The Genus Yersinia: Biochemistry and Genetics of Virulence With 3 Figures

Brubaker, Robert R.

doi:10.1007/978-3-642-65297-4_4

Cited by 131 publications

(123 citation statements)

References 158 publications

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“…The carbohydrate components of FI B , FI V and FI S appeared to be different and all contained phospholipid or galactolipid but not glycolipid ( [3,7,17]. These data con®rmed the hypothesis of Chen and Meyer that Y. pestis has a carbohydrate microcapsule located just under a protein envelope [10].…”

Section: Discussionsupporting

confidence: 57%

“…On the other hand, FI is considered to be a glycoprotein [1,7,17] whose synthesis is determined not only by caf plasmid genes, but also chromosomal genes. Futhermore, it is still unclear whether Y. pestis cells produce a morphologically distinct capsule (capsular antigen) or undifferentiated envelope (envelope antigen) [3]. The aim of this study was the immunochemical characterisation of subunits composing the FI antigen and their probable genetic control.…”

Section: Introductionmentioning

confidence: 99%

“…The structural gene for FI (caf1) and the associated genes (caf1M, caf1A and caf1R) have been cloned and sequenced and shown to be responsible for synthesis of a monomeric form of FI protein of 15±16 kDa [1,2]. FI is considered to be one of the species-speci®c antigens [1±12] and many serological diagnostic kits are based on detection of either FI antigen or antibodies to FI in serum [1,3].…”

Section: Introductionmentioning

confidence: 99%

“…At present, a non-speci®c character of some FI components has been reported [7, 13±16] that may be connected with lipopolysaccharide (LPS) contamination of FI preparations [3,5,17]. On the other hand, FI is considered to be a glycoprotein [1,7,17] whose synthesis is determined not only by caf plasmid genes, but also chromosomal genes.…”

Section: Introductionmentioning

confidence: 99%

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New genes involved in Yersinia pestis fraction I biosynthesis

Feodorova

Devdariani

2001

Journal of Medical Microbiology

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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-speci®c component of the FI complex molecule and is probably encoded by chromosomal genes. It, like caf1 product, was expressed in higher quantities at 378C than at 288C. Among FI subunits there were at least two proteins of 28 6 2 kDa and 43 6 2 kDa which were not speci®c for Y. pestis but were found also in all Yersinia spp. and some other bacteria. These proteins were synthesised independently of the incubation temperature (48±408C) and are possibly encoded chromosomally but outside the caf operon and galactolipid-encoding genes. Both proteins together with galactolipid comprise an envelope antigen found in pFra 2 or plasmidless Y. pestis strains. Organisation of Y. pestis FI (mature capsular antigen) in the form of a complex of the envelope antigen and the caf1 product is discussed.

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Section: Discussionsupporting

confidence: 57%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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New genes involved in Yersinia pestis fraction I biosynthesis

Feodorova

Devdariani

2001

Journal of Medical Microbiology

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“…Ymt is encoded on a 110 kb plasmid that is unique to the bacterium causing the plague (Cherepanov, 1991) and is a known determinant for plague virulence. It is thought to play a role in Y. pestis pathogenicity, both in the rodent host and in the flea vector (Brubaker, 1972;Cao et al, 1997). Ymt comprises 586 amino acids, and, as in most members of the PLD enzymes, from plants, bacteria or mammalians, it contains, in two separate parts of the protein, two copies of the conserved motif HXKX 4 DX 6 G(G/S), which are both essential for the enzyme activity.…”

Section: Pld (Phospholipase D) Activitymentioning

confidence: 99%

Bacterial protein toxins and lipids: role in toxin targeting and activity

Geny

Popoff

2006

Biology of the Cell

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All bacterial toxins, which globally are hydrophilic proteins, interact first with their target cells by recognizing a surface receptor, which is either a lipid or a lipid derivative, or another compound but in a lipid environment. Intracellular active toxins follow various trafficking pathways, the sorting of which is greatly dependent on the nature of the receptor, notably lipidic receptor or receptor embedded into a distinct environment such as lipid microdomains. Numerous other toxins act locally on cell membrane. Indeed, phospholipase activity is a common mechanism shared by several membrane‐damaging toxins. In addition, many toxins active intracellularly or on cell membrane modulate host cell phospholipid pathways. Unusually, a few bacterial toxins require a lipid post‐translational modification to be active. Thereby, lipids are obligate partners of bacterial toxins.

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Attenuated Bacterial Vaccines

Titball

Atkins

2012

Vaccinology

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The Genus Yersinia: Biochemistry and Genetics of Virulence With 3 Figures

Cited by 131 publications

References 158 publications

New genes involved in Yersinia pestis fraction I biosynthesis

New genes involved in Yersinia pestis fraction I biosynthesis

Bacterial protein toxins and lipids: role in toxin targeting and activity

Attenuated Bacterial Vaccines

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