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Infection and Immunity, April 2000, p. 2276-2285, Vol. 68, No. 4
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Leptospiral Major Outer Membrane Protein LipL32 Is a Lipoprotein Expressed during Mammalian Infection

David A. Haake,1,2,* Garlo Chao,1 Richard L. Zuerner,3 Jeanne K. Barnett,4 Dean Barnett,4 Mary Mazel,1 James Matsunaga,1,2 Paul N. Levett,5 and Carole A. Bolin3

Division of Infectious Diseases, Veterans Affairs Greater Los Angeles Healthcare System, Los Angeles, California 900731; Department of Medicine, UCLA School of Medicine, Los Angeles, California 900952; National Animal Disease Center, Agricultural Research Service, U.S. Department of Agriculture, Ames, Iowa 500103; Biology Department, University of Southern Indiana, Evansville, Indiana 477124; and University of the West Indies School of Clinical Medicine and Research, Barbados5

Received 2 September 1999/Returned for modification 3 November 1999/Accepted 4 January 2000

We report the cloning of the gene encoding the 32-kDa lipoprotein, designated LipL32, the most prominent protein in the leptospiral protein profile. We obtained the N-terminal amino acid sequence of a staphylococcal V8 proteolytic-digest fragment to design an oligonucleotide probe. A Lambda-Zap II library containing EcoRI fragments of Leptospira kirschneri DNA was screened, and a 5.0-kb DNA fragment which contained the entire structural lipL32 gene was identified. Several lines of evidence indicate that LipL32 is lipid modified in a manner similar to that of other procaryotic lipoproteins. The deduced amino acid sequence of LipL32 would encode a 272-amino-acid polypeptide with a 19-amino-acid signal peptide, followed by a lipoprotein signal peptidase cleavage site. LipL32 is intrinsically labeled during incubation of L. kirschneri in media containing [3H]palmitate. The linkage of palmitate and the amino-terminal cysteine of LipL32 is acid labile. LipL32 is completely solubilized by Triton X-114 extraction of L. kirschneri; phase separation results in partitioning of LipL32 exclusively into the hydrophobic, detergent phase, indicating that it is a component of the leptospiral outer membrane. CaCl2 (20 mM) must be present during phase separation for recovery of LipL32. LipL32 is expressed not only during cultivation but also during mammalian infection. Immunohistochemistry demonstrated intense LipL32 reactivity with L. kirschneri infecting proximal tubules of hamster kidneys. LipL32 is also a prominent immunogen during human leptospirosis. The sequence and expression of LipL32 is highly conserved among pathogenic Leptospira species. These findings indicate that LipL32 may be important in the pathogenesis, diagnosis, and prevention of leptospirosis.

* Corresponding author. Mailing address: Division of Infectious Diseases, 111F, VA Greater LA Healthcare System, Los Angeles, CA 90073. Phone: (310) 478-3711, x40267. Fax: (310) 268-4928. E-mail: dhaake{at}ucla.edu.

Infection and Immunity, April 2000, p. 2276-2285, Vol. 68, No. 4
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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