Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Louse-borne relapsing fever, caused by Borrelia recurrentis, provides one of the best documented examples of the causative role of tumor necrosis factor (TNF) in the pathology of severe infection in humans. We have identified the principal TNF-inducing factor of B. recurrentis as a variable major lipoprotein (Vmp). Here we report the complete gene sequence of Vmp, including its lipoprotein leader sequence. Using metabolically labeled forms of the native Vmp we confirm that the TNF inducing properties are associated with the lipid portion of the molecule. Quadrupole orthogonal time of flight mass spectrometry unequivocally locates the lipidic moiety at the NH(2)-terminal cysteine of the native polypeptide, and indicates the existence of three forms which are consistent with the structures C16:0, C16:0, C16:0 glyceryl cysteine; C18:1, C16:0, C16:0 glyceryl cysteine; and C18:0, C16:0, C16:0 glyceryl cysteine. These data provide the first direct evidence that the TNF inducing lipid modification of native Borrelia lipoproteins is a structural homologue of the murein lipoprotein of Escherichia coli.

Original publication

DOI

10.1074/jbc.275.2.937

Type

Journal article

Journal

The Journal of biological chemistry

Publication Date

01/2000

Volume

275

Pages

937 - 941

Addresses

University Department of Paediatrics, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom.

Keywords

Monocytes, Cell Line, Humans, Borrelia, Relapsing Fever, Inflammation, Trypsin, Lipoproteins, Tumor Necrosis Factor-alpha, Peptide Fragments, Bacterial Outer Membrane Proteins, Antigens, Surface, Chromatography, High Pressure Liquid, Mass Spectrometry