6 research outputs found

    Leishmania major-phlebotomus duboscqi interactions: inhibition of anti-LPG antibodies and characterisation of two proteins with shared epitopes

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    Objectives: To assess the effect of monoclonal antibodies (MABS) raised against L. major derived LPG on L. major development in vitro and in its natural vector P. duboscqi. Also determine whether LPG molecule and the sand fly the gut Iysates have sharedepitopes. Design: A laboratory based study. Setting: Colony bred P. duboscqi sand flies and all other experiments were done under laboratory conditions. Methods: Laboratory reared sand flies were allowed to feed beneath a blood filled membrane feeder containing 1 x106 amastigotes in 20µl mixed with 0.5 ml of defibrinated rabbit blood with a 1:100 dilution of anti-LPG MABS. Control blood contained a similar number of amastigotes but no MABS. At least five female previously fed sand flies were later dissected on days two, four, and six post-feeding and examined for promastigote forms and parasite loads in the sand fly mid gut. In vitro, the same number of amastigotes in 100µl complete Schneider's Drosophila medium was mixed in a 96 well plate with either 100µl of 1: 100 anti-LPG MABS, 1:1000 anti LPG MABS or undiluted sera from L. major infected mice. The control well contained a similar number of amastigotes but no antibodies added. Following an overnight incubation in a CO2 incubator at 37ºC and growth at 26ºC, parasites were assessed at 3, 6 and 24 hour intervals for changes in their developmental forms. Results: 1:100 dilution of anti-LPG MABS when mixed with amastigotes were effective in reducing L. major development at the early log phase or procyclic stage both in vitro and within the sand fly (

    An alpha-Gal-containing neoglycoprotein-based vaccine partially protects against murine cutaneous leishmaniasis caused by Leishmania major

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    Submitted by Sandra Infurna ([email protected]) on 2018-02-08T14:28:28Z No. of bitstreams: 1 otacilio_moreira_etal_IOC_2017.pdf: 4048766 bytes, checksum: 739bd60ac93001eb3f167318d867f73c (MD5)Approved for entry into archive by Sandra Infurna ([email protected]) on 2018-02-08T14:43:56Z (GMT) No. of bitstreams: 1 otacilio_moreira_etal_IOC_2017.pdf: 4048766 bytes, checksum: 739bd60ac93001eb3f167318d867f73c (MD5)Made available in DSpace on 2018-02-08T14:43:57Z (GMT). No. of bitstreams: 1 otacilio_moreira_etal_IOC_2017.pdf: 4048766 bytes, checksum: 739bd60ac93001eb3f167318d867f73c (MD5) Previous issue date: 2017University of Texas at El Paso. Department of Biological Sciences. Border Biomedical Research Center. El Paso, Texas, USA.University of Texas at El Paso. Department of Chemistry. Border Biomedical Research Center. El Paso, Texas, USA.Liverpool School of Tropical Medicine. Department of Parasitology. Pembroke Place, Liverpool, United Kingdom.University of Texas at El Paso. Department of Biological Sciences. Border Biomedical Research Center. El Paso, Texas, USA.University of Texas at El Paso. Department of Chemistry. Border Biomedical Research Center. El Paso, Texas, USA.Liverpool School of Tropical Medicine. Department of Parasitology. Pembroke Place, Liverpool, United Kingdom.University of Texas at El Paso. Department of Biological Sciences. Border Biomedical Research Center. El Paso, Texas, USA.University of Texas at El Paso. Department of Biological Sciences. Border Biomedical Research Center. El Paso, Texas, USA.Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Molecular e Doenças Endêmicas. Rio de Janeiro, RJ. Brasil.Liverpool School of Tropical Medicine. Department of Parasitology. Pembroke Place, Liverpool, United Kingdom / Liverpool School of Tropical Medicine. Department of Vector Biology. Pembroke Place, Liverpool, United Kingdom.University of Texas at El Paso. Department of Chemistry. Border Biomedical Research Center. El Paso, Texas, USA.University of Texas at El Paso. Department of Biological Sciences. Border Biomedical Research Center. El Paso, Texas, USA.University of Texas at El Paso. Department of Biological Sciences. Border Biomedical Research Center. El Paso, Texas, USA.Protozoan parasites from the genus Leishmania cause broad clinical manifestations known as leishmaniases, which affect millions of people worldwide. Cutaneous leishmaniasis (CL), caused by L. major, is one the most common forms of the disease in the Old World. There is no preventive or therapeutic human vaccine available for L. major CL, and existing drug treatments are expensive, have toxic side effects, and resistant parasite strains have been reported. Hence, further therapeutic interventions against the disease are necessary. Terminal, non-reducing, and linear α-galactopyranosyl (α-Gal) epitopes are abundantly found on the plasma membrane glycolipids of L. major known as glycoinositolphospholipids. The absence of these α-Gal epitopes in human cells makes these glycans highly immunogenic and thus potential targets for vaccine development against CL

    Carbohydrate vaccines: developing sweet solutions to sticky situations?

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