Antigenic and phenotypic modifications of Yersinia pestis under calcium and glucose concentrations simulating the mammalian bloodstream environment.

To study the possible mechanism of extracellular resistance to phagocytes developed by Yersinia pestis in the early stage of plague infection, the behaviour of two Y. pestis strains, the vaccine EV-76 and fully virulent 231 (LD(50), 10 c.f.

Heat-stable serogroup-specific proteins of Yersinia pseudotuberculosis.

A library of mAbs to the species- and serogroup-specific epitopes of Yersinia pseudotuberculosis serogroups I-VI was developed. These mAbs recognized linear sequential protein epitopes, as shown by ELISA and immunoblotting. Using the mAbs, Y.

The interaction of Yersinia pestis with erythrocytes.

Human and murine erythrocytes (RBC) were invaded by Yersinia pestis in vivo and in vitro during a short period and were probably used as an essential source of iron and porphyrin for survival, effective gross multiplication and rapid spread of these bacteria in the bloodstream of mammals. Both iron and porphyrin were extracted by Y. pestis from the RBC through oxidase-catalase activity which produced oxidation of the RBC glucose with generation of H2O2 in large concentration leading to oxidative transformation of haemoglobin into haemin.

Expression of acid-stable proteins and modified lipopolysaccharide of Yersinia pestis in acidic growth medium.

Growth medium simulating the phagolysosomal environment in which Yersinia pestis resides during its intracellular growth in vivo was made by acidification of Ca2+-deficient medium. When used for cultivation of Y. pestis EV-76 (pLCR+;pPst+;pFra+) and its isogenic derivatives--KM-217 (pLCR+;pPst-;pFra-) and KM-218 (pLCR-;Ppst-; pFra-)--this medium permitted survival and proliferation of viable bacteria without any growth restriction.

New genes involved in Yersinia pestis fraction I biosynthesis.

Antigenic and immunochemical properties of Yersinia pestis fraction I (FI) preparations extracted by different methods were studied with polyclonal and monoclonal antibodies. The existence of mature FI in a form of a complex antigen whose subunits have different genetic control was demonstrated. Galactolipid was shown, with caf1 product, to be the second species-specific component of the FI complex molecule and is probably encoded by chromosomal genes.

Immunochemical characterisation of Vibrio cholerae O139 O antigens and production of a diagnostic antiserum without absorption.

Rabbits and mice immunised with chemically extracted O-antigens (O-Ags) of Vibrio cholerae O139 (O-AgB and O-AgD) developed antibodies (Abs) which appeared to be highly specific in ELISA for the relevant antigens and V. cholerae O139 strains without absorption, in contrast to the Abs against the heated O-Ag (O-AgH). An ELISA test based on the use of these Abs was shown to detect V.

Immunogeneity and structural organisation of some pLCR-encoded proteins of Yersinia pestis.

A novel method of cultivation of Yersinia pestis EV-76 and its isogenic strains KM-217 (pPst-;pCad+;pFra-) and KM-218 (pPst-;pCad-;pFra-) and careful extraction of Y. pestis proteins (YPPs) permitted isolation of >35 low Ca2+ response plasmid (pLCR)-encoded products, some of which are potentially new members of the LCR family. Immunisation with each YPP demonstrated that 25-, 54-, 72- and 87-kDa YPPs provided the highest level of protection in mice challenged with Y.

Development, characterisation and diagnostic application of monoclonal antibodies against Yersinia pestis fibrinolysin and coagulase.

A library of monoclonal antibodies (MAbs) which recognised different epitopes of Yersinia pestis fibrinolysin (Fib) was developed. These MAbs were species-specific and demonstrated no cross-reaction in indirect immunofluorescence tests (IIFT) with other gram-negative bacteria possessing plasminogen activator activity. All the MAbs provided equally high levels of immunofluorescence with pPst+ Y.

Identification of Yersinia pestis with varied plasmid composition using monoclonal and polyclonal fluorescent immunoglobulins.

The efficiency of serological identification of Yersinia pestis strains which contain different plasmids was assessed with polyclonal and monoclonal immunoglobulin preparations in the direct fluorescent antibody method. Plague polyclonal luminescent immunoglobulins recognize only those Y. pestis strains which contain pPst, pFra plasmids or both.