Release of Outer Membrane Vesicles from Bordetella pertussis

1999 ◽  
Vol 38 (5) ◽  
pp. 273-278 ◽  
Author(s):  
D. Hozbor ◽  
M.E. Rodriguez ◽  
J. Fernández ◽  
A. Lagares ◽  
N. Guiso ◽  
...  
2020 ◽  
Vol 11 ◽  
Author(s):  
Maia L. Elizagaray ◽  
Marco Túlio R. Gomes ◽  
Erika S. Guimaraes ◽  
Martín Rumbo ◽  
Daniela F. Hozbor ◽  
...  

2018 ◽  
Vol 5 (2) ◽  
pp. 43-46
Author(s):  
M Sekhavati ◽  
SD Siadat ◽  
M Noofeli ◽  
A Mohebati Mobarez ◽  
◽  
...  

Vaccine ◽  
2011 ◽  
Vol 29 (8) ◽  
pp. 1649-1656 ◽  
Author(s):  
Cristian J.A. Asensio ◽  
María Emilia Gaillard ◽  
Griselda Moreno ◽  
Daniela Bottero ◽  
Eugenia Zurita ◽  
...  

2020 ◽  
Vol 14 (3) ◽  
pp. 213-226
Author(s):  
Maryam Sadat Soltani ◽  
Fereshteh Eftekhar ◽  
Fereshteh Shahcheraghi ◽  
Mojtaba Noofeli ◽  
Seyed Reza Banihashemi ◽  
...  

Author(s):  
Mohammad Sekhavati ◽  
Ashraf Mohabati Mobarez ◽  
Seyed Davar Siadat ◽  
Mojtaba Noofeli

Background and Objectives: There are many pertussis outbreaks which is mainly due to the reduction in the immunity of acellular pertussis (aP) vaccines. Therefore, there is a crucial necessity to develop a new generation of pertussis vaccine. Pre- ceding researches have shown that Bordetella pertussis outer membrane vesicles (OMVs) have appropriate specifications, making them a suitable vaccine candidate against pertussis. Materials and Methods: The OMVs were separated by a new serial ultra centrifugation technique. Transmission electron microscopy (TEM) examination, SDS-PAGE, Western blotting and ELISA assay were used to characterize the OMVs. Results: TEM studies showed the size of the extracted OMVs at 40-200 nm. The presence of pertussis toxin, filamentous hemagglutinin, and pertactin was verified using Western blot and ELISA assay. Conclusion: The presented technique is a simple and effective way to obtain OMVs from Bordetella pertussis. So it can be utilized as an appropriate procedure in the development of an OMV-based vaccine against pertussis.  


2021 ◽  
Vol 25 (6) ◽  
pp. 399-407
Author(s):  
Maryam sadat Soltani ◽  
Mojtaba Noofeli ◽  
Seyed Reza Banihashemi ◽  
Fereshteh Shahcheraghi ◽  
Fereshteh Eftekhar ◽  
...  

2019 ◽  
Author(s):  
Jiajun Wang ◽  
Rémi Terrasse ◽  
Jayesh Arun Bafna ◽  
Lorraine Benier ◽  
Mathias Winterhalter

Multi-drug resistance in Gram-negative bacteria is often associated with low permeability of the outer membrane. To investigate the role of membrane channels in the uptake of antibiotics, we extract, purify and reconstitute them into artificial planar membranes. To avoid this time-consuming procedure, here we show a robust approach using fusion of native outer membrane vesicles (OMV) into planar lipid bilayer which moreover allows also to some extend the characterization of membrane protein channels in their native environment. Two major membrane channels from <i>Escherichia coli</i>, OmpF and OmpC, were overexpressed from the host and the corresponding OMVs were collected. Each OMV fusion revealed surprisingly single or only few channel activities. The asymmetry of the OMV´s translates after fusion into the lipid membrane with the LPS dominantly present at the side of OMV addition. Compared to conventional reconstitution methods, the channels fused from OMVs containing LPS have similar conductance but a much broader distribution. The addition of Enrofloxacin on the LPS side yields somewhat higher association (<i>k<sub>on</sub></i>) and lower dissociation (<i>k<sub>off</sub></i>) rates compared to LPS-free reconstitution. We conclude that using outer membrane vesicles is a fast and easy approach for functional and structural studies of membrane channels in the native membrane.


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