Tyrosine phosphate hydrolysis of host proteins by Trypanosoma cruzi is linked to cell invasion.
Invasion of cultured L6E9 myoblasts by Trypanosoma cruzi induced tyrosine dephosphorylation of proteins of 234, 205, and 50 kDa. Invasion was greatly reduced in the presence of the protein tyrosine phosphate inhibitors sodium o-vanadate and zinc chloride, and in the presence of excess phosphotyrosine or p-nitrophenyl phosphate, but not in the presence of excess phosphoserine or phosphothreonine. These results suggest an important role for protein tyrosine dephosphorylation in the invasion of host cells by T. cruzi.
Zhong
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Department of Pathobiology, University of Illinois at Urbana-Champaign 61802, USA.
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Moreno
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D000818:Animals; D006868:Hydrolysis; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases / Q000037:antagonists & inhibitors / Q000502:physiology; D011506:Proteins / Q000378:metabolism*; D014349:Trypanosoma cruzi / Q000502:physiology*; D014443:Tyrosine / Q000378:metabolism*
D011506:Proteins; D014443:Tyrosine; D017027:Protein Tyrosine Phosphatases