Characterization of Brucella abortus and Brucella melitensis native haptens as outer membrane O-type polysaccharides independent from the smooth lipopolysaccharide.


:Brucella native haptens (NHs) extracted with hot water from smooth (S)-type B. abortus and B. melitensis were purified to high levels of serological activity and compared with the polysaccharide obtained by acid hydrolysis (PS) of the S lipopolysaccharide (S-LPS). By 13C nuclear magnetic resonance analysis, NHs showed the spectrum of a homopolymer of alpha-1,2- or alpha-1,2- plus alpha-1,3-linked 4-formamido-4,6-dideoxy-D-mannose (N-formylperosamine) previously reported for the LPS O chain. However, while PS contained up to 0.6% 3-deoxy-D-manno-2-octulosonate, this LPS-core marker was absent from NH. High performance liquid chromatography and thin-layer chromatography showed heterogeneity in NH purified from whole cells but not in PS. By immunoprecipitation, polysaccharides indistinguishable from NH were demonstrated in extracts obtained with phenol-water, saline at 60 degrees C, and ether-water treatments, and none of these treatments caused S-LPS hydrolysis detectable with antibodies to the O chain and lipid A. Two lines of evidence showed that NH was in the cell surface. First, NH became biotinylated when B. abortus live cells were labelled with biotin-hydrazide, and the examination of cell fractions and electron microscopy sections with streptavidin-peroxidase and streptavidin-coloidal gold, respectively, showed that labelling was extrinsic. Moreover, whereas only traces of NH were found in cytosols, the amount of NH was enriched in cell envelopes and in the outer membrane blebs spontaneously released by brucellae during growth. Interactions between NH and S-LPS were observed in crude cell extracts, and such interactions could be reconstituted by using purified NH and LPS. The results demonstrate that NH is not a hydrolytic product of S-LPS and suggest a model in which LPS-independent O-type polysaccharides (NH) are intertwined with the O chain in the outer membrane of S-type brucellae.


J Bacteriol


Journal of bacteriology


Aragón V,Díaz R,Moreno E,Moriyón I




Has Abstract


1996-02-01 00:00:00












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  • Characterization of chloramphenicol acetyltransferase from chloramphenicol-resistant Staphylococcus aureus.

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    authors: Shaw WV,Brodsky RF

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  • Genetic dissection of DNA binding and luminescence gene activation by the Vibrio fischeri LuxR protein.

    abstract::The Vibrio fischeri luminescence (lux) genes are regulated by the 250-amino-acid-residue LuxR protein and a V. fischeri metabolite termed autoinducer. The V. fischeri lux regulon consists of two divergently transcribed units. Autoinducer and LuxR activate transcription of the luxICDABE operon and autoregulate the luxR...

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    authors: Choi SH,Greenberg EP

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    authors: Schnetz K,Toloczyki C,Rak B

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    pub_type: 杂志文章


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    journal_title:Journal of bacteriology

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    journal_title:Journal of bacteriology

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    authors: Kingsbury DT

    更新日期:1967-09-01 00:00:00

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    journal_title:Journal of bacteriology

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    authors: Caffrey P,Owen P

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    authors: Kornitzer D,Teff D,Altuvia S,Oppenheim AB

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    journal_title:Journal of bacteriology

    pub_type: 杂志文章


    authors: Ureta A,Nordlund S

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    pub_type: 杂志文章


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    pub_type: 杂志文章


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