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• W2144427831 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 Steinernema feltiae (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 34·4% of their initial water content (from 65·1±1·7% to 42·7±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 protein (ranging from 11 to 21 amino acids), the 21-amino-acid peptide NVASDAVETVGNAAGQAG(D/T)AV 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." @default.
• W2144427831 created "2016-06-24" @default.
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• W2144427831 date "2000-10-01" @default.
• W2144427831 modified "2023-09-26" @default.
• W2144427831 title "Desiccation stress of entomopathogenic nematodes induces the accumulation of a novel heat-stable protein" @default.
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• W2144427831 doi "https://doi.org/10.1017/s0031182099006563" @default.
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