Comparative zymographic analysis of metallopeptidase of Leishmania (Viannia) peruviana and Leishmania (Viannia) braziliensis isolates from Peru

Autor: Jorge Arevalo, Patrícia Reyes-Uribe, Jose Batista de Jesus, Taissa Pereira-dos-Santos, Elisa Cupolillo, Camila Mesquita-Rodrigues, Patricia Cuervo
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Leishmania (Viannia) peruviana
Metallopeptidase
purl.org/pe-repo/ocde/ford#3.03.07 [https]
Leishmaniasis
Cutaneous
Biology
Metallopeptidases
Leishmania Peruviana
Polyacrylamide Gel Electrophoresis
Gene Expression Regulation
Enzymologic
Microbiology
Enzyme Activity
Cutaneous leishmaniasis
Genetic similarity
Species Specificity
Protein Degradation
Peru
Gene Expression Regulation Enzymologic
medicine
Leishmania (Viannia) braziliensis
Animals
Humans
chemistry.chemical_classification
Leishmania
Leishmania (Viannia) Braziliensis
Zymography
Ph
Mucocutaneous leishmaniasis
Hydrogen-Ion Concentration
medicine.disease
biology.organism_classification
Peru|Polymerase Chain Reaction
Molecular Weight
Infectious Diseases
Enzyme
chemistry
Metalloproteases
Parasitology
Leishmaniasis Cutaneous
Peptidases
Restriction Fragment Length Polymorphism
Leishmania (Viannia) Peruviana
Popis: American tegumentary leishmaniasis (ATL) in Peru is mainly associated with Leishmania (Viannia) peruviana and L. (V.) braziliensis. These parasites are genetically related, and their characterization as distinct species is controversial. Despite their genetic similarity, each species is associated with different clinical manifestations of ATL; L. (V.) peruviana causes only cutaneous leishmaniasis, whereas L. (V.) braziliensis can cause both cutaneous and mucocutaneous leishmaniasis. Because the primary cutaneous lesions caused by infection with these species are indistinguishable, it is necessary to develop a suitable method to differentiate them in order to prevent possible metastasis to oropharyngeal mucosa. In the present study, we investigated the proteolytic profile of L. (V.) peruviana and L. (V.) braziliensis isolates from Peru by zymographic analysis in SDS-PAGE copolymerized with gelatin. Enzymes were characterized according to their pH range of activity and sensitivity to distinct peptidase inhibitors. We observed that L. (V.) peruviana isolates displayed three proteolytic bands with molecular masses ranging from 55 to 80. kDa, whereas L. (V.) braziliensis isolates showed six proteolytic activities between 55 and 130. kDa. Using specific inhibitors, we determined that these proteolytic activities are due to metallopeptidases and present optimal activity between the pH range 5.5 and 10.0. Our results suggest that the expression of metallopeptidases in L. (V.) peruviana and L. (V.) braziliensis isolates from Peru is species-specific.
Databáze: OpenAIRE
Externí odkaz: