@article{fdi:010070943,
  title = {{T}rypanosoma musculi infection in mice critically relies on mannose receptor-mediated arginase induction by a {T}b{KHC}1 kinesin h chain homolog},
  author = {{N}zoumbou-{B}oko, {R}. and {D}e {M}uylder, {G}. and {S}emballa, {S}. and {L}ecordier, {L}. and {D}auchy, {F}. {A}. and {G}obert, {A}. {P}. and {H}olzmuller, {P}. and {L}emesre, {J}ean-{L}oup and {B}ras {G}oncalves, {R}achel and {B}arnab{\'e}, {C}hristian and {C}ourtois, {P}. and {D}aulouede, {S}. and {B}eschin, {A}. and {P}ays, {E}. and {V}incendeau, {P}.},
  editor = {},
  language = {{ENG}},
  abstract = {{A}rginase activity induction in macrophages is an escape mechanism developed by parasites to cope with the host's immune defense and benefit from increased host-derived growth factor production. {W}e report that arginase expression and activity were induced in macrophages during mouse infection by {T}rypanosoma musculi, a natural parasite of this host. {T}his induction was reproduced in vitro by excreted/secreted factors of the parasite. {A} m{A}b directed to {T}b{KHC}1, an orphan kinesin {H} chain from {T}rypanosoma brucei, inhibited {T}. musculi excreted/secreted factor-mediated arginase induction. {A}nti-{T}b{KHC}1 {A}b also inhibited {T}. musculi growth, both in vitro and in vivo. {I}nduction of arginase activity and parasite growth involved {C}-type lectin receptors, because mannose injection decreased arginase activity induction and parasite load in vitro and in vivo. {A}ccordingly, the parasite load was reduced in mice lacking mannose receptor {C}-type 1. {T}he {T}. musculi {KHC}1 homolog showed high similarity with {T}b{KHC}1. {B}ioinformatics analysis revealed the presence of homologs of this gene in other trypanosomes, including pathogens for humans and animals. {H}ost metabolism dysregulation represents an effective parasite mechanism to hamper the host immune response and modify host molecule production to favor parasite invasion and growth. {T}hus, this orphan kinesin plays an important role in promoting trypanosome infection, and its neutralization or the lock of its partner host molecules offers promising approaches to increasing resistance to infection and new developments in vaccination against trypanosomiasis.},
  keywords = {},
  booktitle = {},
  journal = {{J}ournal of {I}mmunology},
  volume = {199},
  numero = {5},
  pages = {1762--1771},
  ISSN = {0022-1767},
  year = {2017},
  DOI = {10.4049/jimmunol.1700179},
  URL = {https://www.documentation.ird.fr/hor/fdi:010070943},
}