Protein Serine/Threonine Phosphatase Type 2C of Leishmania mexicana

Frontiers in Cellular and Infection Microbiology

Mariana Zuñiga-Fabián¹  Nallely Cabrera²  Ruy Pérez-Montfort²  Ricardo Mondragón-Flores³  Jenny Nancy Gómez-Sandoval⁴  Araceli Rojas-Bernabé⁵  Maria Magdalena Aguirre-García⁶  Alma Reyna Escalona-Montaño⁶  Laila Gutiérrez-Kobeh⁶  Augusto González-Canto⁷  Ingeborg Becker⁷ 

[1] Ciencias Experimentales, Escuela Nacional Colegio de Ciencias y Humanidades Plantel, Naucalpan, Mexico;Departamento de Bioquímica y Biología Estructural, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Ciudad de México, Mexico;Departamento de Bioquímica, Centro de Investigación y Estudios Avanzados (CINVESTAV-IPN), Ciudad de México, Mexico;División de Ingeniería en Biotecnología, Universidad Politécnica del Valle de Toluca, Almoloya de Juárez, Mexico;Escuela Superior de Medicina, Instituto Politécnico Nacional, Ciudad de México, Mexico;Unidad de Investigación UNAM-INC, División de Investigación, Facultad de Medicina, Instituto Nacional de Cardiología Ignacio Chávez., Ciudad de México, Mexico;Unidad de Investigación en Medicina Experimental, Facultad de Medicina, Universidad Nacional Autónoma de México, Hospital General de México, Ciudad de México, Mexico;

关键词: phosphoprotein phosphatase;    threonine phosphatases;    PP2C;    Leishmania mexicana;    leishmaniasis;   

DOI  :  10.3389/fcimb.2021.641356

来源: Frontiers

【 摘 要 】

Protein phosphorylation and dephosphorylation are increasingly recognized as important processes for regulating multiple physiological mechanisms. Phosphorylation is carried out by protein kinases and dephosphorylation by protein phosphatases. Phosphoprotein phosphatases (PPPs), one of three families of protein serine/threonine phosphatases, have great structural diversity and are involved in regulating many cell functions. PP2C, a type of PPP, is found in Leishmania, a dimorphic protozoan parasite and the causal agent of leishmaniasis. The aim of this study was to clone, purify, biochemically characterize and quantify the expression of PP2C in Leishmania mexicana (LmxPP2C). Recombinant LmxPP2C dephosphorylated a specific threonine (with optimal activity at pH 8) in the presence of the manganese divalent cation (Mn+2). LmxPP2C activity was inhibited by sanguinarine (a specific inhibitor) but was unaffected by protein tyrosine phosphatase inhibitors. Western blot analysis indicated that anti-LmxPP2C antibodies recognized a molecule of 45.2 kDa. Transmission electron microscopy with immunodetection localized LmxPP2C in the flagellar pocket and flagellum of promastigotes but showed poor staining in amastigotes. Interestingly, LmxPP2C belongs to the ortholog group OG6_142542, which contains only protozoa of the family Trypanosomatidae. This suggests a specific function of the enzyme in the flagellar pocket of these microorganisms.

【 授权许可】

CC BY