The extracellular release of Schistosoma mansoni HMGB1 nuclear protein is mediated by acetylation |
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| Authors: | Vitor Coutinho Carneiro,Renata de Moraes Maciel,Isabel Caetano de Abreu da Silva,Claudia Neto Paiva,Marcelo Rosado Fantappié |
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| Affiliation: | a Instituto de Bioquímica Médica, Programa de Biotecnologia e Biologia Molecular, Universidade Federal do Rio de Janeiro, CCS, Ilha do Fundão, Rio de Janeiro 21941-590, Brazil
b Departamento de Imunologia, Instituto de Microbiologia Professor Paulo de Góes, Universidade Federal do Rio de Janeiro, CCS, Ilha do Fundão, Rio de Janeiro 21941-590, Brazil |
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| Abstract: | Schistosoma mansoni HMGB1 (SmHMGB1) was revealed to be a substrate for the parasite histone acetyltransferases SmGCN5 and SmCBP1. We found that full-length SmHMGB1, as well as its HMG-box B (but not HMG-box A) were acetylated in vitro by SmGCN5 and SmCBP1. However, SmCBP1 was able to acetylate both substrates more efficiently than SmGCN5. Interestingly, the removal of the C-terminal acidic tail of SmHMGB1 (SmHMGB1ΔC) resulted in increased acetylation of the protein. We showed by mammalian cell transfection assays that SmHMGB1 and SmHMGB1ΔC were transported from the nucleus to the cytoplasm after sodium butyrate (NaB) treatment. Importantly, after NaB treatment, SmHMGB1 was also present outside the cell. Together, our data suggest that acetylation of SmHMGB1 plays a role in cellular trafficking, culminating with its secretion to the extracellular milieu. The possible role of SmHMGB1 acetylation in the pathogenesis of schistosomiasis is discussed. |
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| Keywords: | Schistosoma mansoni HMGB1 Acetylation Secretion Inflammation |
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