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Infection and Immunity, May 2003, p. 2414-2421, Vol. 71, No. 5
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.5.2414-2421.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

LipL21 Is a Novel Surface-Exposed Lipoprotein of Pathogenic Leptospira Species

Paul A. Cullen,1 David A. Haake,2,3 Dieter M. Bulach,1 Richard L. Zuerner,4 and Ben Adler1*

Bacterial Pathogenesis Research Group, Department of Microbiology, Monash University, Melbourne, Victoria 3800, Australia,1 School of Medicine, University of California at Los Angeles, Los Angeles, California 90095,2 Divison of Infectious Diseases, Veteran Affairs Greater Los Angeles Healthcare System, Los Angeles, California 90073,3 Bacterial Diseases of Livestock Research Unit, National Animal Disease Center, Agricultural Research Service, U.S. Department of Agriculture, Ames, Iowa 500104

Received 16 December 2002/ Returned for modification 24 January 2003/ Accepted 6 February 2003

Leptospira is the etiologic agent of leptospirosis, a bacterial zoonosis distributed worldwide. Leptospiral lipopolysaccharide is a protective immunogen, but the extensive serological diversity of leptospires has inspired a search for conserved outer membrane proteins (OMPs) that may stimulate heterologous immunity. Previously, a global analysis of leptospiral OMPs (P. A. Cullen, S. J. Cordwell, D. M. Bulach, D. A. Haake, and B. Adler, Infect. Immun. 70:2311-2318, 2002) identified pL21, a novel 21-kDa protein that is the second most abundant constituent of the Leptospira interrogans serovar Lai outer membrane proteome. In this study, we identified the gene encoding pL21 and found it to encode a putative lipoprotein; accordingly, the protein was renamed LipL21. Southern hybridization analysis revealed the presence of lipL21 in all of the pathogenic species but in none of the saprophytic species examined. Alignment of the LipL21 sequence from six strains of Leptospira revealed 96 to 100% identity. When specific polyclonal antisera to recombinant LipL21 were used, LipL21 was isolated together with other known leptospiral OMPs by both Triton X-114 extraction and sucrose density gradient membrane fractionation. All nine strains of pathogenic leptospires investigated by Western blotting, whether culture attenuated or virulent, were found to express LipL21. In contrast, the expression of LipL21 or an antigenically related protein could not be detected in nonpathogenic L. biflexa. Infected hamster sera and two of eight human leptospirosis sera tested were found to react with recombinant LipL21. Native LipL21 was found to incorporate tritiated palmitic acid, consistent with the prediction of a lipoprotein signal peptidase cleavage site. Biotinylation of the leptospiral surface resulted in selective labeling of LipL21 and the previously known OMPs LipL32 and LipL41. These findings show that LipL21 is a surface-exposed, abundant outer membrane lipoprotein that is expressed during infection and conserved among pathogenic Leptospira species.

* Corresponding author. Mailing address: Bacterial Pathogenesis Research Group, Department of Microbiology, Monash University, Melbourne, Victoria 3800, Australia. Phone: 61 3 9905 4815. Fax: 61 3 9905 4811. E-mail: Ben.Adler{at}med.monash.edu.au.

Editor: J. T. Barbieri

Infection and Immunity, May 2003, p. 2414-2421, Vol. 71, No. 5
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.5.2414-2421.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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