Literature DB >> 19428838

Pleiotropic effects of the lpxM mutation in Yersinia pestis resulting in modification of the biosynthesis of major immunoreactive antigens.

V A Feodorova1, L N Pan'kina, E P Savostina, O S Kuznetsov, N P Konnov, L V Sayapina, S V Dentovskaya, R Z Shaikhutdinova, S A Ageev, B Lindner, A N Kondakova, O V Bystrova, N A Kocharova, S N Senchenkova, O Holst, G B Pier, Y A Knirel, A P Anisimov, V L Motin.   

Abstract

Deletion mutants in the lpxM gene in two Yersinia pestis strains, the live Russian vaccine strain EV NIIEG and a fully virulent strain, 231, synthesise a less toxic penta-acylated lipopolysaccharide (LPS). Analysis of these mutants revealed they possessed marked reductions in expression and immunoreactivity of numerous major proteins and carbohydrate antigens, including F1, Pla, Ymt, V antigen, LPS, and ECA. Moreover, both mutants demonstrated altered epitope specificities of the antigens as determined in immunodot-ELISAs and immunoblotting analyses using a panel of monoclonal antibodies. The strains also differed in their susceptibility to the diagnostic plague bacteriophage L-413C. These findings indicate that the effects of the lpxM mutation on reduced virulence and enhanced immunity of the Y. pestis EV DeltalpxM is also associated with these pleiotropic changes and not just to changes in the lipid A acylation.

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Year:  2009        PMID: 19428838      PMCID: PMC2999740          DOI: 10.1016/j.vaccine.2009.02.020

Source DB:  PubMed          Journal:  Vaccine        ISSN: 0264-410X            Impact factor:   3.641


  62 in total

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  12 in total

1.  Structure-guided enzymology of the lipid A acyltransferase LpxM reveals a dual activity mechanism.

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