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¹ Centre for Molecular Microbiology and Infection, Department of Microbiology, Imperial College London, London SW7 2AZ, England, UK
² Reference Laboratory for Neisseria, National Center of Microbiology, Institute of Health Carlos III, 28220 Majadahonda, Madrid, Spain
³ National Institute of Biological Standards and Control, South Mimms, Potters Bar, Hertfordshire EN6 3QG, England, UK
⁴ JEOL (UK) Ltd., JEOL House, Silvercourt, Watchmead, Welwyn Garden City, Hertfordshire AL7 1LT, England, UK
⁵ Vaccine Evaluation Unit, North West Regional HPA Laboratory, Manchester Royal Infirmary, Manchester M13 9WZ, England, UK

CORRESPONDENCE Christoph M. Tang: c.tang{at}imperial.ac.uk

The presence of serum bactericidal antibodies is a proven correlate of protection against systemic infection with the important human pathogen Neisseria meningitidis. We have identified three serogroup C N. meningitidis (MenC) isolates recovered from patients with invasive meningococcal disease that resist killing by bactericidal antibodies induced by the MenC conjugate vaccine. None of the patients had received the vaccine, which has been successfully introduced in countries in North America and Europe. The increased resistance was not caused by changes either in lipopolysaccharide sialylation or acetylation of the 2-9–linked polysialic acid capsule. Instead, the resistance of the isolates resulted from the presence of an insertion sequence, IS1301, in the intergenic region (IGR) between the sia and ctr operons, which are necessary for capsule biosynthesis and export, respectively. The insertion sequence led to an increase in the transcript levels of surrounding genes and the amount of capsule expressed by the strains. The increased amount of capsule was associated with down-regulation of the alternative pathway of complement activation, providing a generic mechanism by which the bacterium protects itself against bactericidal antibodies. The strains with IS1301 in the IGR avoided complement-mediated lysis in the presence of bactericidal antibodies directed at the outer membrane protein, PorA, or raised against whole cells.

© 2008 Uria et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jgp.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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