LipL41, a Hemin Binding Protein from Leptospira santarosai (LB265)

Abstract

Leptospirosis, a widespread zoonotic disease, is caused by pathogen Leptospira. Outer membrane lipoprotein is the potential virulence factor of Leptospira. LipL41 is one of the major lipoprotein and highly conserved in Leptospira spp. Previous study suggests that LipL41 shows hemin binding ability and might have a potential role in iron regulation and storage. The hemin binding ability of LipL41 is determined with a Kd = 0.59 ± 0.14 μM. Two possible heme regulatory motifs (HRMs), C[P/S], are found in LipL41 as 140Cys‐Ser and 220Cys‐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. At the C‐terminus of LipL41, there are two tetratricopeptide repeats (TPRs), which might involve in the protein‐protein interaction of the supramolecular assembly.