scholarly journals Role of Intrinsic Disorder in Animal Desiccation Tolerance

PROTEOMICS ◽  
2018 ◽  
Vol 18 (21-22) ◽  
pp. 1800067 ◽  
Author(s):  
Brett Janis ◽  
Clinton Belott ◽  
Michael A. Menze
Keyword(s):  
Desiccation Tolerance ◽  
Intrinsic Disorder

Role of the Sheath in Desiccation Tolerance of Two Entomopathogenic Nematodes

Nematologica ◽  
1991 ◽  
Vol 37 (1-4) ◽  
pp. 324-332 ◽  
Author(s):  
R. Gaugler ◽  
L. Rickert Campbell
Keyword(s):  
Desiccation Tolerance ◽  
Entomopathogenic Nematodes

The role of peltate scales in desiccation tolerance of Pleopeltis polypodioides

Planta ◽  
2016 ◽  
Vol 245 (1) ◽  
pp. 207-220 ◽  
Author(s):  
Susan P. John ◽  
Karl H. Hasenstein
Keyword(s):  
Desiccation Tolerance

Desiccation tolerance in developing soybean seeds: The role of stress proteins

1995 ◽  
Vol 93 (4) ◽  
pp. 630-638 ◽  
Author(s):  
S. A. Blackman ◽  
R. L. Obendorf ◽  
A. C. Leopold
Keyword(s):  
Desiccation Tolerance ◽  
Stress Proteins ◽  
Soybean Seeds

Role of intrinsic disorder in transient interactions of hub proteins

2006 ◽  
Vol 66 (4) ◽  
pp. 761-765 ◽  
Author(s):  
Gajinder Pal Singh ◽  
Mythily Ganapathi ◽  
Debasis Dash
Keyword(s):  
Intrinsic Disorder ◽  
Transient Interactions ◽  
Hub Proteins

Desiccation tolerance in developing soybean seeds: The role of stress proteins

1995 ◽  
Vol 93 (4) ◽  
pp. 630-638 ◽  
Author(s):  
S. A. Blackman ◽  
R. L. Obendorf ◽  
A. C. Leopold
Keyword(s):  
Desiccation Tolerance ◽  
Stress Proteins ◽  
Soybean Seeds

scholarly journals The role of phospholipid headgroup composition and trehalose in the desiccation tolerance of Caenorhabditis elegans

Cryobiology ◽  
2015 ◽  
Vol 71 (3) ◽  
pp. 551
Author(s):  
Sawsan E. Abusharkh ◽  
Cihan Erkut ◽  
Jana Oertel ◽  
Teymuras V. Kurzchalia ◽  
Karim Fahmy
Keyword(s):  
Caenorhabditis Elegans ◽  
Desiccation Tolerance

scholarly journals Investigation of a new mechanism of desiccation-stress tolerance in Salmonella

2013 ◽  
Author(s):  
Shlomo Sela ◽  
Michael McClelland
Keyword(s):  
Desiccation Tolerance ◽  
Biofilm Formation ◽  
Function Analysis ◽  
Swarming Motility ◽  
Comparable Amount ◽  
Dehydration Tolerance ◽  
Regulatory Pathways ◽  
Pathogen Survival ◽  
Surfactant Activity

Low-moisture foods (LMF) are increasingly involved in foodborne illness. While bacteria cannot grow in LMF due to the low water content, pathogens such as Salmonella can still survive in dry foods and pose health risks to consumer. We recently found that Salmonella secretes a proteinaceous compound during desiccation, which we identified as OsmY, an osmotic stress response protein of 177 amino acids. To elucidate the role of OsmY in conferring tolerance against desiccation and other stresses in Salmonella entericaserovarTyphimurium (STm), our specific objectives were: (1) Characterize the involvement of OsmY in desiccation tolerance; (2) Perform structure-function analysis of OsmY; (3) Study OsmY expression under various growth- and environmental conditions of relevance to agriculture; (4) Examine the involvement of OsmY in response to other stresses of relevance to agriculture; and (5) Elucidate regulatory pathways involved in controlling osmY expression. We demonstrated that an osmY-mutant strain is impaired in both desiccation tolerance (DT) and in long-term persistence during cold storage (LTP). Genetic complementation and addition of a recombinantOsmY (rOsmY) restored the mutant survival back to that of the wild type (wt). To analyze the function of specific domains we have generated a recombinantOsmY (rOsmY) protein. A dose-response DT study showed that rOsmY has the highest protection at a concentration of 0.5 nM. This effect was protein- specific as a comparable amount of bovine serum albumin, an unrelated protein, had a three-time lower protection level. Further characterization of OsmY revealed that the protein has a surfactant activity and is involved in swarming motility. OsmY was shown to facilitate biofilm formation during dehydration but not during bacterial growth under optimal growth conditions. This finding suggests that expression and secretion of OsmY under stress conditions was potentially associated with facilitating biofilm production. OsmY contains two conserved BON domains. To better understand the role of the BON sites in OsmY-mediated dehydration tolerance, we have generated two additional rOsmY constructs, lacking either BON1 or BON2 sites. BON1-minus (but not BON2) protein has decreased dehydration tolerance compared to intact rOsmY, suggesting that BON1 is required for maximal OsmY-mediated activity. Addition of BON1-peptide at concentration below 0.4 µM did not affect STm survival. Interestingly, a toxic effect of BON1 peptide was observed in concentration as low as 0.4 µM. Higher concentrations resulted in complete abrogation of the rOsmY effect, supporting the notion that BON-mediated interaction is essential for rOsmY activity. We performed extensive analysis of RNA expression of STm undergoing desiccation after exponential and stationary growth, identifying all categories of genes that are differentially expressed during this process. We also performed massively in-parallel screening of all genes in which mutation caused changes in fitness during drying, identifying over 400 such genes, which are now undergoing confirmation. As expected OsmY is one of these genes. In conclusion, this is the first study to identify that OsmY protein secreted during dehydration contributes to desiccation tolerance in Salmonella by facilitating dehydration- mediated biofilm formation. Expression of OsmY also enhances swarming motility, apparently through its surfactant activity. The BON1 domain is required for full OsmY activity, demonstrating a potential intervention to reduce pathogen survival in food processing. Expression and fitness screens have begun to elucidate the processes of desiccation, with the potential to uncover additional specific targets for efforts to mitigate pathogen survival in desiccation. 

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