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Infection and Immunity, December 2001, p. 7616-7624, Vol. 69, No. 12
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.12.7616-7624.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Molecular Characterization of Thermoinduced Immunogenic Proteins Q1p42 and Hsp15 of Leptospira interrogans

Jarlath E. Nally,dagger Sergey Artiushin, and John F. Timoney*

Department of Veterinary Science, University of Kentucky, Lexington, Kentucky 40546-0099

Received 20 June 2001/Returned for modification 27 August 2001/Accepted 26 September 2001

Leptospira interrogans is a mammalian pathogen which must adapt to a range of new environmental conditions including temperature change when it infects new hosts. In vitro studies of organisms cultured at 30°C and shifted to 37°C for 5 to 7 days have confirmed that synthesis of several proteins involved in equine infection is regulated in response to temperature change (J. E. Nally, J. F. Timoney, and B. Stevenson, Infect. Immun. 69:400-404, 2001). In order to specifically identify antigenic proteins upregulated at 37°C, groups of three ponies were immunized with organisms shifted to 37°C for 5 to 7 days or with organisms maintained at 30°C. A lambda ZAP II genomic DNA library was screened with the pool of antisera to organisms shifted to 37°C. Clones reactive with this pool but unreactive with the pool of pony antisera to organisms cultured at 30°C were selected for further analysis. Sequence analysis of the first two clones identified open reading frames for proteins designated Qlp42 and Hsp15. Qlp42 is predicted to be an outer membrane lipoprotein. Its synthesis was upregulated when cultures were shifted from 30 to 37°C and downregulated when cultures were shifted from 37 to 30°C. Although the predicted molecular mass of Qlp42 is 39.8 kDa for the mature protein, Qlp42-specific equine antiserum was reactive with two bands of 30 and 29.5 kDa. Hsp15 is a stress response protein and a member of the Hsp20/alpha -crystallin family. PCR detected homologues of qlp42 and hsp15 in pathogenic serovars of L. interrogans but not in the nonpathogenic Leptospira biflexa. Enzyme-linked immunosorbent assays of antibody in convalescent sera from mares naturally infected with L. interrogans suggest that Qlp42 is expressed during leptospiral infection.

* Corresponding author. Mailing address: 108 Maxwell H. Gluck Equine Research Center, Department of Veterinary Science, University of Kentucky, Lexington, KY 40546-0099. Phone: (859) 257-4172. Fax: (859) 257-5169. E-mail: jtimoney{at}pop.uky.edu.

dagger Present address: Division of Infectious Diseases, Department of Medicine, University of California at Los Angeles, Los Angeles, CA 90095.

Infection and Immunity, December 2001, p. 7616-7624, Vol. 69, No. 12
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.12.7616-7624.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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