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Infection and Immunity, May 2001, p. 3335-3342, Vol. 69, No. 5
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.5.3335-3342.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Monoclonal Antibodies Specific for Neisseria meningitidis Group B Polysaccharide and Their Peptide Mimotopes

J. S. Shin,1,dagger J. S. Lin,1 P. W. Anderson,1 R. A. Insel,1 and M. H. Nahm1,2,*

Department of Pediatrics1 and Department of Pathology,2 University of Rochester School of Medicine and Dentistry, Rochester, New York 14642

Received 13 November 2000/Returned for modification 8 January 2001/Accepted 29 January 2001

From five mice immunized with Escherichia coli K1 bacteria, we produced 12 immunoglobulin M hybridomas secreting monoclonal antibodies (MAbs) that bind to Neisseria meningitidis group B (NMGB). The 12 MAbs also bound the capsular polysaccharide (PS) of E. coli K1 [which, like NMGB, is alpha (2-8)-linked polysialic acid (PSA)] and bound to EV36, a nonpathogenic E. coli K-12 strain producing alpha (2-8) PSA. Except for HmenB5, which cross-reacted with N. meningitidis group C, none of the MAbs bound to N. meningitidis groups A, C, and Y. Of the 12 MAbs, 6 were autoantibodies as defined by binding to CHP-134, a neuroblastoma cell line expressing short-chain alpha (2-8) PSA; five of these MAbs killed NMGB in the presence of rabbit complement, and two also killed NMGB with human complement. The other six MAbs, however, were nonautoreactive; all killed NMGB with rabbit complement, and five killed NMGB with human complement. To obtain peptide mimotopes of NMGB PS, four of the nonautoreactive MAbs (HmenB2, HmenB3, HmenB13, and HmenB14) were used to screen two types of phage libraries, one with a linear peptide of 7 amino acids and the other with a circular peptide of 7 amino acids inserted between two linked cysteines. We obtained 86 phage clones that bound to the screening MAb in the absence but not in the presence of E. coli K1 PSA in solution. The clones contained 31 linear and 4 circular mimotopes expressing unique sequences. These mimotopes nonrandomly expressed amino acids and were different from previously described mimotopes for NMGB PS. The new mimotopes may be useful in producing a vaccine(s) capable of eliciting anti-NMGB antibodies not reactive with neuronal tissue.

* Corresponding author. Mailing address: University of Rochester School of Medicine and Dentistry, Departments of Pediatrics and Pathology, 601 Elmwood Ave., Box 608, Rochester, NY 14642. Phone: (716) 273-4157. Fax: (716) 273-1101. E-mail: moon_nahm{at}urmc.rochester.edu.

dagger Present address: Department of Microbiology, College of Medicine, Yonsei University, Seoul (120-752), Korea.

Infection and Immunity, May 2001, p. 3335-3342, Vol. 69, No. 5
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.5.3335-3342.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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