GP63 Function in the Interaction of Trypanosomatids with the Invertebrate Host: Facts and Prospects
The GP63 of the protozoan parasite Leishmania is a highly abundant zinc metallopeptidase, mainly glycosylphosphatidylinositol-anchored to the parasite surface, which contributes to a myriad of well-established functions for Leishmania in the interaction w
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GP63 Function in the Interaction of Trypanosomatids with the Invertebrate Host: Facts and Prospects Claudia M. d’Avila-Levy, Ellen C.F. Altoé, Lívia A. Uehara, Marta H. Branquinha, and André L.S. Santos
Abstract The GP63 of the protozoan parasite Leishmania is a highly abundant zinc metallopeptidase, mainly glycosylphosphatidylinositol-anchored to the parasite surface, which contributes to a myriad of well-established functions for Leishmania in the interaction with the mammalian host. However, the role of GP63 in the Leishmania-insect vector interplay is still a matter of controversy. Data from GP63 homologues in insect and plant trypanosomatids strongly suggest a participation of GP63 in this interface, either through nutrient acquisition or through binding to the insect gut receptors. GP63 has also been described in the developmental forms of Trypanosoma cruzi, Trypanosoma brucei and Trypanosoma rangeli that deal with the vector. Here, the available data from GP63 will be analyzed from the perspective of the interaction of trypanosomatids with the invertebrate host.
Abbreviations EC EDTA EGTA GIPLs GPI
Enzyme class Ethylenediaminetetraacetic acid Ethylene glycol tetraacetic acid Glycoinositolphospholipids Glycosylphosphatidylinositol
C.M. d’Avila-Levy (*) • E.C.F. Altoé • L.A. Uehara Laboratório de Biologia Molecular e Doenças Endêmicas, Instituto Oswaldo Cruz (IOC), Fundação Oswaldo Cruz (FIOCRUZ), Rio de Janeiro, Brazil e-mail: [email protected] M.H. Branquinha • A.L.S. Santos Laboratório de Investigação de Peptidases, Departamento de Microbiologia Geral, Instituto de Microbiologia Paulo de Góes (IMPG), Universidade Federal do Rio de Janeiro (UFRJ), Ilha do Fundão, Rio de Janeiro, Brazil A.L.S. Santos et al. (eds.), Proteins and Proteomics of Leishmania and Trypanosoma, Subcellular Biochemistry 74, DOI 10.1007/978-94-007-7305-9_11, © Springer Science+Business Media Dordrecht 2014
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GPI-PLC HIV LPG MSP PARP PSP VSG
1
Glycosylphosphatidylinositol-phospholipase C Human immunodeficiency virus Lipophosphoglycan Major surface peptidase Procyclic acidic repetitive protein Promastigote surface peptidase Glycosylphosphatidylinositol-anchored variant surface protein
GP63 in Leishmania, Phytomonads and Monoxenic Trypanosomatids
In the mid-1980s, it was identified and characterized a protein in promastigotes of different species of the genera Leishmania (Fong and Chang 1982; Lepay et al. 1983; Bouvier et al. 1985; Etges et al. 1986) that presented immunological crossreactivity with sera from hosts infected with Leishmania spp. This protein presents a molecular mass around 63 kDa, is a zinc metallopeptidase, accounts for about 1 % of the total proteins in promastigotes and is mainly glycosylphosphatidylinositol(GPI)-anchored to the plasma membrane, while hydrophilic and secreted isoforms are also described. This protein was termed leishmanolysin, glycoprotein of 63 kDa (GP63), surface acid peptidase, promastigote surface peptidase (PSP) and lately as major surface peptidase (
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