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Study of the vaccine potential of the LigB protein from Leptospira spp.


Leptospirosis is a zoonosis with wide distribution worldwide, caused by pathogenic spirochetes of the genus Leptospira. In the world, it is estimated that its incidence is approximately one million cases with 58,900 deaths per year. In livestock, it causes great economic losses due to reproductive changes in infected animals.Available commercial vaccines are composed of leptospiral cultures from different inactivated serovars (bacterins). Currently, they are used in livestock and licensed for human use only in few countries. They present low efficiency and, they promote protection only against the serovars present in the preparation and fail to induce long-term immunity, which requires annual or semi-annual administration.As an alternative, the development of a vaccine that can protect against different pathogenic serovars has been proposed. The leptospiral immunoglobulin (Ig) -like B protein (LigB) is considered the most promising vaccine antigen to date. This protein has similar Ig-like domains to those found in other bacterial proteins, such as the invasin from Yersinia pseudotuberculosis and intimin from Escherichia coli. Results obtained by different groups, regarding the ability of LigB protein to induce protection against leptospirosis in model of lethal challenge homologous in hamsters, are contradictory. Our hypothesis is that these different obtained results may be due to structural problems of the recombinant proteins used. Furthermore, it is not known whether the LigB protein is capable of inducing heterologous protection against different serovars of leptospires.In this sense, the objectives of this project are: 1- to confirm the ability of LigB protein to induce immunoprotective response in a model of lethal homologous challenge in hamsters, using samples of purified recombinant proteins with the presence of ordered secondary structure proven through analysis by dichroism Circular; 2- To assess the ability of the LigB protein to induce cross-protection. (AU)

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(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
IGLEZIAS, SILVIA D'ANDRETTA; ESTIMA ABREU, PATRICIA ANTONIA; KANAMURA, CRISTINA; MAGALDI, ANTONIO JOSE; SEGURO, ANTONIO CARLOS; DE BRITO, THALES. Immunohistochemical detection of Lp25 and LipL32 proteins in skeletal and cardiac muscles of fatal human leptospirosis. Revista do Instituto de Medicina Tropical de São Paulo, v. 62, . (19/00546-0)
HO, JOANA DIAS; TAKARA, LUIZ EDUARDO MASSAO; MONARIS, DENIZE; GONCALVES, ALINE PATRICIA; SOUZA-FILHO, ANTONIO FRANCISCO; DE SOUZA, GISELE OLIVEIRA; HEINEMANN, MARCOS BRYAN; HO, PAULO LEE; ABREU, PATRICIA ANTONIA ESTIMA. GroEL protein of the Leptospira spp. interacts with host proteins and induces cytokines secretion on macrophages. BMC Microbiology, v. 21, n. 1, . (10/51215-9, 19/09804-1, 19/00546-0)

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