ArticleClinical and diagnostic laboratory immunology1996
Specific serodiagnosis of human leishmaniasis with recombinant Leishmania P2 acidic ribosomal proteins.
Article in Clinical and diagnostic laboratory immunology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.
- Potential antigenic targets used in immunological tests for diagnosis of tegumentary leishmaniasis: A systematic review.PloS one · 2021Pooled it
- Candidate antigens for serological testing (ELISA) and diagnosis of canine visceral leishmaniasis.Revista brasileira de parasitologia veterinaria = Brazilian journal of veterinary parasitology : Orgao Oficial do Colegio Brasileiro de Parasitologia Veterinaria · 2025Article
- Use of Recombinant Antigens for Sensitive Serodiagnosis of American Tegumentary Leishmaniasis Caused by Different Leishmania Species.Journal of clinical microbiology · 2017Article
- Identification of differentially expressed proteins from Leishmania amazonensis associated with the loss of virulence of the parasites.PLoS neglected tropical diseases · 2014Article
- Identifying vaccine targets for anti-leishmanial vaccine development.Expert review of vaccines · 2014Review
- Towards a more precise serological diagnosis of human tegumentary leishmaniasis using Leishmania recombinant proteins.PloS one · 2013Article
- Diagnosis of visceral leishmaniasis: developments over the last decade.Parasitology research · 2012Review
- Cloning and characterization of the acidic ribosomal protein P2 of Cryptosporidium parvum, a new 17-kilodalton antigen.Clinical and vaccine immunology : CVI · 2010Article
- The Leishmania infantum PUF proteins are targets of the humoral response during visceral leishmaniasis.BMC research notes · 2010Article
- Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis.Clinical and vaccine immunology : CVI · 2009Article
- The immunodominant T helper 2 (Th2) response elicited in BALB/c mice by the Leishmania LiP2a and LiP2b acidic ribosomal proteins cannot be reverted by strong Th1 inducers.Clinical and experimental immunology · 2007Article
- Design, construction, and evaluation of a specific chimeric antigen to diagnose chagasic infection.Journal of clinical microbiology · 2006Article
- The Leishmania infantum acidic ribosomal protein LiP2a induces a prominent humoral response in vivo and stimulates cell proliferation in vitro and interferon-gamma (IFN-gamma) production by murine splenocytes.Clinical and experimental immunology · 2000Article
- Multicomponent chimeric antigen for serodiagnosis of canine visceral leishmaniasis.Journal of clinical microbiology · 1998Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Leishmania P2 proteins have been analyzed as potential tools for the 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 recognized by 76% (16 of 21) and 42% (9 of 21), respectively, of sera from patients with mucocutaneous leishmaniasis and by 50% (5 of 10) and 40% (4 of 10), respectively, of sera from patients with visceral leishmaniasis. The Leishmania P2 proteins were engineered to have deletions 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 patients. The results show that while the modified recombinant proteins rLiP2a-Q and rLiP2b-Q, in which the five carboxyl-terminal amino acids had been deleted, maintain the leishmaniasis-specific epitopes, they do not react with sera from patients with autoimmune disease and Chagas' 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 proteins may be considered specific tools for the immunodiagnosis of mucocutaneous and visceral leishmaniasis.
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