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Peptidoglycan recognition proteins from the earthworm, Eisenia andrei: Differential inducibility and tissue-specific expression.
Park, Beom Jun; Yoon, Yoo Bin; Park, Soon Cheol; Lee, Dong Ho; Shin, Chuog; Kwak, Hee-Jin; Kim, Jung-Woong; Cho, Sung-Jin.
Afiliación
  • Park BJ; Department of Life Science, Chung-Ang University, Seoul, 06974, South Korea.
  • Yoon YB; Department of Life Science, Chung-Ang University, Seoul, 06974, South Korea.
  • Park SC; Department of Life Science, Chung-Ang University, Seoul, 06974, South Korea.
  • Lee DH; Da Vinci College of General Education, Chung-Ang University, Seoul, 06974, South Korea.
  • Shin C; Department of Biological Science and Technology, College of Science and Technology, Yonsei University, Wonju, 26493, South Korea.
  • Kwak HJ; Department of Ecology, Evolution and Behavior, Alexander Silberman Institute of Life Sciences, Faculty of Science, Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.
  • Kim JW; Department of Life Science, Chung-Ang University, Seoul, 06974, South Korea. Electronic address: jungkim@cau.ac.kr.
  • Cho SJ; Department of Biological Sciences and Biotechnology, Chungbuk National University, Chungbuk, 28644, South Korea. Electronic address: sjchobio@chungbuk.ac.kr.
Dev Comp Immunol ; 135: 104483, 2022 10.
Article en En | MEDLINE | ID: mdl-35760219
Several pattern recognition receptors (PRRs) involved in innate immunity have been identified and characterized in earthworms. Peptidoglycan recognition proteins (PGRPs) are highly conserved PRRs that activate effector pathways such as prophenoloxidase cascade and Toll-like receptor pathway. In addition, PGRPs function as an enzyme, N-acetylmuramoyl-l-alanine amidase (NAMLAA), to directly hydrolyze peptidoglycan. We identified four full-length complementary DNA (cDNA) sequences, Ean-PGRP1/2/3/4, in Eisenia andrei, an earthworm. Sequence and phylogenetic analyses indicate that earthworm PGRP orthologs resemble short PGRP member proteins. The subcellular localizations of four Ean-PGRPs lacking the transmembrane domain are predicted to be extracellular or cytoplasmic. All Ean-PGRPs contain a highly conserved PGRP domain with a conserved Zn2+ binding site including a tyrosine residue essential for active amidase activity. Three highly conserved amino-acid residues (His, Trp, and Thr) necessary for amidase activity are also present, indicating that the Ean-PGRPs can be predicted to have amidase activity. Furthermore, we demonstrate that the Ean-PGRP genes are differentially induced by certain bacterial species, suggesting that the innate immune system of earthworms is likely to be somewhat specific rather than entirely non-specific. Tissue expression patterns indicate that Ean-PGRP mRNAs are primarily expressed in the immune-competent tissues and that their expression is tissue-specific according to Ean-PGRP types, particularly for Ean-PGRP1.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oligoquetos Límite: Animals Idioma: En Revista: Dev Comp Immunol Año: 2022 Tipo del documento: Article País de afiliación: Corea del Sur Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oligoquetos Límite: Animals Idioma: En Revista: Dev Comp Immunol Año: 2022 Tipo del documento: Article País de afiliación: Corea del Sur Pais de publicación: Estados Unidos