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Improving serodiagnosis of human and canine leishmaniasis with recombinant Leishmania braziliensis cathepsin l-like protein and a synthetic peptide containing its linear B-cell epitope.

BACKGROUND
Early diagnosis and correct human leishmaniasis is important for the treatment of disease. Another important step in the control of visceral leishmaniasis is the identification of infected dogs, which is the main domestic reservoir of L. infantum. recombinant proteins and synthetic peptides based Leishmania genes have emerged as valuable targets for serodiagnosis because of their increased sensitivity, specificity and potential for standardization. Cathepsin L-like surface antigen gene that is secreted by amastigotes and has little in common with host proteins, factors that allow this protein as a good target for the serodiagnosis of leishmaniasis. Feline Recombinant Proteins



RESULTS
We mapped linear B cell epitopes in the Cathepsin L-like protein from L. braziliensis. A synthetic peptide containing epitopes and recombinant proteins were evaluated for serodiagnosis of human tegumentary and visceral leishmaniasis and visceral leishmaniasis dogs.


CONCLUSION
Best done recombinant proteins for human and canine visceral leishmaniasis tegumentary, with 96.30% and 89.33% accuracy, respectively. Synthetic peptide is the best for discrimination of human visceral leishmaniasis, with 97.14% specificity, sensitivity of 94.55% and 96.00% accuracy. Comparison with T. cruzi-infected humans and dogs show that the identified epitopes specific to Leishmania parasites, which minimizes the possibility of cross reactions.
Improving serodiagnosis of human and canine leishmaniasis with recombinant Leishmania braziliensis cathepsin l-like protein and a synthetic peptide containing its linear B-cell epitope.


Recombinant canine IgE IgE Fc and Fc-fusion protein binds TRAIL canine neoplastic mast cells.


Screening for expression of high affinity receptors for IgE by reverse transcriptase PCR, revealed that almost all dog mast cell tumors expressed FcɛRIα mRNA, supporting the idea to develop an anti-neoplastic treatment based molecules that can target this receptor. The use of cytotoxic cytokines to trigger apoptosis signal is one strategy to promote cell death in malignant mast cell. The sequence coding for canine IgE and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) identified through genome analysis. 

The selected area of ​​the coding sequences Guinea Pig Recombinant Proteins for these genes were cloned and compared with predicted genome sequence. Fc region of IgE dog, dog death domain and IgE Fc TRAIL: TRAIL fusion construct generated and epitope-tagged proteins expressed, using a eukaryotic expression system. Specific binding of recombinant canine IgE Fc-containing proteins for human recombinant FcɛRIα and canine mast cell tumor lines expressing FcɛRIα (C2), but no one failed to express FcɛRIα (MCLA), shown

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