-6 (not shown) indicated a mixture of two LPS types called LPS-6A and LPS-6B. The former was identified as one of the
Growth of bacteria, isolation of LPS, and SDS-PAGE
Y. pestis strain KM218, a plasmidless derivative of the Russian vaccine strain EV line NIIEG, was grown at 6 °C in liquid aerated media containing fish-flour hydrolysate and yeast autolysate as described.1 The lipopolysaccharide (LPS-6) was extracted from dried cells with phenol/CHCl3/light petroleum8 and purified by enzymatic digestion of nucleic acids and proteins followed by repeated ultracentrifugation (105,000g, 4 h). LPS-6B was extracted from the LPS-6 preparation by the Bligh & Dyer
Acknowledgments
This work was performed within the framework of the International Science and Technology Center (ISTC) Partner Project #1197, supported by the Cooperative Threat Reduction Program of the US Department of Defense (ISTC Partner). A.P.A. and R.Z.S. were also supported by the Contract #43.600.1.4.0031 from the Ministry for Industry, Science and Technology of Russia, and B.L. was supported by the German Research Foundation (grant LI4481). Authors thank H. Moll for help with fatty acid analysis.
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Present address: Institute for Biological Sciences, National Research Council, Ottawa, ON, Canada K1A 0R6.