GP63 Function in the Interaction of Trypanosomatids with the Invertebrate Host: Facts and Prospects

  • Claudia M. d’Avila-LevyEmail author
  • Ellen C. F. Altoé
  • Lívia A. Uehara
  • Marta H. Branquinha
  • André L. S. Santos
Part of the Subcellular Biochemistry book series (SCBI, volume 74)


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.


GP63 Gene Bloodstream Form Invertebrate Host Procyclic Form Metacyclic Trypomastigotes 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



Enzyme class


Ethylenediaminetetraacetic acid


Ethylene glycol tetraacetic acid






Glycosylphosphatidylinositol-phospholipase C


Human immunodeficiency virus




Major surface peptidase


Procyclic acidic repetitive protein


Promastigote surface peptidase


Glycosylphosphatidylinositol-anchored variant surface protein



 This study was supported by grants from the following Brazilian Agencies: Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES), Conselho Nacional de Desenvolvimento Científico e Tecnológico (MCT/CNPq), Fundação de Amparo à Pesquisa no Estado do Rio de Janeiro (FAPERJ) and Fundação Oswaldo Cruz (FIOCRUZ).


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Copyright information

© Springer Science+Business Media Dordrecht 2014

Authors and Affiliations

  • Claudia M. d’Avila-Levy
    • 1
    Email author
  • Ellen C. F. Altoé
    • 1
  • Lívia A. Uehara
    • 1
  • Marta H. Branquinha
    • 2
  • André L. S. Santos
    • 2
  1. 1.Laboratório de Biologia Molecular e Doenças Endêmicas, Instituto Oswaldo Cruz (IOC)Fundação Oswaldo Cruz (FIOCRUZ)Rio de JaneiroBrazil
  2. 2.Laboratório de Investigação de Peptidases, Departamento de Microbiologia Geral, Instituto de Microbiologia Paulo de Góes (IMPG)Universidade Federal do Rio de Janeiro (UFRJ)Rio de JaneiroBrazil

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