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Infection and Immunity, January 2002, p. 323-334, Vol. 70, No. 1
0019-9567/01/$04.00+0     DOI: 10.1128/IAI.70.1.323-334.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Novel 45-Kilodalton Leptospiral Protein That Is Processed to a 31-Kilodalton Growth-Phase-Regulated Peripheral Membrane Protein

James Matsunaga,1,2* Tracy A. Young,1 Jeanne K. Barnett,3 Dean Barnett,3 Carole A. Bolin,4 and David A. Haake1,2

Veterans Affairs Greater Los Angeles Healthcare System, Los Angeles, California 90073,1 Department of Medicine, UCLA School of Medicine, Los Angeles, California 90095,2 Department of Biology, University of Southern Indiana, Evansville, Indiana 47712,3 College of Veterinary Medicine, Michigan State University, East Lansing, Michigan 488244

Received 28 June 2001/ Returned for modification 16 August 2001/ Accepted 26 September 2001

Leptospiral protein antigens are of interest as potential virulence factors and as candidate serodiagnostic and immunoprotective reagents. We identified leptospiral protein antigens by screening a genomic expression library with serum from a rabbit hyperimmunized with formalin-killed, virulent Leptospira kirschneri serovar grippotyphosa. Genes expressing known outer membrane lipoproteins LipL32 and LipL41, the heat shock protein GroEL, and the {alpha}, ß, and ß' subunits of RNA polymerase were isolated from the library. In addition, a new leptospiral gene that in Escherichia coli expressed a 45-kDa antigen with an amino-terminal signal peptide followed by the spirochetal lipobox Val-4-Phe-3-Asn-2-Ala-1{downarrow}Cys+1 was isolated. We designated this putative lipoprotein LipL45. Immunoblot analysis of a panel of Leptospira strains probed with LipL45 antiserum demonstrated that many low-passage strains expressed LipL45. In contrast, LipL45 was not detected in high-passage, culture-attenuated strains, suggesting that LipL45 is a virulence-associated protein. In addition, all leptospiral strains tested, irrespective of culture passage, expressed a 31-kDa antigen that was recognized by LipL45 antiserum. Southern blot and peptide mapping studies indicated that this 31-kDa antigen was derived from the carboxy terminus of LipL45; therefore, it was designated P31LipL45. Membrane fractionation studies demonstrated that P31LipL45 is a peripheral membrane protein. Finally, we found that P31LipL45 levels increased as Leptospira entered the stationary phase, indicating that P31LipL45 levels were regulated. Hamsters infected with L. kirschneri formed an antibody response to LipL45, indicating that LipL45 was expressed during infection. Furthermore, the immunohistochemistry of kidneys from infected hamsters indicated that LipL45 was expressed by L. kirschneri that colonized the renal tubule. These observations suggest that expression of LipL45 responds to environmental cues, including those encountered during infection of a mammalian host.

* Corresponding author. Mailing address: VA Greater Los Angeles Healthcare System, Building 113, Room 306, Los Angeles, CA 90073. Phone: (310) 478-3711, ext. 42144. Fax: (310) 268-4142. E-mail: jamesm{at}ucla.edu.

Editor: D. L. Burns

Infection and Immunity, January 2002, p. 323-334, Vol. 70, No. 1
0019-9567/01/$04.00+0     DOI: 10.1128/IAI.70.1.323-334.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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