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Infect Immun, May 1998, p. 2143-2153, Vol. 66, No. 5
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Active and Passive Immunity against Borrelia
burgdorferi Decorin Binding Protein A (DbpA) Protects
against Infection
Mark S.
Hanson,1,*
David R.
Cassatt,1
Betty P.
Guo,2,
Nita K.
Patel,1
Michael P.
McCarthy,1
David W.
Dorward,3 and
Magnus
Höök2
MedImmune, Inc., Gaithersburg, Maryland
208781;
Department of Biochemistry & Biophysics, Center for Extracellular Matrix Biology, Albert B. Alkek
Institute of Biosciences and Technology, Texas A&M University,
Houston, Texas 770302; and
Microscopy Branch, Rocky Mountain Laboratories, National
Institute of Allergy and Infectious Diseases, National Institutes
of Health, Hamilton, Montana 598403
Received 19 September 1997/Returned for modification 26 November
1997/Accepted 19 February 1998
Borrelia burgdorferi, the spirochete that causes Lyme
disease, binds decorin, a collagen-associated extracellular matrix
proteoglycan found in the skin (the site of entry for the spirochete)
and in many other tissues. Two borrelial adhesins that recognize this proteoglycan, decorin binding proteins A and B (DbpA and DbpB, respectively), have recently been identified. Infection of mice by
low-dose B. burgdorferi challenge elicited antibodies
against DbpA and DbpB that were sustained at high levels, suggesting
that these antigens are expressed in vivo. Scanning immunoelectron microscopy showed that DbpA was surface accessible on intact borreliae. Passive administration of DbpA antiserum protected mice from infection following challenge with heterologous B. burgdorferi sensu
stricto isolates, even when serum administration was delayed for up to 4 days after challenge. DbpA is the first antigen target identified that is capable of mediating immune resolution of early, localized B. burgdorferi infections. DbpA immunization also protected
mice from B. burgdorferi challenge; DbpB immunization was
much less effective. DbpA antiserum inhibited in vitro growth of many
B. burgdorferi sensu lato isolates of diverse geographic,
phylogenetic, and clinical origins. In combination, these findings
support a role for DbpA in the immunoprophylaxis of Lyme disease and
suggest that DbpA vaccines have the potential to eliminate early-stage B. burgdorferi infections.
*
Corresponding author. Mailing address: MedImmune, Inc.,
35 West Watkins Mill Rd., Gaithersburg, MD 20878. Phone: (301)
527-4264. Fax: (301) 527-4200. E-mail: hansonm{at}medimmune.com.

Present address: Department of Microbiology and Molecular Genetics,
Harvard Medical School, Boston, MA 02115.
Infect Immun, May 1998, p. 2143-2153, Vol. 66, No. 5
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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