57 research outputs found
How Effective is Sharpshooter Control at Limiting Pierce's Disease Spread in California Vineyards?
No full textPierce’s disease management in southern California vineyards hinges on chemical control of populations of the vector, the invasive glassy-winged sharpshooter (Homalodisca vitripennis), residing in citrus. Systemic insecticides (imidacloprid) are regularly applied to citrus, which is a preferred plant type for the sharpshooter, to reduce insect abundance before they move into vineyards. These treatment programs have been successful, reducing regional sharpshooter populations to a fraction of what they once were. Grape growers also frequently apply systemic insecticides in vineyards, but the efficacy of these treatments for disease management is not known. Over the last three years we conducted a series of surveys in treated and untreated vineyards in Temecula Valley to determine the relative economic value of within-vineyard chemical control for Pierces disease management. In each of the past three seasons we surveyed 34 vineyards in the Temecula Valley that differ in their use of systemic insecticides, and monitored regularly populations of sharpshooters and beneficial insects. Among the years overall Pierce’s disease prevalence was low; averaging approximately 1% based on visual symptoms. Prevalence differed slightly among fields of different treatment categories with the lowest infection rates in those vineyards that were either consistently or intermittently treated with imidacloprid. Based on sticky trap monitoring, consistently or intermittently treated vineyards also had lower catches of sharpshooters than untreated fields, but natural enemy catch did not differ appreciably among the three treatment categories. Finally, tap sampling results showed slightly lower natural enemy abundance in consistently treated sites, but the abundance of non-predatory arthropods was also substantially lower in those sites. Collectively, these results suggest that imidacloprid treatments may reduce slightly disease spread, at least in part due to reductions in vector pressure, but without any clear non-target effects on natural enemies that may lead to secondary pest outbreaks. However, it may not be critical to treat vineyards every year; at least not as long as regional vector populations continue to be reduced through areawide control programs
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Investigating the Role of the Zinc-Finger PARPs in Mediating Antiviral Innate Immunity
Get PDFMany viruses seek to manipulate the cellular environment during infection by seizing control over host post translational modifications (PTMs) by using viral E3-ubiquitin ligases, phosphatases, and kinases. Some viruses, including the genus of Alphaviruses, encode for a macrodomain, an enzymatic protein domain capable of reversing the PTM of ADP-ribosylation (ADPr). ADPr is found in a diverse range of host processes ranging from DNA damage and repair to protein quality control. When their macrodomains are disrupted, viruses lose infectious capacity, drawing attention to the importance of this modification. Identifying which host proteins are involved with this interaction could be key to understanding how these viruses are functioning and how they are manipulating the cell. The host factors at play are known as PARPs, which stands for poly-ADP-ribose-polymerases. Here, I have explored a number of these host PARPs and found novel ways in which they interact with alphaviruses to restrict viral replication. A number of PARPs are implicated in the interaction, most specifically those that either bear a macrodomain themselves, the macroPARPs of PARP9,14,and 15, or the Zinc Finger PARPS, PARP7,12, and 13. Further exploration of these PARPs, how they interact with both viral proteins and each other, is critical to fully understanding the role that ADP-ribosylation plays in restricting Alphavirus infection, as well as how alphaviruses are subverting that control
University of Nebraska College of Medicine Class of 1975 (3 Year)
No full textThree-Year - John Michael Adams, David Arnold Allerheiligen, Mark Jay Alison, Timothy Malcolm Anderson, Dean Anthony, Regan Kale Asher, Carl Earl Baker, Charles D. Barton, William Reynolds Beck, Kenneth W. Beresford, William Frank Bina, III, David Harold Bingham, Edwin John Bollerup, Matthew Merrill Bosley, Eugene Everett Bourne, Michael Frank Boyer, Dennis August Boysen, Richard M. Bregman, William E. Brennock, Bruce Harold Brumm, William Edward Brush, William Lee Buchanan, II, John Rodney Cardiff, Timothy Rae Chappell, Gary Lynn Chingren, Robert L. Collins, John Louis Colombo, Lynn Walter Cooman, Jr., Linda Blanche Blackwell Cottrell, Christopher Paul Crotty, David L. Davis, Ruth Ann Swan Demmel, Larry Dwayne Dillon, John Winston E. Douglas-Jones, Daniel Thomas Durant, Carole Kay Early, Frederick James Echternacht, Mark Edward Elles, Patrick Clay Elwood, Jimmy Dean Emery, John Michael Finkner, Desiray Claire Fitzgibbons, Glen Alan Forney, Richard Dale French, Lee Joseph Friend, Robert Anthony Frisenda, Natalie Larsen Gehringer, Nancy Germer, Richard G. Gilbert, Roderick Dean Gottula, Dennis Raymond Gutzman, Gregory David Haessler, Wayne Paul Halfar, Daniel Edward Halm, Ronald Francis Hanthorn, Gary Dean Heaton, Bruce William Henricks, Eugene N. Herbek, Dennis Lee Hodge, Robert Martin House, Jr., Mark Thomas Houser, William Gregory Hughes, Steven Lee Husen, Jerry James Hynes, Joel Edward Janousek, Mark Emil Janulewict, Roger David Jensen, Michael Bruce Jones, Gerald Frank Keasling, Mark Michael Kitzman, Michael Stephen Kochel, Linda Suzanne Kujawa, C. J. LaBenz, Dorothy Elizabeth Deppe Lawse, Olufemi Henry Lee-Johnson, Kathleen Lawless Lewis, Max Wayne Linder, Anant Kumar Lodhia, Chris Felber Maasdam, Jeffery Nesbit MacDonald, Robert James Manly, Alan Stephen Marion, Pamela Jean Masoud, David Thomas Miller, John Boyer Moeschler, Patrick William Morell, Micke C. Nave, Paul Douglas Nelsen, Robert Gene Penn, Bruce Carter Pinkerton, Ameen Ishak Ramzy, James Fred Reppert, James Burr Ross, Thomas David Roubinek, Kenneth Rene Schaefer, Donald Roger Schafer, Janet A. Schlechte, Ronald Opper Schwab, George Herbert Seberg, Jr., Robert Steven Shires, John Peter Slosburg, Gene Francis Stohs, Herschel E. Stoller, Michael Terry Sullivan, Sylvia Sydow, Milford Eugene Thieszen, James Dow Thompson, John R. Thompson, Jr., Thomas Patrick Trevisani, Charles Alfred Vacanti, Gerald L. Vitamvas, Frank Edward Waechter, III, Michael Larry Westcott, David Owen Wiebers, Donald Lee Wikoff, Mark Finley Wildgen, Michael Dale Wilkins, Stanley Dean Woerth, R. Hal Younglove, Mark Guy Zukaitas
September 26th, 1975 - Frank Joseph Daugherty
July 16th, 1975 - Allen Mark Morris, Joseph Ernest Francis Shanahan
December 19th, 1975 - Michael Joe Goeden, Mackay Joseph Hull, Terry I. Monk, Stuart Gordon Oxfordhttps://digitalcommons.unmc.edu/comclass/1056/thumbnail.jp
Display of various peptides and mini-proteins using eCPX (shaded) and CPX (white) as measured using flow cytometry
No full textThe -axis indicates the fold fluorescence above background for each protein target in the corresponding fluorescent channel. P2 was labeled with Mona, which is fused to the fluorescent protein YPet. CRPpep and V114 were labeled with biotinylated CRP and VEGF, respectively, then labeled with SA–PE. Mini-Z and T7pep were labeled with Alexa -conjugated human IgG and anti-T7•tag monoclonal IgG, respectively. SApep was detected with SA–PE.<p><b>Copyright information:</b></p><p>Taken from "Directed evolution of a biterminal bacterial display scaffold enhances the display of diverse peptides"</p><p></p><p>Protein Engineering, Design and Selection 2008;21(7):435-442.</p><p>Published online 13 May 2008</p><p>PMCID:PMC2427320.</p><p>© 2008 The Author(s)</p
Flow cytometric measurement of simultaneous N- and C-terminal display (bi-terminal display)
No full textOverlays of two-parameter histograms resulting from clones displaying SApep and P2 on the N- and C-terminus, respectively, with a 6 () or a 26 () residue linker between SApep and the N-terminus of eCPX. In both (A) and (B) plots, the four distinct populations consist of non-displaying cells mock-labeled with SA–PE and Ypet-Mona (bottom left population), cells that display SApep and P2 labeled with only SA–PE (top left population), with SA–PE and YPet-Mona (top right population), or with only YPet-Mona (bottom right population).<p><b>Copyright information:</b></p><p>Taken from "Directed evolution of a biterminal bacterial display scaffold enhances the display of diverse peptides"</p><p></p><p>Protein Engineering, Design and Selection 2008;21(7):435-442.</p><p>Published online 13 May 2008</p><p>PMCID:PMC2427320.</p><p>© 2008 The Author(s)</p
Functional and Evolutionary Analyses Identify Proteolysis as a General Mechanism for NLRP1 Inflammasome Activation
No full textDiverse viral proteases activate the NLRP1 inflammasome
Get PDFThe NLRP1 inflammasome is a multiprotein complex that is a potent activator of inflammation. Mouse NLRP1B can be activated through proteolytic cleavage by the bacterial Lethal Toxin (LeTx) protease, resulting in degradation of the N-terminal domains of NLRP1B and liberation of the bioactive C-terminal domain, which includes the caspase activation and recruitment domain (CARD). However, natural pathogen-derived effectors that can activate human NLRP1 have remained unknown. Here, we use an evolutionary model to identify several proteases from diverse picornaviruses that cleave human NLRP1 within a rapidly evolving region of the protein, leading to host-specific and virus-specific activation of the NLRP1 inflammasome. Our work demonstrates that NLRP1 acts as a 'tripwire' to recognize the enzymatic function of a wide range of viral proteases and suggests that host mimicry of viral polyprotein cleavage sites can be an evolutionary strategy to activate a robust inflammatory immune response
Functional and Evolutionary Analyses Identify Proteolysis as a General Mechanism for NLRP1 Inflammasome Activation.
Get PDFInflammasomes are cytosolic multi-protein complexes that initiate immune responses to infection by recruiting and activating the Caspase-1 protease. Human NLRP1 was the first protein shown to form an inflammasome, but its physiological mechanism of activation remains unknown. Recently, specific variants of mouse and rat NLRP1 were found to be activated upon N-terminal cleavage by the anthrax lethal factor protease. However, agonists for other NLRP1 variants, including human NLRP1, are not known, and it remains unclear if they are also activated by proteolysis. Here we demonstrate that two mouse NLRP1 paralogs (NLRP1AB6 and NLRP1BB6) are also activated by N-terminal proteolytic cleavage. We also demonstrate that proteolysis within a specific N-terminal linker region is sufficient to activate human NLRP1. Evolutionary analysis of primate NLRP1 shows the linker/cleavage region has evolved under positive selection, indicative of pathogen-induced selective pressure. Collectively, these results identify proteolysis as a general mechanism of NLRP1 inflammasome activation that appears to be contributing to the rapid evolution of NLRP1 in rodents and primates
The B6 variant of NLRP1B is not cleaved by LF but can form an inflammasome in response to proteolysis.
No full text(A) The amino acid sequence of the first 244 residues of NLRP1BB6 was aligned to the homologous sequence of NLRP1B129. The arrow above the alignment indicates the LF-cleavage site in NLRP1B129. Asterisks indicate sites of amino acid identity. (B) For detection of NLRP1B expression, 293T cells were transfected with the indicated amounts of and empty vector (V) or plasmids encoding GFP-HA-NLRP1B129 or GFP-HA-NLRP1BB6 (construct schematics and the predicted molecular weight of each protein is depicted in the upper panel). Cells were treated overnight with anthrax lethal toxin protein (LeTx, 1μg/ml) 24h post-transfection, and then lysates were analyzed by immunoblotting (IB) with the indicated antibodies. For NLRP1 expression and cleavage, CASP1 and IL1B were omitted to prevent cell death and resulting apparent differences of expression. For blots probed with anti-HA (NLRP1B), the lysates were not boiled prior to loading to prevent aggregation and smearing of full-length and FIIND-processed NLRP1B on the immunoblot. To visualize the N-terminal processed form of NLRP1B, the lysates were boiled and resolved on a separate gel. (C) 293T Cells were transfected with the same amount of titrated NLRP1B encoding plasmid and treated as in B, but transfections also included plasmids encoding mouse CASP1 (200ng), IL-1β (200ng) and 200ng of empty vector. (D) For detection of NLRP1B expression, 293T cells were transfected for 36h with 250ng of plasmids encoding WT 129 or B6 NLRP1B or mutants engineered to express the TEV-protease site. Each plasmid was co-transfected with either 100ng of empty vector (V) or plasmids encoding TEV-protease (pTEV) or lethal factor protease (pLF), supplemented with 300ng empty vector (pMSCV). Cells were not treated with LeTx and lysates were analyzed by immunoblotting as in (B). (E) Cells were treated as in C, but with 8ng of plasmids encoding NLRP1B, along with 200ng of plasmids encoding mCASP-1 and mIL-1β, and 200ng empty vector to normalize plasmid quantities. Lower quantities of NLRP1B were transfected as compared to panel D so to avoid spontaneous NLPR1B activation. For panels B-E, data shown are representative of at least three similar experiments.</p
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