Crystal structure of LipL32, the most abundant surface protein of pathogenic Leptospira spp.

Julian Vivian, Travis Clarke Beddoe, Adrian Dale McAlister, Matthew Charles James Wilce, Leyla Zaker-Tabrizi, Sally Tanya Troy, Emma Byres, David Edmund Hoke, Paul Antony Cullen, Miranda Lo, Gerald Laurence Murray, Ben Adler, Jamie Rossjohn

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Spirochetes of the genus Leptospira cause leptospirosis in humans and animals worldwide. Proteins exposed on the bacterial cell surface are implicated in the pathogenesis of leptospirosis. However, the biological role of the majority of these proteins is unknown; this is principally due to the lack of genetic systems for investigating Leptospira and the absence of any structural information on leptospiral antigens. To address this, we have determined the 2.0 A resolution structure of the lipoprotein LipL32, the most abundant outer membrane and surface protein present exclusively in pathogenic Leptospira species. The extracellular domain of LipL32 revealed a compact, globular, jelly-roll fold from which projected an unusual extended beta-hairpin that served as a principal mediator of the observed crystallographic dimer. Two acidic-rich patches were also identified as potential binding sites for positively-charged ligands, such as laminin, to which LipL32 has a propensity to bind. Although LipL32 shared no significant sequence identity to any known protein, it possessed structural homology to the adhesins that bind components of the extracellular matrix, suggesting that LipL32 functions in an analogous manner. Moreover, the structure provides a framework for understanding the immunological role of this major surface lipoprotein.
Original languageEnglish
Pages (from-to)1229 - 1238
Number of pages10
JournalJournal of Molecular Biology
Issue number5
Publication statusPublished - 2009

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