Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The whitefly Bemisia tabaci is an important pest of worldwide agriculture. Previous work has shown that B. tabaci actively suppresses host plant defenses, but our knowledge of the specific mechanisms involved remains limited. Here we describe a B. tabaci salivary protein, the ferritin BtFer1, and its role in facilitating exploitation of host plants. We show that BtFer1 exhibits Fe2+ binding ability and ferroxidase activity, and that secretion of BtFer1 during B. tabaci feeding suppresses H2O2-generated oxidative signals in tomato (Solanum lycopersicum). Silencing BtFer1 enhanced the induction of the jasmonic acid (JA)-mediated defense signaling pathway in response to whitefly feeding, and led to increased callose deposition and the production of proteinase inhibitors that prevent whiteflies from continuously ingesting and digesting phloem sap. Consistent with these effects, silencing BtFer1 reduced whitefly survival on tomato but not on artificial diet. Using a JA-deficient spr2 mutant plant further showed that suppression of JA defenses by BtFer1 is sufficient to increase B. tabaci survival. Taken together, these results demonstrate that BtFer1 acts as an effector protein that mediates whitefly-tomato interactions. These findings represent an important step forward in understanding the molecular mechanisms by which whiteflies and other insect herbivores suppress host plant defenses.
J Exp Bot 2019 06 28
PMID:A salivary ferritin in the whitefly suppresses plant defenses and facilitates host exploitation. 3094 71

Members of the Low Phosphate Root (LPR) family have been identified in rice (Oryza sativa) and expression analyses have been conducted. Here, we investigated the functions of one of the five members in rice, LPR5. qRT-PCR and promoter-GUS reporter analyses indicated that under Pi-sufficient conditions OsLPR5 was highly expressed in the roots, and specific expression occurred in the leaf collars and nodes, and its expression was increased under Pi-deficient conditions. In vitro analysis of the purified OsLPR5 protein showed that it exhibited ferroxidase activity. Overexpression of OsLPR5 triggered higher ferroxidase activity, and elevated concentrations of Fe(III) in the xylem sap and of total Fe in the roots and shoots. Transient expression of OsLPR5 in Nicotiana benthamiana provided evidence of its subcellular localization to the cell wall and endoplasmic reticulum. Knockout mutation in OsLPR5 by means of CRISPR-Cas9 resulted in adverse effects on Pi translocation, on the relative expression of Cis-NATOsPHO1;2, and on several morphological traits, including root development and yield potential. Our results indicate that ferroxidase-dependent OsLPR5 has both a broad-spectrum influence on growth and development in rice as well as affecting a subset of physiological and molecular traits that govern Pi homeostasis.
J Exp Bot 2020 Aug 06
PMID:The ferroxidase LPR5 functions in the maintenance of phosphate homeostasis and is required for normal growth and development of rice. 3261 34