English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

The cytosolic tryparedoxin peroxidase (cTXNPx) of  Leishmania donovani  is a defensive enzyme. Apart from the nonsecretory form, the cTXNPx is released in the spent media of  Leishmania  cultures and also in the host cell cytosol. The secretory form of the enzyme from the parasite interacts with multiple proteins in the host cell cytosol, the apoptosis-inducing factor (AIF) being one of them. Immunoprecipitation with anti-cTXNPx and anti-AIF antibodies suggests a strong interaction between AIF and cTXNPx. Consequent to parasite invasion, the migration of AIF to the nucleus to precipitate apoptosis is inhibited in the presence of recombinant cTXNPx expressed in the host cell. This inhibition of AIF movement results in lesser host cell death, giving an advantage to the parasite for continued survival. Staurosporine-induced AIF migration to the nucleus was also inhibited in the presence of recombinant cTXNPx in the host cell. Therefore, this study demonstrates the ability of a  Leishmania  parasite enzyme, cTXNPx, to interfere with the migration of the host AIF protein, providing a survival advantage to the  Leishmania  parasite.

A Novel Role of Secretory Cytosolic Tryparedoxin Peroxidase in Delaying Apoptosis of Leishmania -Infected Macrophages