St Andrews Research Repository

St Andrews University Home
View Item 
  •   St Andrews Research Repository
  • Chemistry (School of)
  • Chemistry
  • Chemistry Theses
  • View Item
  •   St Andrews Research Repository
  • Chemistry (School of)
  • Chemistry
  • Chemistry Theses
  • View Item
  •   St Andrews Research Repository
  • Chemistry (School of)
  • Chemistry
  • Chemistry Theses
  • View Item
  • Login
JavaScript is disabled for your browser. Some features of this site may not work without it.

Structural and functional studies of porins from pathogenic bacteria

Thumbnail
View/Open
LuanaFerraraPhDThesis.pdf (79.75Mb)
Date
2018
Author
Ferrara, Luana
Supervisor
Naismith, Jim
Metadata
Show full item record
Altmetrics Handle Statistics
Abstract
Multi-drug resistant bacteria have become a real threat to public health worldwide. Gram-negative bacteria, in particular, have shown high level of antibiotic resistance due to the presence of an additional membrane, known as outer-membrane (OM), that acts as an extra barrier. Most antibiotics enter the cells via a particular class of outer-membrane proteins (OMPs) known as porins. Porins are β-barrel channels that allow the passive diffusion of hydrophobic compounds. The porins are known to select against molecules on the basis of size and charge. When exposed to antibiotics, bacteria can modify the OM permeability by altering their porins profile. Mutations affecting the size and conductivity of the pore channel, and modification of the level of porins expression are just a few examples of how the bacteria can decrease the influx of antibiotics. In order to better understand their interaction with antibiotics, this thesis presents structural and functional studies on porins from pathogenic bacteria. The structure of the natively expressed major outer-membrane protein (MOMP) from Campylobacter jejuni was determines, revelling the presence of a calcium-binding site inside the channel. Electro-physiology and in silico modelling analysis have shown to be important for the stability and the function of the protein. Omp50 from C. jejuni was expressed in E. Coli and its tyrosine kinase activity was analysed in vitro. Finally the structures of the two major porins from Enterobacter aerogens were determined and compared to their orthologs within the Enterobacteriaceae family. Further, a liposome-swelling assay (LSA) was used to deter-mine the rate of permeation of clinically relevant antibiotics through a series of porins. Combining these data allow a more detailed molecular understanding of translocation.
Type
Thesis, PhD Doctor of Philosophy
Collections
  • Chemistry Theses
URI
http://hdl.handle.net/10023/15639

Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.

Advanced Search

Browse

All of RepositoryCommunities & CollectionsBy Issue DateNamesTitlesSubjectsClassificationTypeFunderThis CollectionBy Issue DateNamesTitlesSubjectsClassificationTypeFunder

My Account

Login

Open Access

To find out how you can benefit from open access to research, see our library web pages and Open Access blog. For open access help contact: openaccess@st-andrews.ac.uk.

Accessibility

Read our Accessibility statement.

How to submit research papers

The full text of research papers can be submitted to the repository via Pure, the University's research information system. For help see our guide: How to deposit in Pure.

Electronic thesis deposit

Help with deposit.

Repository help

For repository help contact: Digital-Repository@st-andrews.ac.uk.

Give Feedback

Cookie policy

This site may use cookies. Please see Terms and Conditions.

Usage statistics

COUNTER-compliant statistics on downloads from the repository are available from the IRUS-UK Service. Contact us for information.

© University of St Andrews Library

University of St Andrews is a charity registered in Scotland, No SC013532.

  • Facebook
  • Twitter