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Infection and Immunity, March 2009, p. 952-958, Vol. 77, No. 3
0019-9567/09/$08.00+0     doi:10.1128/IAI.01370-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Major Surface Protein LipL32 Is Not Required for Either Acute or Chronic Infection with Leptospira interrogans{triangledown} ,{dagger}

Gerald L. Murray,1 Amporn Srikram,2 David E. Hoke,1 Elsio A. Wunder Jr.,3 Rebekah Henry,1 Miranda Lo,1 Kunkun Zhang,4 Rasana W. Sermswan,5 Albert I. Ko,3,6 and Ben Adler1,4*

Australian Bacterial Pathogenesis Program,1 Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Department of Microbiology, Monash University, Clayton, Victoria 3800, Australia,4 Melioidosis Research Center,2 Department of Biochemistry, Faculty of Medicine, Khon Kaen University, Khon Kaen 40002, Thailand,5 Gonçalo Moniz Research Center, Oswaldo Cruz Foundation, Brazilian Ministry of Health, Salvador, Bahia 40296, Brazil,3 Division of International Medicine and Infectious Disease, Weill Medical College of Cornell University, New York, New York 100216

Received 8 November 2008/ Returned for modification 8 December 2008/ Accepted 12 December 2008

Leptospira interrogans is responsible for leptospirosis, a zoonosis of worldwide distribution. LipL32 is the major outer membrane protein of pathogenic leptospires, accounting for up to 75% of total outer membrane protein. In recent times LipL32 has become the focus of intense study because of its surface location, dominance in the host immune response, and conservation among pathogenic species. In this study, an lipL32 mutant was constructed in L. interrogans using transposon mutagenesis. The lipL32 mutant had normal morphology and growth rate compared to the wild type and was equally adherent to extracellular matrix. Protein composition of the cell membranes was found to be largely unaffected by the loss of LipL32, with no obvious compensatory increase in other proteins. Microarray studies found no obvious stress response or upregulation of genes that may compensate for the loss of LipL32 but did suggest an association between LipL32 and the synthesis of heme and vitamin B12. When hamsters were inoculated by systemic and mucosal routes, the mutant caused acute severe disease manifestations that were indistinguishable from wild-type L. interrogans infection. In the rat model of chronic infection, the LipL32 mutant colonized the renal tubules as efficiently as the wild-type strain. In conclusion, this study showed that LipL32 does not play a role in either the acute or chronic models of infection. Considering the abundance and conservation of LipL32 among all pathogenic Leptospira spp. and its absence in saprophytic Leptospira, this finding is remarkable. The role of this protein in leptospiral biology and pathogenesis thus remains elusive.

* Corresponding author. Mailing address: Department of Microbiology, Monash University, Clayton, Victoria 3800, Australia. Phone: 61 3 9905 4815. Fax: 61 3 9905 4811. E-mail: ben.adler{at}med.monash.edu.au

{triangledown} Published ahead of print on 22 December 2008.

{dagger} Supplemental material for this article may be found at http://iai.asm.org/.

Editor: R. P. Morrison

Infection and Immunity, March 2009, p. 952-958, Vol. 77, No. 3
0019-9567/09/$08.00+0     doi:10.1128/IAI.01370-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



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