Molecular modeling and in-silico engineering of Cardamom mosaic virus coat protein for the presentation of immunogenic epitopes of Leptospira LipL32.

Expression of Cardamom mosaic virus (CdMV) coat protein (CP) in E. coli forms virus-like particles. In this study, the structure of CdMV CP was predicted and used as a platform to display epitopes of the most abundant surface-associated protein, LipL32 of Leptospira at C, N, and both the termini of CdMV CP.

Presence of 46 kDa gelatinase on the outer membrane of Leptospira.

Leptospira infection involves the adhesion of the bacteria followed by invasion of the host crossing the extracellular matrix barrier. In an effort to understand the molecular mechanism of this process, the possibility of occurrence of matrix degrading enzymes from Leptospira was investigated. Zymographic analysis showed that the outer membrane of Leptospires contains a gelatinase of average molecular size of 46 kDa.

A zymography analysis of proteinase activity present in Leptospira.

Leptospirosis is a major public health problem caused by spirochete Leptospira which is an extracellular pathogen. During infection and invasion, the bacteria cross the physical barriers and later it encounter with the host defence mechanism. These processes may involve proteolytic degradation of the host tissue biomatrix.

A diagnostically useful 200-kDa protein is secreted through the surface pores of the filarial parasite Setaria digitata.

The excretory/secretory (ES) materials from filarial parasites form an important tool for immunodiagnosis of filariasis. We have raised monoclonal antibodies against ES proteins isolated from the medium incubated with live adult bovine filarial parasite Setaria digitata. The hybridoma were cloned and characterised with respect to the individual proteins of the ES materials.