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Localization and induction of the A2 virulence factor in Leishmania : evidence that A2 is a stress response protein
Author(s) -
McCall LauraIsobel,
Matlashewski Greg
Publication year - 2010
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2010.07229.x
Subject(s) - phagolysosome , biology , leishmania , leishmania major , amastigote , heat shock protein , leishmania donovani , kinetoplastida , endoplasmic reticulum , visceral leishmaniasis , vector (molecular biology) , leishmaniasis , microbiology and biotechnology , immunology , gene , parasite hosting , recombinant dna , phagosome , phagocytosis , biochemistry , protozoal disease , world wide web , computer science , malaria
Summary Leishmaniasis is a vector‐borne infectious disease with a wide range of pathologies depending on the species of Leishmania. Leishmania parasites are transmitted by the sand fly vector as promastigotes; within the mammalian host, Leishmania parasites differentiate into amastigotes and replicate in macrophages. The A2 protein from Leishmania donovani is expressed predominantly in amastigotes and therefore likely plays a role in survival in the mammalian host. In the present study, we have determined that the A2 protein colocalized with the Leishmania endoplasmic reticulum binding protein, BiP, was induced by stress and complexed with BiP following heat shock. The A2 gene in Leishmania major is a non‐expressed pseudogene, and we present evidence that ectopic expression of a transfected A2 gene in L. major enhanced its viability following heat shock. A2 may therefore play a role in protecting L. donovani from stress associated with infection in visceral organs, including the fever typically associated with visceral leishmaniasis. Interestingly, when comparing A2 protein localization, we also observed that the Leishmania secreted acid phosphatase SAcP protein was transported out of the parasite‐containing phagolysosome and was located throughout the macrophage cytoplasm in vesicles, providing the first example of a secreted Leishmania‐ derived protein exiting the parasite‐containing phagolysosome.