Purification of Pili and Outer Membrane Vesicles of Neisseria gonorrhoeae by Wheat Germ Agglutinin Affinity Chromatography

Perera, V. Y.; Penn, Charles W.; Smith, H.

doi:10.1099/00221287-128-7-1613

Cited by 4 publications

(6 citation statements)

References 32 publications

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“…The outer membranes obtained were similar to the extracellular outer-membrane projections of B. pertussis reported by Morse and Morse (1 970) and resembled outer-membrane vesicles of gram-negative bacteria reported by others (Work et al, 1966;Perera et al, 1982). The localisation of pS1 in the cytoplasmic membranes conformed to the concept that most bacterial proteins destined for either the periplasm or the outer membrane are synthesised as precursors in the cytoplasmic membrane (Randall et al, 1978 ;Hall and Silhavy, 198 1 ;Pagks and Lazdunski, 1981).…”

Section: Discussionsupporting

confidence: 63%

Accumulation of a precursor of subunit S1 of pertussis toxin in cell envelopes of Bordetella pertussis in response to the membrane perturbant phenethyl alcohol

Perera

Freer

1987

Journal of Medical Microbiology

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Section: Discussionsupporting

confidence: 63%

Accumulation of a precursor of subunit S1 of pertussis toxin in cell envelopes of Bordetella pertussis in response to the membrane perturbant phenethyl alcohol

Perera

Freer

1987

Journal of Medical Microbiology

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“…Many Gram-negative bacteria shed the outer membrane in the form of vesicles which contain LPS (Work et al, 1966;Devoe & Gilchrist, 1973;Perera et al, 1982). Morse & Morse (1970) reported similar OMV in culture supernates of B. pertussis.…”

Section: Discussionmentioning

confidence: 96%

Release of Pertussis Toxin and Its Interaction With Outer-membrane Antigens

Perera

Wardlaw²,

Freer³

1987

Microbiology

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The absence of subunit S3 in cell-associated pertussis toxin (PT) from a mutant of Bordetella pertussis which failed to produce cell-free toxin suggested that this subunit was involved in the release of PT into the culture medium. The addition of methylated beta-cyclodextrin (MCD) to the culture medium caused a small but consistent increase in the release of lipopolysaccharide (LPS) by four wild-type strains of B. pertussis. Since previous studies have shown that MCD also enhances the levels of PT in culture supernates, it seemed probable that the increased shedding of outer-membranes vesicles (OMV) may explain the increased levels of both cell-free PT and LPS. Release of PT was inhibited in media buffered with HEPES but was unaffected in Tris/HC1 buffer. This suggested that in addition to shedding of the outer membrane, increased permeability and greater destabilization of the outer membrane, as caused by Tris/HC1 buffer, may be important in the release of PT. Our data do not support the idea that PT is packaged into OMV because only an insignificant proportion (0.01%) of the total cell-free PT was associated with LPS. The association of PT with small micelles derived from outer-membrane amphiphiles may be more important since the LPS content of PT purified from culture supernates (containing no large OMV) was nearly 18% by weight.

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“…The shape of the heterogeneously sized OMVs resembled those released by other members of Neisseriaceae family [35, 36]. We purified OMVs from eight K. kingae isolates of different origin.…”

Section: Discussionmentioning

confidence: 99%

Cytotoxic effects of Kingella kingae outer membrane vesicles on human cells

Maldonado

Wei

Kachlany

et al. 2011

Microbial Pathogenesis

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Kingella kingae is an emerging pathogen causing osteoarticular infections in pediatric patients. Electron microscopy of K. kingae clinical isolates revealed the heterogeneously-sized membranous structures blebbing from the outer membrane that were classified as outer membrane vesicles (OMVs). OMVs purified from the secreted fraction of a septic arthritis K. kingae isolate were characterized. Among several major proteins, K. kingae OMVs contained virulence factors RtxA toxin and PilC2 pilus adhesin. RtxA was also found secreted as a soluble protein in the extracellular environment indicating that the bacterium may utilize different mechanisms for the toxin delivery. OMVs were shown to be hemolytic and possess some leukotoxic activity while high leukotoxicity was detected in the non-hemolytic OMV-free component of the secreted fraction. OMVs were internalized by human osteoblasts and synovial cells. Upon interaction with OMVs, the cells produced increased levels of human granulocyte-macrophage colony-stimulating factor (GM-CSF) and interleuskin 6 (IL-6) suggesting that these cytokines might be involved in the signaling response of infected joint and bone tissues during natural K. kingae infection. This study is the first report of OMV production by K. kingae and demonstrates that OMVs are a complex virulence factor of the organism causing cytolytic and inflammatory effects on host cells.

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Purification of Pili and Outer Membrane Vesicles of Neisseria gonorrhoeae by Wheat Germ Agglutinin Affinity Chromatography

Cited by 4 publications

References 32 publications

Accumulation of a precursor of subunit S1 of pertussis toxin in cell envelopes of Bordetella pertussis in response to the membrane perturbant phenethyl alcohol

Accumulation of a precursor of subunit S1 of pertussis toxin in cell envelopes of Bordetella pertussis in response to the membrane perturbant phenethyl alcohol

Release of Pertussis Toxin and Its Interaction With Outer-membrane Antigens

Cytotoxic effects of Kingella kingae outer membrane vesicles on human cells

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