Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response
Biochim. Biophys. Acta, Gen. Subj.
; 1861(1): 3490-3497, 2017.
Artigo
em Inglês
| Sec. Est. Saúde SP, SESSP-IBPROD, Sec. Est. Saúde SP
| ID: but-ib13620
Biblioteca responsável:
BR78.1
Localização: BR78.1
ABSTRACT
Background:
The Micro-Exon Gene-14 (MEG-14) displays a remarkable structure that allows the generation of antigenic variation in Schistosomes. Previous studies showed that the soluble portion of the MEG-14 protein displays features of an intrinsically disordered protein and is expressed exclusively in the parasite esophageal gland. These features indicated a potential for interaction with host proteins present in the plasma and cells from ingested blood.Methods:
A yeast two-hybrid experiment using as bait the soluble domain of Schistosoma mansoni MEG-14 (sMEG-14) against a human leukocyte cDNA library was performed. Pull-down and surface plasmon resonance (SPR) experiments were used to validate the interaction between sMEG-14 and human S100A9. Synchrotron radiation circular dichroism (SRCD) were used to detect structural changes upon interaction between sMEG-14 and human S100A9. Feeding of live parasites with S100A9 attached to a fluorophore allowed the tracking of the fate of this protein in the parasite digestive system.Results:
S100A9 interacted with sMEG-14 consistently in yeast two-hybrid assay, pull-down and SPR experiments. SRCD suggested that MEG-14 acquired a more regular structure as a result of the interaction with S100A9. Accumulation of recombinant S100A9 in the parasite's esophageal gland, when ingested by live worms suggests that such interaction may occur in vivo.Conclusion:
S100A9, a protein previously described to be involved in modulation of inflammatory response, was found to interact with sMEG-14. Generalsignificance:
Our results allow proposing a mechanism involving MEG-14 for the parasite to block inflammatory signaling, which would occur upon release of S100A9 when ingested blood cells are lysed.
Texto completo:
Disponível
Coleções:
Bases de dados nacionais
/
Brasil
Base de dados:
Sec. Est. Saúde SP
/
SESSP-IBPROD
Idioma:
Inglês
Revista:
Biochim. Biophys. Acta, Gen. Subj.
Ano de publicação:
2017
Tipo de documento:
Artigo