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Determining OMP topology by computation, surface plasmon resonance and cysteine labelling: The test case of OMPG

Lookup NU author(s): Virak Visudtiphole, Dr David Allen Chalton, Dr Qi Hong, Professor Jeremy LakeyORCiD


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Bacterial outer-membrane proteins (OMP) are important in pathogenicity and the recently solved structure of OmpG provides an excellent test case for topological predictions since it is monomeric. Here we compare the results of applying several computerised structure prediction algorithms to the sequence of OmpG. Furthermore, we probe the OmpG topology by both an established chemical labelling approach and a new method which combines epitope insertion and surface plasmon resonance. The computational approaches are broadly accurate but the exact choice of the number of β strands remains difficult. The algorithms also tend to predict the entire β strand rather than just the transmembrane region. Epitope insertion clearly pinpoints exposed loops but its utility in defining buried or periplasmic sites is less clear cut. Cysteine-mutant labelling is largely confined to exposed residues but one periplasmic cysteine may be labelled by reagents entering via the OmpG pore. © 2006.

Publication metadata

Author(s): Visudtiphole V, Chalton DA, Hong Q, Lakey JH

Publication type: Article

Publication status: Published

Journal: Biochemical and Biophysical Research Communications

Year: 2006

Volume: 351

Issue: 1

Pages: 113-117

ISSN (print): 0006-291X

ISSN (electronic): 1090-2104

Publisher: Academic Press


DOI: 10.1016/j.bbrc.2006.10.003

PubMed id: 17055462


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Funder referenceFunder name
48873Wellcome Trust