Investigation of Compressive Properties of Wollastonite (CaSiO3) reinforced Acrylonitrile Butadiene Styrene composites

Volume 8 Issue 4 (April 201

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Not AvailableThe present study envisages expression of immunodominant ectodomain of peste des petits ruminants virus (PPRV) fusion (F) protein in Escherichia coli BL21 (DE3) and its characterization to assess its immunoreactivity. The ectodomain gene sequences corresponding to 222 amino acids, was amplified from PPR vaccine virus, cloned into pET33b vector and expressed in E. coli at an optimal temperature of 37 ◦C with 1 mM IPTG for 5 h. The expressed and Ni-NTA purified PPRV F protein (31 kDa) was characterized by SDS-PAGE and Western blot using anti-his-tagged-conjugate, anti-serum raised against recombinant PPRV F protein, hyper immune serum against whole PPRV and convalescent sera from sheep and goats. The expressed protein was assessed for its immunoreactivity by ELISA and immunoblotting. The antibody response mounted against the recombinant PPRV F protein in immunized rabbits was detected by recombinant PPRV F antigen based indirect ELISA, and whole virus antigen based indirect ELISA, which indicating the native confirmation ofthe expressed protein in E. coli. Indirect ELISA was optimized using known true positive and negative sera with respect to PPRV antibodies in order to assess the reactivity of the PPRV F protein in detecting PPRV F antibodies in small ruminants. The E. coli expressed recombinant ectodomain of PPRV F protein exhibits immunoreactivity and was able to specifically detect PPRV antibodies in response to both vaccination and disease in natural host.Not Availabl

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Not AvailableIn the present report, investigation of foot-and-mouth disease (FMD) outbreak in a commercial pig farm located in the outskirts of Bengaluru in February 2018 was carried out. Disease with high morbidity and severity was noticed in the pig herd consisting of 500 animals. Clinically, the animals showed marked dullness, off feeding and limping along with severe vesicular lesions and ulcers on snout and skin around the coronary bands of pigs. The outbreak was caused by FMDV type O as tested by sandwich ELISA of the samples collected from a dead piglet.Demonstration of high levels of antibodies to structural proteins specific to serotype O (as compared to two other serotypes) in the presence of high titres of non-structural antibodies in the randomly collected samples 2 weeks after the episode was suggestive of widespread infection on the farm in the absence of zoo-sanitary measures.Disease transmission in the vaccinated cattle was also evidenced as animals housed in close proximity developed the disease. Vaccination of pigs in addition to large animals is important to avoid transmission of the disease to other animals as pigs may serve as source of active infection as observed in the present outbreak.Not Availabl

Expression and characterization of immunodominant region of fusion protein of peste des petits ruminants virus in E. coli

The present study envisages expression of immunodominant ectodomain of peste des petits ruminants virus (PPRV) fusion (F) protein in Escherichia coli BL21 (DE3) and its characterization to assess its immunoreactivity. The ectodomain gene sequences corresponding to 222 amino acids, was amplified from PPR vaccine virus, cloned into pET33b vector and expressed in E. coli at an optimal temperature of 37 degrees C with 1 mM IPTG for 5 h. The expressed and Ni-NTA purified PPRV F protein (31 kDa) was characterized by SDS-PAGE and Western blot using anti-his-tagged-conjugate, anti-serum raised against recombinant PPRV F protein, hyper immune serum against whole PPRV and convalescent sera from sheep and goats. The expressed protein was assessed for its immunoreactivity by ELISA and immunoblotting. The antibody response mounted against the recombinant PPRV F protein in immunized rabbits was detected by recombinant PPRV F antigen based indirect ELISA, and whole virus antigen based indirect ELISA, which indicating the native confirmation of the expressed protein in E. coli. Indirect ELISA was optimized using known true positive and negative sera with respect to PPRV antibodies in order to assess the reactivity of the PPRV F protein in detecting PPRV F antibodies in small ruminants. The E. coli expressed recombinant ectodomain of PPRV F protein exhibits immunoreactivity and was able to specifically detect PPRV antibodies in response to both vaccination and disease in natural host. (C) 2016 Elsevier B.V. All rights reserved