Characterization of a clone from an adult worm cDNA library selected with anti-Schistosoma mansoni human antibodies dissociated from immune complexes: a preliminary report


Autoria(s): Valli,Luiz Carlos Pedrosa; Kanamura,Herminia Yohko; Cotrim,Paulo Cesar; Oliveira,Guilherme Correa; Oliveira,Edward José de
Data(s)

01/06/2007

Resumo

Considering the scarcity of defined antigens, actually useful and reliable for use in the field studies, we propose an alternative method for selection of cDNA clones with potential use in the diagnosis of schistosomiasis. Human antibodies specific to a protein fraction of 31/32 kDa (Sm31/32), dissociated from immune complexes, are used for screening of clones from an adult worm cDNA library. Partial sequencing of five clones, selected through this strategy, showed to be related to Schistosoma mansoni: two were identified as homologous to heat shock protein 70, one to glutathione S-transferase, one to homeodomain protein, and one to a previously described EST (expressed sequence tag) of S. mansoni. This last clone was the most consistently reactive during the screening process with the anti-Sm31/32 antibodies dissociated from the immune complexes. The complete sequence of this clone was obtained and the translation data yielded only one ORF (open reading frame) that code for a protein with 57 amino acids. Based on this amino acid sequence two peptides were chemically synthesized and evaluated separately against a pool of serum samples from schistosomiasis patients and non-schistosomiasis individuals. Both peptides showed strong reactivity only against the positive pool, suggesting that these peptides may be useful as antigens for the diagnosis of schistosomiasis mansoni.

Formato

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Identificador

http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0036-46652007000300009

Idioma(s)

en

Publicador

Instituto de Medicina Tropical

Fonte

Revista do Instituto de Medicina Tropical de São Paulo v.49 n.3 2007

Palavras-Chave #Schistosoma mansoni #cDNA library #Immunoscreening #DNA sequencing #Synthetic peptides
Tipo

journal article