M. Soto et al., SPECIFIC SERODIAGNOSIS OF HUMAN LEISHMANIASIS WITH RECOMBINANT LEISHMANIA P2 ACIDIC RIBOSOMAL-PROTEINS, Clinical and diagnostic laboratory immunology, 3(4), 1996, pp. 387-391
The Leishmania P2 proteins have been analyzed as potential tools for t
he immunodiagnosis of human mucocutaneous and visceral leishmaniasis.
Two recombinant Leishmania infantum proteins, rLiP2a and rLiP2b, were
used. The analysis indicated that the rLiP2a and rLiP2b proteins are r
ecognized by 76% (16 of 21) and 42% (9 of 21), respectively, of sera f
rom patients with mucocutaneous leishmaniasis and by 50% (5 of 10) and
40% (4 of 10), respectively, of sera from patients with visceral leis
hmaniasis. The Leishmania P2 proteins were engineered to have deletion
s of particular amino acids from the carboxyl-terminal region in order
to avoid cross-reactivity with sera from patients with systemic lupus
erythematosus and Chagas' disease, since it is known that this region
is the main target of the autoantibodies present in sera from these p
atients. The results show that while the modified recombinant proteins
rLiP2a-Q and rLiP2b-Q, in which the five carboxyl-terminal amino acid
s had been deleted, maintain the leishmaniasis-specific epitopes, they
do not react with sera from patients with autoimmune disease and Chag
as' disease. For this reason, and also because the sera from patients
with tuberculosis and leprosy, diseases that have to be considered in
a differential clinical diagnosis of infectious diseases, do not react
with the rLiP2a-Q or rLiP2b-Q protein, we think that the engineered p
roteins may be considered specific tools for the immunodiagnosis of mu
cocutaneous and visceral leishmaniasis.