title: Desiccation stress of entomopathogenic nematodes induces the accumulation of a novel heat-stable protein.
abstract: The present study describes a novel heat-stable, water-stress-related protein with a molecular mass of 47 kDa (designated Desc47) in the entomopathogenic nematode Steinernemafeltiae (IS-6). The protein was accumulated about 10-fold (from 7.84 +/- 1.85 to 74.09 +/- 4.35 % relative content level [RCL]) in dehydrated clumps of infective juveniles (IJs), which had lost 344.% of their initial water content (from 65.1 +/- 1.7% to 427 +/- 0.72%) in a desiccation-tolerance-inducing treatment (97% relative humidity [RH] for 3 days). The appearance of Desc47 was accompanied by trehalose accumulation (from 300 to 600 mg trehalose/g protein) during the process of inducing the IJs into a quiescent anhydrobiotic state. A second cycle of IJ dehydration did not alter the RCL of Desc47 (79.3% for the first cycle and 73.3% for the second cycle). Desc47 retained its high RCL (69.7%) in rehydrated active IJs for 3 days, reaching 51.2% of its initial RCL only after a week. No homology to other known proteins was found by mass-spectrometry electrospray-ion-trap analysis. However, of the 5 sequences obtained from the 11protein(ranging from to 21 amino acids), the 21-amino-acid peptide N V A S D A V E T V G N A A G Q A G (D/T) A V showed excellent homology (74% identity in 19 amino acids) to the cold-responsive protein COR14b (g6564861) from Triticum aestivum. In the Caenorhabditis elegans predicted proteome database search, the N21 yielded the first-best identity score (59 % identity in 17 amino acids) to the CE-LEA homologue protein (g2353333). In plants, COR and LEA are related proteins, heat-stable, which are expressed in response to both dehydration and cold acclimation. The implication of the involvement of Desc47 and the osmoprotectant trehalose in the desiccation-tolerance mechanisms of S. feltiae is discussed.
authors.affiliation: Department of Animal Sciences, Faculty of Agricultural, Food and Environmental Quality Sciences of the Hebrezw University of Jerusalem, Rehovot, Israel. a-Solomon3@northwestern.edu
authors.forename: A
authors.initials: A
authors.lastname: Solomon
authors.forename: R
authors.initials: R
authors.lastname: Salomon
authors.forename: I
authors.initials: I
authors.lastname: Paperna
authors.forename: I
authors.initials: I
authors.lastname: Glazer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003890:Desiccation; D004591:Electrophoresis, Polyacrylamide Gel / Q000662:veterinary; D006360:Heat-Shock Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D006358:Hot Temperature; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009348:Nematoda / Q000378:metabolism*; D016415:Sequence Alignment; D014199:Trehalose / Q000378:metabolism; D014867:Water
chemical_list: C417862:Desc47 protein, Steinernemafeltiae; D006360:Heat-Shock Proteins; D014867:Water; D014199:Trehalose