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Infection and Immunity, February 2001, p. 1009-1015, Vol. 69, No. 2
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.2.1009-1015.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

In Vitro and In Vivo Neutralization of the Relapsing Fever Agent Borrelia hermsii with Serotype-Specific Immunoglobulin M Antibodies

Alan G. Barbour1,2,* and Virgilio Bundoc2,dagger

Departments of Microbiology & Molecular Genetics and Medicine, University of California Irvine, Irvine, California 92697,1 and Department of Microbiology, University of Texas Health Science Center, San Antonio, Texas 287402

Received 5 June 2000/Returned for modification 3 August 2000/Accepted 27 September 2000

The antigenic variation of the relapsing fever agent Borrelia hermsii is associated with changes in the expression of the Vlp and Vsp outer membrane lipoproteins. To investigate whether these serotype-defining proteins are the target of a neutralizing and protective antibody response, monoclonal antibodies were produced from spleens of infected mice just after clearance of serotype 7 cells from the blood. Two immunoglobulin M monoclonal antibodies, H7-7 and H7-12, were studied in detail. Both antibodies specifically agglutinated serotype 7 cells and inhibited their growth in vitro. Administered to mice before or after infection, both antibodies provided protection against infection or substantially reduced the number of spirochetes in the blood of mice after infection. Whereas antibody H7-12 bound to Vlp7 in Western blotting, enzyme-linked immunosorbent assay, and immunoprecipitation assays, as well as to whole cells in other immunoassays, antibody H7-7 only bound to wet, intact cells of serotype 7. Antibody H7-7 selected against cells expressing Vlp7 in vitro and in vivo, an indication that Vlp7 was a conformation-sensitive antigen for the antibody. Vaccination of mice with recombinant Vlp7 with adjuvant elicited antibodies that bound to fixed whole cells of serotype 7 and to Vlp7 in Western blots, but these antibodies did not inhibit the growth of serotype 7 in vitro and did not provide protection against an infectious challenge with serotype 7. The study established that a Vlp protein was the target of a neutralizing antibody response, and it also indicated that the conformation and/or the native topology of Vlp were important for eliciting that immunity.

* Corresponding author. Mailing address: Department of Microbiology & Molecular Genetics, University of California, Irvine, CA 92660. Phone: (949) 824-5626. Fax: (949) 824-8598. E-mail: abarbour{at}uci.edu.

dagger Present address: ManorCare Health Services, 550 S. Carlin Springs Rd., Arlington, VA 20024.

Infection and Immunity, February 2001, p. 1009-1015, Vol. 69, No. 2
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.2.1009-1015.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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