40 research outputs found

    HTLV-1 infection in solid organ transplant donors and recipients in Spain

    Get PDF
    Background: HTLV-1 infection is a neglected disease, despite infecting 10–15 million people worldwide and severe illnesses develop in 10% of carriers lifelong. Acknowledging a greater risk for developing HTLV-1 associated illnesses due to immunosuppression, screening is being widely considered in the transplantation setting. Herein, we report the experience with universal HTLV testing of donors and recipients of solid organ transplants in a survey conducted in Spain. Methods: All hospitals belonging to the Spanish HTLV network were invited to participate in the study. Briefly, HTLV antibody screening was performed retrospectively in all specimens collected from solid organ donors and recipients attended since the year 2008. Results: A total of 5751 individuals were tested for HTLV antibodies at 8 sites. Donors represented 2312 (42.2%), of whom 17 (0.3%) were living kidney donors. The remaining 3439 (59.8%) were recipients. Spaniards represented nearly 80%. Overall, 9 individuals (0.16%) were initially reactive for HTLV antibodies. Six were donors and 3 were recipients. Using confirmatory tests, HTLV-1 could be confirmed in only two donors, one Spaniard and another from Colombia. Both kidneys of the Spaniard were inadvertently transplanted. Subacute myelopathy developed within 1 year in one recipient. The second recipient seroconverted for HTLV-1 but the kidney had to be removed soon due to rejection. Immunosuppression was stopped and 3 years later the patient remains in dialysis but otherwise asymptomatic. Conclusion: The rate of HTLV-1 is low but not negligible in donors/recipients of solid organ transplants in Spain. Universal HTLV screening should be recommended in all donor and recipients of solid organ transplantation in Spain. Evidence is overwhelming for very high virus transmission and increased risk along with the rapid development of subacute myelopath

    Rapid subacute myelopathy following kidney transplantation from HTLV-1 donors: role of immunosuppresors and failure of antiretrovirals

    Get PDF
    Two kidney transplant recipients from a single donor became infected with HTLV-1 (human T-lymphotropic virus type 1) in Spain. One developed myelopathy 8 months following surgery despite early prescription of antiretroviral therapy. The allograft was removed from the second recipient at month 8 due to rejection and immunosuppressors discontinued. To date, 3 years later, this patient remains infected but asymptomatic. HTLV-1 infection was recognized retrospectively in the donor, a native Spaniard who had sex partners from endemic regions. Our findings call for a reappraisal of screening policies on donor-recipient organ transplantation. Based on the high risk of disease development and the large flux of persons from HTLV-1 endemic regions, pre-transplant HTLV-1 testing should be mandatory in Spain

    Overview of the JET results in support to ITER

    Get PDF

    Molecular Cloning And Insecticidal Effect Of Inga Laurina Trypsin Inhibitor On Diatraea Saccharalis And Heliothis Virescens

    No full text
    Native Inga laurina (Fabaceae) trypsin inhibitor (ILTI) was tested for anti-insect activity against Diatraea saccharalis and Heliothis virescens larvae. The addition of 0.1% ILTI to the diet of D. saccharalis did not alter larval survival but decreased larval weight by 51%. The H. virescens larvae that were fed a diet containing 0.5% ILTI showed an 84% decrease in weight. ILTI was not digested by the midgut proteinases of either species of larvae. The trypsin levels were reduced by 55.3% in the feces of D. saccharalis and increased by 24.1% in the feces of H. virescens. The trypsin activity in both species fed with ILTI was sensitive to the inhibitor, suggesting that no novel proteinase resistant to ILTI was induced. Additionally, ILTI exhibited inhibitory activity against the proteinases present in the larval midgut of different species of Lepidoptera. The organization of the ilti gene was elucidated by analyzing its corresponding genomic sequence. The recombinant ILTI protein (reILTI) was expressed and purified, and its efficacy was evaluated. Both native ILTI and reILTI exhibited a similar strong inhibitory effect on bovine trypsin activity. These results suggest that ILTI presents insecticidal properties against both insects and may thus be a useful tool in the genetic engineering of plants. © 2012 Elsevier Inc.1563-4148158Abdeen, A., Virgos, A., Olivella, E., Villanueva, J., Aviles, X., Gabarra, R., Prat, S., Multiple insect resistance in transgenic tomato plants over-expressing two families of plant proteinase inhibitors (2005) Plant Mol. Biol., 57, pp. 189-202Alfonso-Rubí, J., Ortego, F., Castañera, P., Carbonero, P., Díaz, I., Transgenic expression of trypsin inhibitor CMe from barley in indica and japonica rice, confers resistance to the rice weevil Sitophilus oryzae (2003) Transgenic Res., 12, pp. 23-31Babu, S.R., Subrahmanyam, S., Bio-potency of serine proteinase inhibitors from Acacia senegal seeds on digestive proteinases, larval growth and development of Helicoverpa armigera (Hübner) (2010) Pestic. Biochem. Physiol., 98, pp. 349-358Bhattacharyya, A., Leighton, S.M., Babu, C.R., Bioinsecticidal activity of Archidendron ellipticum trypsin inhibitor on growth and serine digestive enzymes during larval development of Spodoptera litura (2007) Comp. Biochem. Physiol., 145, pp. 669-677Bijina, B., Chellappan, S., Basheer, S.M., Elyas, K.K., Bahkali, A.H., Chandrasekaran, M., Protease inhibitor from Moringa oleifera leaves: Isolation, purification, and characterization (2011) Process. Biochem., 46, pp. 2291-2300Boulter, D., Insect pest control by copying nature using genetically engineered crops (1993) Phytochemistry, 34, pp. 1453-1466Bown, D.P., Wilkinson, H.S., Gatehouse, J.A., Regulation of expression of genes encoding digestive proteases in the gut of a polyphagous lepidopteran larva in response to dietary protease inhibitors (2004) Physiol. Entomol., 29, pp. 278-290Bradford, M.M., A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254Breiteneder, H., Radauer, C., A classification of plant food allergens (2004) J. Allergy Clin. Immunol., 113, pp. 821-830Brioschi, D., Nadalini, L.D., Bengtson, M.H., Sogayar, M.C., Moura, D.S., Silva-Filho, M.C., General up regulation of Spodoptera frugiperda trypsins and chymotrypsins allows its adaptation to soybean proteinase inhibitor (2007) Insect Biochem. Mol. Biol., 37, pp. 1283-1290Brito, L.O., Lopes, A.R., Parra, J.R.P., Terra, W.R., Silva-Filho, M.C., Adaptation of tobacco budworm Heliothis virescens to proteinase inhibitors may be mediated by the synthesis of new proteinases (2001) Comp. Biochem. Physiol. B, 128, pp. 365-375Broadway, R.M., Duffey, S.S., The effect of dietary protein on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua (1986) J. Insect Physiol., 32, pp. 673-680Carlini, C.R., Grossi-De-Sá, M.F., Plant toxic proteins with insecticidal properties, a review on their potentialities as bioinsecticides (2002) Toxicon, 40, pp. 1515-1539Coelho, M.B., Marangoni, S., MacEdo, M.L.R., Insecticidal action of Annona coriacea lectin against the flour moth Anagasta kuehniella and the rice moth Corcyra cephalonica (Lepidoptera: Pyralidae) (2007) Comp. Biochem. Physiol. C, 146, pp. 406-414De Leo, F., Bonadé-Bottino, M.A., Ceci, L.R., Gallerani, R., Jouanin, L., Opposite effects on Spodoptera littoralis larvae of high expression level of a trypsin proteinase inhibitor in transgenic plants (1998) Plant Physiol., 118, pp. 997-1004Dunse, K.M., Stevens, J.A., Lay, F.T., Gaspar, Y.M., Heath, R.L., Anderson, M.A., Coexpression of potato type i and II proteinase inhibitors gives cotton plants protection against insect damage in the field (2010) PNAS, 107, pp. 15011-15015Erlanger, B.F., Kokowsky, N., Cohen, W., The preparation and properties of two chromogenic substrates of trypsin (1961) Arch. Biochem. Biophys., 95, pp. 271-278Falco, M.C., Silva, F.M.C., Expression of soybean proteinase inhibitors in transgenic sugarcane plants: Effects on natural defense against Diatraea saccharalis (2003) Plant Physiol. Biochem., 41, pp. 761-766Fan, S.G., Wu, G.J., Characteristics of plant proteinase inhibitors and their applications in combating phytophagous insects (2005) Bot. Bull. Acad. Sin., 46, pp. 273-292Farrar, R.R., Barbour, J.D., Kenedy, G.G., Quantifying food consumption and growth in insects (1989) Ann. Entomol. Soc. Am., 82, pp. 593-598Ferry, N., Edwards, M.G., Gatehouse, T., Campell, P., Christou, P., Gatehouse, A.M.R., Transgenic plants for insect pest control: A forward looking scientific perspective (2006) Transgenic Res., 15, pp. 13-19Fitt, G.P., The ecology of Heliothis species in relation to agroecosystems (1989) Annu. Rev. Entomol., 34, pp. 17-52Garcia, V.A., Freire, M.G.M., Novello, J.C., Marangoni, S., MacEdo, M.L.R., Trypsin inhibitor from Poecilanthe parviflora seeds: Purification, characterization, and activity against pest proteinases (2004) Protein J., 23, pp. 343-350Gatehouse, J.A., Prospects for using proteinase inhibitors to protect transgenic plants against attack by herbivorous insects (2011) Curr. Protein Pept. Sci., 5, pp. 409-416Girard, C., Le Metayer, M., Bonade-Bottino, M., Pham-Delegue, M.H., Jouanin, L., High level of resistance to proteinase inhibitors may be conferred by proteolytic cleavage in beetle larvae (1998) Insect Biochem. Mol. Biol., 28, pp. 229-237Girard, C., Le Metayer, M., Zaccomer, B., Bartlet, E., Williams, I., Bonade-Bottino, M., Pham-Delegue, M.H., Jouanin, L., Growth stimulation of beetle larvae reared on transgenic oilseed rape expressing a cysteine proteinase inhibitor (1998) J. Insect Physiol., 44, pp. 263-270Giri, A.P., Harsulkar, A.M., Deshpande, V.V., Sainani, M.N., Gupta, V.S., Ranjekar, P.K., Chickpea defensive proteinase inhibitors can be inactivated by podborer gut proteinases (1998) Plant Physiol., 116, pp. 393-401Giri, A.P., Chougule, N.P., Telang, M.A., Gupta, V.S., Engineering insect tolerant plants using plant defensive proteinase inhibitors (2005) Phytochemistry, 8, pp. 117-137Gomes, C.E.M., Barbosa, A.E.A.D., MacEdo, L.L.P., Pitanga, J.C.M., Moura, F.T., Oliveira, A.S., Moura, R.M., Sales, M.P., Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly) (2005) Plant Physiol. Biochem., 43, pp. 1095-1102Gotor, C., Pintor-Toro, J.A., Romero, L.C., Isolation of a new member of the soybean Kunitz-type proteinase inhibitors (1995) Plant Physiol., 107, pp. 1015-1016Harsulkar, A.M., Giri, A.P., Patankar, A.G., Gupta, V.S., Sainani, M.N., Ranjekar, P.K., Deshpande, V.V., Successive use of non-host plant proteinase inhibitors required for effective inhibition of gut proteinases and larval growth of Helicoverpa armigera (1999) Plant Physiol., 121, pp. 450-497Hartl, M., Giri, A.P., Kaur, H., Baldwin, I.T., Serine proteinase inhibitors specifically defend Solanum nigrum against generalist herbivores but do not influence plant growth and development (2010) Plant Cell, 22, pp. 4158-4175Hilder, V.A., Gatehouse, A.M.R., Boulter, D., Transgenic plants conferring insect tolerance: Proteinase inhibitor approach (1993) Transgenic Plants Eng. Util., 1, pp. 317-338Hung, C.H., Peng, P.H., Huang, C.C., Wang, H.L., Chen, Y.J., Chen, Y.L., Chi, L.M., Genomic and cDNA cloning, characterization of Delonix regia trypsin inhibitor (DrTI) gene, and expression of DrTI in Escherichia coli (2007) Biosci. Biotechnol. Biochem., 71, pp. 98-103Jongsma, M.A., Bolter, C.J., The adaptation of insects to plant proteinase inhibitors (1997) J. Insect Physiol., 43, pp. 885-896Jongsma, M.A., Bakker, P.L., Peters, J., Bosch, D., Stiekema, W.J., Adaptation of Spodoptera exigua larvae to plant proteinase inhibitors by induction of gut proteinase activity insensitive to inhibition (1995) Proc. Natl. Acad. Sci. U. S. A., 92, pp. 8041-8045Kim, J.Y., Park, S.C., Kim, M.H., Lim, H.T., Park, Y., Hahm, K.S., Antimicrobial activity studies on a trypsin-chymotrypsin proteinase inhibitor obtained from potato (2005) Biochem. Biophys. Res. Commun., 330, pp. 921-927Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685Lingaraju, M.H., Gowda, L.R., A Kunitz trypsin inhibitor of Entada scandens seeds: Another member with single disulfide bridge (2008) BBA, 1784, pp. 850-855Lopes, J.L.S., Valadares, N.F., Moraes, D.I., Rosa, J.C., Araújo, H.S.S., Beltramini, L.M., Physico-chemical and antifungal properties of proteinase inhibitors from Acacia plumose (2009) Phytochemistry, 70, pp. 871-879Lorenzi, H., (2002) Árvores Brasileiras: Manual de Identificação e Cultivos de Plantas Arbóreas Do Brasil, 2. , 2a ed. Editora Plantarum Nova Odessa 368 ppMacEdo, M.L.R., Fernandes, K.V.S., Sales, M.P., Xavier-Filho, J., Vicilins variants and the resistance of cowpea (Vigna unguiculata) seeds to the cowpea weevil (Callosobruchus maculatus) (1993) Comp. Biochem. Physiol. C, 105, pp. 89-94MacEdo, M.L.R., Mello, G.C., Freire, M.G.M., Novello, J.C., Marangoni, S., Matos, D.G.G., Effect of a trypsin inhibitor from Dimorphandra mollis seeds on the development of Callosobruchus maculates (2002) Plant Physiol. Biochem., 40, pp. 891-898MacEdo, M.L.R., Garcia, V.A., Freire, M.G.M., Richardson, M., Characterization of a Kunitz trypsin inhibitor with a single disulfide bridge from seeds of Inga laurina (SW.) Willd (2007) Phytochemistry, 68, pp. 1104-1111MacEdo, M.L.R., Pando, S.C., Chevreuil, L.R., Marangoni, S., Properties of a Kunitz-type trypsin inhibitor from Delonix regia seeds against digestive proteinases of Anagasta kuehniella (Z.) and Corcyra cephalonica (S.) (Lepidoptera: Pyralidae) (2009) Protein Pept. Lett., 16, pp. 1459-1465MacEdo, M.L.R., Freire, M.G.M., Franco, O.L., Migliolo, L., Oliveira, C.F.R., Practical and theoretical characterization of Inga laurina Kunitz inhibitor on the control of Homalinotus coriaceus (2011) Comp. Biochem. Physiol. B, 158, pp. 164-172Major, I.L., Constabel, C.P., Functional analysis of the Kunitz trypsin inhibitor family in poplar reveals biochemical diversity and multiplicity in defense against herbivore (2008) Plant Physiol., 146, pp. 888-903Marchetti, S., Delledonne, M., Fogher, C., Chiabà, C., Chiesa, F., Savazzini, F., Giordano, A., Soybean Kunitz, C-II and PI-IV inhibitor genes confer different levels of insect resistance to tobacco and potato transgenic plants (2000) Theor. Appl. Genet., 101, pp. 519-526Michaud, D., Avoiding proteinase-mediated resistance in herbivorous pests (1997) Trends Biotechnol., 15, pp. 4-6Mordue (luntz), A.J., Blackwell, A., Azadirachtin: An update (1993) J. Insect Physiol., 39, pp. 903-924Oliva, M.L.V., Silva, M.C.C., Sallai, R.C., Brito, M.V., Sampaio, M.U., A novel subclassification for Kunitz proteinase inhibitors from leguminous seeds (2010) Biochimie, 11, pp. 1667-1673Oliveira, A.S., Migliolo, L., Aquino, R.O., Ribeiro, J.K.C., MacEdo, L.L.P., Andrade, L.B.S., Bemquerer, M.P., Sales, M.P., Identification of a Kunitz-type proteinase inhibitor from Pithecellobium dumosum seeds with insecticidal properties and double activity (2007) J. Agric. Food Chem., 55, pp. 7342-7349Parde, V.D., Sharma, H.C., Kachole, M.S., In vivo inhibition of Helicoverpa armigera gut pro-proteinase activation by non-host plant proteinase inhibitors (2010) J. Insect Physiol., 56, pp. 1315-1324Parra, J.R.P., Criação de insetos para estudos com patógenos (1998) Controle Microbiano de Insetos, pp. 1015-1038. , S.B. Alves, FEALQ PiracicabaParra, J.R.P., Mihsfeldt, L.H., Comparison of artificial diets for rearing the sugarcane borer (1992) Adv. Insect Rearing Res. Pest Manag., pp. 195-209Pompermayer, P., Lopes, A.R., Terra, W.R., Parra, J.R.P., Falco, M.C., Silva-Filho, M.C., Effects of soybean proteinase inhibitor on development, survival and reproductive potential of the sugarcane borer, Diatraea saccharalis (2001) Entomol. Exp. Appl., 99, pp. 79-85Pompermayer, P., Falco, M.C., Parra, J.R.P., Silva-Filho, M.C., Coupling diet quality and Bowman-Birk and Kunitz-type soybean proteinase inhibitor effectiveness to Diatraea saccharalis development and mortality (2003) Entomol. Exp. Appl., 109, pp. 217-224Rayapuram, C., Baldwin, I.T., Using nutritional indices to study LOX3-dependent insect resistance (2006) Plant Cell Environ., 29, pp. 1585-1594Roy, S., Dutta, S.K., Genomic and cDNA cloning, expression, purification, and characterization of chymotrypsin-trypsin inhibitor from Winged Bean seeds (2009) Biosci. Biotechnol. Biochem., 73, pp. 2671-2676Ryan, C.A., Proteinase inhibitors in plants: Genes for improving defenses against insects and pathogens (1990) Annu. Rev. Phytopathol., 28, pp. 425-449Silva, W., Freire, M.G.M., Parra, J.R.P., Marangoni, S., MacEdo, M.L.R., Evaluation of the Adenanthera pavonina seed proteinase inhibitor (ApTI) as a bioinsecticidal tool with potential for the control of Diatraea saccharalis (2011) Process. Biochem., 47, pp. 257-263Song, S.I., Kim, C.H., Baek, S.J., Choi, Y.D., Nucleotide sequences of cDNAs encoding the precursors for soybean (Glycine max) trypsin inhibitors (Kunitz type) (1993) Plant Physiol., 101, pp. 1401-1402Telang, M., Srinivasan, A., Patankar, A., Harsulkar, A., Joshi, V., Damle, A., Deshpande, V., Gupta, V., Bitter gourd proteinase inhibitors: Potential growth inhibitors of Helicoverpa armigera and Spodoptera litura (2003) Phytochemistry, 63, pp. 643-652Telang, M.A., Giri, A.P., Pyati, P.S., Gupta, V.S., Tegeder, M., Franceschi, V.R., Winged bean chymotrypsin inhibitors retard growth of Helicoverpa armigera (2009) Gene, 431, pp. 80-85Waldbauer, G.P., The consumption and utilization of food by insects (1968) Adv. Insect Physiol., 5, pp. 229-288Yang, L., Fang, Z., Dicke, M., Van Loon, J.J.A., Jongsma, M.A., The diamondback moth, Plutella xylostella, specifically inactivates Mustard Trypsin Inhibitor 2 (MTI2) to overcome host plant defence (2009) Insect Biochem. Mol. Biol., 39, pp. 55-61Zhang, D., Yang, Y., Castlebury, L.A., Cerniglia, C.E., A method for the large scale isolation of high transformation efficiency fungal genomic DNA (1996) FEMS Microbiol. Lett., 145, pp. 216-26
    corecore