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Sir2-Related Protein 1 from Leishmania amazonensis is a glycosylated NAD+-dependent deacetylase

Published online by Cambridge University Press:  08 August 2011

M. R. FESSEL ,
C. B. LIRA ,
S. GIORGIO ,
C. H. I. RAMOS  and
M. I. N. CANO
M. R. FESSEL
Affiliation:
Chemistry Institute, University of Campinas UNICAMP, Campinas SP 13083-970, Brazil
C. B. LIRA
Affiliation:
Departamento de Genética, Instituto de Biociências, Universidade Estadual Paulista Júlio de Mesquita Filho - UNESP, Botucatu, SP 18618-000, Brazil
S. GIORGIO
Affiliation:
Instituto de Biologia, Unicamp, Campinas, São Paulo, Brazil
C. H. I. RAMOS*
Affiliation:
Chemistry Institute, University of Campinas UNICAMP, Campinas SP 13083-970, Brazil
M. I. N. CANO*
Affiliation:
Departamento de Genética, Instituto de Biociências, Universidade Estadual Paulista Júlio de Mesquita Filho - UNESP, Botucatu, SP 18618-000, Brazil
*
*Corresponding author: Departamento de Genética, Instituto de Biociências, Universidade Estadual Paulista Júlio de Mesquita Filho - UNESP, Botucatu, SP 18618-000, Brazil. Fax: +55 14 3811 6229. E-mail: cramos@iqm.unicamp.br
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Summary

Sirtuin proteins form a family of NAD+-dependent protein deacetylases that are considered potential drug targets against parasites. Here, we present the first characterization of a sirtuin orthologue from Leishmania amazonensis, an aetiological agent of American tegumentary leishmaniasis that has been the subject of many studies focused in the development of therapeutic approaches. The protein has high sequence identity with other Kinetoplastid Silent information regulator 2 Related Protein 1 (Sir2RP1) and was named LaSir2RP1. The gene exists as a single copy, encoding a monomeric protein (LaSir2RP1) of approximately 41 kDa that has NAD+-dependent deacetylase activity. LaSir2RP1 was immunodetected in total protein extracts, in cytoplasmic granules, and in the secreted material of both promastigotes and lesion-derived amastigotes. Analysis of both lectin‑affinity purified promastigote and amastigote extracts revealed the presence of a major enriched protein of approximately 66 kDa that was recognized by an anti-LaSir2RP1 serum, suggesting that a parasite sirtuin could be glycosylated in vivo.

Keywords

Leishmania amazonensissirtuinLaSir2RP1secreted/excretedglycoproteindeacetylase
Type
Research Article
Information
Parasitology , Volume 138 , Issue 10 , September 2011 , pp. 1245 - 1258
Copyright
Copyright © Cambridge University Press 2011

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