Heterologous expression, purification and immunological reactivity of a recombinant HSP60 from Paracoccidioides brasiliensis
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2002-03
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The complete coding cDNA of HSP60 from Paracoccidioides brasiliensis was overexpressed in an Escherichia
coli host to produce high levels of recombinant protein. The protein was purified by affinity chromatography.
A total of 169 human serum samples were tested for reactivity by Western blot analysis with the purified HSP60
recombinant protein. Immunoblots indicated that the recombinant P. brasiliensis HSP60 was recognized by
antibodies in 72 of 75 sera from paracoccidioidomycosis patients. No cross-reactivity was detected with
individual sera from patients with aspergillosis, sporotrichosis, cryptococcosis, and tuberculosis. Reactivity to
HSP60 was observed in sera from 9.52% of control healthy individuals and 11.5% of patients with histoplas-
mosis. The high sensitivity and specificity (97.3 and 92.5%, respectively) for HSP60 suggested that the
recombinant protein can be used singly or in association with other recombinant antigens to detect antibody
responses in P. brasiliensis-infected patients.
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CUNHA, Daniela A.; ZANCOPÉ-OLIVEIRA, Roseli M.; FELIPE, M. Sueli S.; SALEM-IZACC, Silvia M.; DEEPE JR, George S ; SOARES, Célia M. A. Heterologous expression, purification and immunological reactivity of a recombinant HSP60 from Paracoccidioides brasiliensis. Clinical and Diagnostic Laboratory Immunology, Washington, v. 9, n. 2, p. 374-377, Mar. 2002.