Structure of the transmembrane domain of Salmonella insertion protein B (SipB). Mechanism of insertion investigated by novel biophysical and computational methodologies.
The entry of Salmonella into host cells begins with the translocation of bacterial effector proteins into host cells, SipB is involved in this translocon formation and is thus critical to invasion. Our main objective was to obtain a detailed picture of the mechanism of membrane insertion and possib...
Saved in:
Main Author: | |
---|---|
Other Authors: | |
Format: | Research Report |
Language: | English |
Published: |
2008
|
Subjects: | |
Online Access: | http://hdl.handle.net/10356/14554 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Nanyang Technological University |
Language: | English |
Summary: | The entry of Salmonella into host cells begins with the translocation of bacterial effector proteins into host cells, SipB is involved in this translocon formation and is thus critical to invasion. Our main objective was to obtain a detailed picture of the mechanism of membrane insertion and possible oligomerisation of SipB.
Here we describe the recombinant expression of SipB in E.coli using a vector encoding the sequence of full-length SipB. Also documented are the challenges encountered in mass production of this protein for analysis.
In spite of not having any specific funding for this project (see comments in this and previous report) or manpower (not even one PhD student), we have managed to obtain some results and a URECA student experienced training in this project. |
---|