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The ancient CgPEPCK-1, not CgPECK-2, evolved into a multifunctional molecule as an intracellular enzyme and extracellular PRR.
Yin, Xiaoting; Qiu, Limei; Long, Dandan; Lv, Zhao; Liu, Qing; Wang, Senyu; Zhang, Weiqian; Zhang, Kexin; Xie, Mengxi.
Afiliación
  • Yin X; CAS and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, CAS Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, 266071, China; Laboratory of Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology (Qingd
  • Qiu L; CAS and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, CAS Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, 266071, China; Laboratory of Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology (Qingd
  • Long D; CAS and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, CAS Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, 266071, China; Laboratory of Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology (Qingd
  • Lv Z; CAS and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, CAS Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, 266071, China; Laboratory of Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology (Qingd
  • Liu Q; CAS and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, CAS Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, 266071, China; Laboratory of Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology (Qingd
  • Wang S; CAS and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, CAS Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, 266071, China; School of Marine Biology and Engineering, Qingdao Agricultural University, Qingdao, 266109, China.
  • Zhang W; CAS and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, CAS Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, 266071, China.
  • Zhang K; CAS and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, CAS Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, 266071, China; School of Marine Biology and Engineering, Qingdao Agricultural University, Qingdao, 266109, China.
  • Xie M; CAS and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, CAS Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, 266071, China.
Dev Comp Immunol ; 145: 104722, 2023 08.
Article en En | MEDLINE | ID: mdl-37116769
Phosphoenolpyruvate carboxykinase (PEPCK) is a well-known lyase involved in gluconeogenesis, while their evolution and function differentiation have not been fully understood. In this study, by constructing a phylogenetic tree to examine PEPCKs throughout the evolution from poriferans to vertebrates, Mollusk was highlighted as the only phylum to exhibit two distinct lineages, Mollusca_PEPCK-1 and Mollusca_PEPCK-2. Further study of two representative members from Crassostrea gigas (CgPEPCK-1 and CgPEPCK-2) showed that they both shared conserved sequences and structural characteristics of the catalytic enzyme, while CgPEPCK-2 displayed a higher expression level than CgPEPCK-1 in all tested tissues, and CgPEPCK-1 was specifically implicated in the immune defense against LPS stimulation and Vibrio splendidus infection. Functional analysis revealed that CgPEPCK-2 had stronger enzymatic activity than CgPEPCK-1, while CgPEPCK-1 exhibited stronger binding activity with various PAMPs, and only the protein of CgPEPCK-1 increased significantly in hemolymph during immune stimulation. All results supported that distinct sequence and function differentiations of the PEPCK gene family should have occurred since Mollusk. The more advanced evolutionary branch Mollusca_PEPCK-2 should preserve its essential function as a catalytic enzyme to be more specialized and efficient, while the ancient branch Mollusca_PEPCK-1 probably contained some members, such as CgPEPCK-1, that should be integrated into the immune system as an extracellular immune recognition receptor.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Vibriosis / Fosfoenolpiruvato Carboxiquinasa (ATP) Límite: Animals Idioma: En Revista: Dev Comp Immunol Año: 2023 Tipo del documento: Article Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Vibriosis / Fosfoenolpiruvato Carboxiquinasa (ATP) Límite: Animals Idioma: En Revista: Dev Comp Immunol Año: 2023 Tipo del documento: Article Pais de publicación: Estados Unidos