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Identification and Structural Characterisation of Novel Outer Membrane Proteins in the genus Borrelia

Dyer, Adam (2013) Identification and Structural Characterisation of Novel Outer Membrane Proteins in the genus Borrelia. Doctoral thesis, University of Huddersfield.

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Although considered Gram-negative the outer membrane (OM) of Borrelia is unique, consisting of a variety of glycolipids, a significant number of surface exposed lipoproteins and a smaller number of integral membrane-spanning β-barrels. Many of these proteins are known to act as adhesins and invasins binding to regulators of the host immune response and extracellular matrix proteins. Many Gram-negative bacteria have the evolutionary conserved OmpA-like transmembrane domain consisting of an eight-stranded membrane spanning β- barrel. The prototypical example is E. coli OmpA; a multifunctional protein involved in a wide variety of physiological and pathological functions. To date the OmpA-like transmembrane domain has not been identified in the Spirochaete phylum. An approach based on hidden Markov models and topology and fold prediction identified a group of homologous genes in the genus Borrelia (BAPKO_0026, BAPKO_0422, BAPKO_0423 and BAPKO_0571), which are predicted to form an eight stranded OM-spanning β-barrel structure with similar structure to E. coli OmpA/W. One of these orthologues in B. afzelii (BAPKO_0422) has been expressed, purified and characterised in vitro; circular dichroism studies show a large percentage of β-strand. A low resolution molecular envelope generated from small-angle X-ray scattering data is consistent with an eight-stranded β-barrel.

Item Type: Thesis (Doctoral)
Subjects: Q Science > Q Science (General)
Schools: School of Applied Sciences
Depositing User: Rosemary Wood
Date Deposited: 10 Dec 2013 13:11
Last Modified: 28 Aug 2021 19:31


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