Research Projects

Leptospira is a spirochete with numerous outer membrane, outer surface, and secretory proteins that may play a crucial role in infection. Recent research has shown that few proteins display roles in invasion, either by interacting with the host extracellular matrix (ECM) or sequestering host immune factors for evasion. One surface protein, Leptospira Immunoglobulin like (Lig) family proteins, has been found to have multifaceted functions, such as binding with host ECMs and modulating the host complement system. The group has recently established two novel functions for this protein - nuclease and protease -, suggesting its role in degrading the host Neutrophil Extracellular Traps (NET) to escape NET-mediated killing. Other surface-exposed proteins, such as Leptospiral complement regulator-acquiring protein A (LcpA), may also play a role in evasion. LcpA is exclusively present in pathogenic leptospira spp. and does not show sequence homology with others in non-redundant databases. The 3-D structure of LcpA and its interaction with the complement regulator, C4BP, is unknown, and further investigation is warranted to provide insight into the atomic details of interaction and evasion phenomenon in leptospira.