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Infection and Immunity, December 1999, p. 6526-6532, Vol. 67, No. 12
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Human Opsonins Induced during Meningococcal Disease Recognize Transferrin Binding Protein Complexes

A. K. Lehmann,1,* A. R. Gorringe,2 K. M. Reddin,2 K. West,2 I. Smith,1 and A. Halstensen1

Institute of Medicine, University of Bergen, N-5021 Bergen, Norway,1 and Centre for Applied Microbiology and Research, Salisbury SP4 0JG, United Kingdom2

Received 19 April 1999/Returned for modification 15 June 1999/Accepted 31 August 1999

Patient serum opsonins against transferrin binding protein A+B (TbpA+B) complexes from two Neisseria meningitidis strains (K454 and B16B6, with 85- and 68-kDa TbpB, respectively) were quantified by a functional phagocytosis and oxidative burst assay. TbpA+B complexes adsorbed to fluorescent beads were opsonized with individual acute and convalescent sera from 40 patients infected by a variety of meningococcal strains. Flow cytometric quantitation of leukocyte phagocytosis products (PP) demonstrated that disease-induced serum opsonins recognized TbpA+B, and the highest anti-TbpA+B serum opsonic activities were found between admission to hospital and 6 weeks later. The PP values obtained with TbpA+B from strain B16B6 (PPB16B6) were higher than those obtained with TbpA+B from strain K454 (PPK454), with both acute and convalescent sera (P < 0.0001), and correlated positively with higher immunoglobulin G enzyme-linked immunosorbent assay titers against TbpA+B from strain B16B6 than from strain K454 (P < 0.001). In spite of considerable variations between individuals, significant correlations were found between the PPB16B6 and PPK454 values, and the PP values did not depend on the variability of the TbpB proteins of the disease-causing strains. Simultaneously measured oxidative burst activity correlated closely with the PP values. We conclude that highly cross-reactive anti-TbpA+B serum opsonins are produced during meningococcal disease. The anti-TbpA+B opsonic activities were not affected by the variability of the TbpB proteins of the disease-causing strains, which further adds to the evidence for the vaccine potential of meningococcal TbpA+B complexes.

* Corresponding author. Mailing address: Institute of Medicine, University of Bergen, Haukeland University Hospital, N-5021 Bergen, Norway. Phone: (47) 55975000. Fax: (47) 55972950. E-mail: Anne.Lehmann{at}medb.uib.no.

Infection and Immunity, December 1999, p. 6526-6532, Vol. 67, No. 12
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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