Structure determination of the major outer membrane protein from Campylobacter jejuni & Structural and functional studies of the endonuclease from Lassa virus
Abstract
The major outer membrane protein, MOMP, is the main protein in the outer
membrane of pathogenic Campylobacter bacteria. Infection with Campylobacter is
the principle cause of severe enteritis and untreated may result in non-trauma
related paralysis. Studies have shown, that MOMP can act as antigen and thus has
the potential to provide protection by induced humoral immunity. In our study, we
expressed recombinant MOMP in Escherichia1coli, developed an alternative method
to extract the outer membrane protein from its lipid environment and solved and
characterised its crystal structure. The information acquired through these structural
studies sheds new light on the structural characteristics of this important membrane
protein.
The West-African Lassa virus can cause deadly haemorrhagic fever. Lassa virus only
possesses five proteins, which are synergistically responsible for the virus’ life cycle,
and virulence. The way in which the individual proteins act with one another and
with host cell proteins is not fully understood. The polymerase L is the largest of the
five proteins and has multiple functions. In this study, we first divided the L protein
into different domains and tested their recombinant expression in Escherichia1coli.
For first time, we solved the crystal structure of the putative endonuclease domain
of Lassa virus and validated its endonucleolytic function by means of RNA digestion
assays and alanine point mutations.
Type
Thesis, PhD Doctor of Philosophy
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