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Leptospirosis is one of the most widespread zoonotic diseases in the world. It is caused by the pathogen  Leptospira  that results in multiple-organ failure, in particular of the kidney. Outer membrane lipoprotein is the suspected virulence factor of  Leptospira . In  Leptospira  spp LipL41 is one major lipoprotein and is highly conserved. Previous study suggests that LipL41 bears hemin-binding ability and might play a possible role in iron regulation and storage. However, the characterization of hemin-binding ability of LipL41 is still unclear. Here the hemin-binding ability of LipL41 was examined, yielding a  K    d   = 0.59 ± 0.14 μM. Two possible heme regulatory motifs (HRMs), C[P/S], were found in LipL41 at  140 Cys-Ser and  220 Cys-Pro. The mutation study indicates that Cys140 and Cys220 might be cooperatively involved in hemin binding. A supramolecular assembly of LipL41 was determined by transmission electron microscopy. The LipL41 oligomer consists of 36 molecules and folds as a double-layered particle. At the C-terminus of LipL41, there are two tetratricopeptide repeats (TPRs), which might be involved in the protein-protein interaction of the supramolecular assembly.

LipL41, a Hemin Binding Protein from Leptospira santarosai serovar Shermani