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Six M guanidinium chloride is able to unfold BTV VP7 while 8 M urea could not.

Twenty percent glycerol and 300 mM sodium chloride appear to have a protective effect on BTV VP7's structure, as significantly more structure is seen at 90℃ when compared to BTV VP7 without the addition of these chemicals. Both glycerol and sodium chloride are common vaccine additives.

Twenty percent glycerol and 300 mM sodium chloride appear to have a protective effect on BTV VP7's structure, as significantly more structure is seen at 90℃ when compared to BTV VP7 without the addition of these chemicals. Both glycerol and sodium chloride are common vaccine additives.

Japanese encephalitis is one of the most important mosquito-borne and zoonotic diseases in Asia and the Pacific region. Although the dominant Japanese encephalitis virus (JEV) genotype has shifted from G3 to G1 in Korea since 1990, a G3 strain (Anyang 300) has been used in vaccines for horses for almost 40 years. This study aimed to investigate the seroconversion rates and geometric mean titers (GMTs) of virus-neutralizing antibodies (VNAs) against JEV G1 and G3 in horses immunized with the G3 vaccine.

Serum samples of 1,231 horses immunized with the Anyang 300 vaccine were collected in 2018. VNA titers against JEV KV1899 (G1) and Anyang 300 (G3) were measured in all serum samples using the virus neutralization test. read more Titers were analyzed according to blood sampling time (prior to and following annual revaccination), age, and region.

Rates of VNA titer >10 were 45.1% and 77.8% for G1, and 49.1% and 82.9% for G3 in samples taken before and after revaccination, respectively. GMTs of genotype-specific VNAs against JEV G1 and G3 were 8.3 and 11.6 before revaccination and rose to 27.2 and 65.4 following revaccination. Overall sero-positivity did not significantly differ between genotypes, but GMTs significantly differed among genotypes and sampling times. No significant difference was found in GMTs among age groups or regions.

Genotype-specific neutralizing antibody titers against JEV G1 and G3 differed significantly in horses immunized with the G3 vaccine. Antigenic differences between genotypes could reduce the vaccine's efficacy, requiring the development of a new vaccine.

Genotype-specific neutralizing antibody titers against JEV G1 and G3 differed significantly in horses immunized with the G3 vaccine. Antigenic differences between genotypes could reduce the vaccine's efficacy, requiring the development of a new vaccine.

The success of foot-and-mouth disease (FMD) serological serosurveillance greatly depends on the FMD vaccine which does not include any non-structural proteins (NSPs) of the FMD virus. Since pure FMD vaccines from NSPs are used with the FMD eradication programs using DIVA (Differentiating Infected from Vaccinated Animals) tests. Apart from the

test defined in the World Organisation for Animal Health, two different test kits were developed in-process NSP detection purposes. The first test kit was developed in 2010 and the second one has been very recently developed in 2019.

In this study, the level of NSP has been examined by first-chemiluminescent filtration assisted (FAL)-enzyme-linked immunosorbent assay (ELISA) based

, in-process test kit for Turkey FMD vaccine antigen samples. A total of 94 samples were used. The critical maximum acceptable levels of NSP were determined after purification stage of samples.

As a maximum NSP level, 70 ng NSP for the polyethylene glycol concentrated samples and 30 ng NSP for the vaccine antigen mixture samples were accepted. A mini repeatability study was also performed. The correlation between the NSP, total protein, and 146S particul quantity of samples were analyzed.

As a conclusion, the chemiluminescent FAL-ELISA based test kit can be used for the NSP purity level determination of in-process samples.

As a conclusion, the chemiluminescent FAL-ELISA based test kit can be used for the NSP purity level determination of in-process samples.

is an opportunistic parasite infecting all warm-blooded animals including humans. The dense granule antigens (GRAs) play an important role in parasite survival and virulence and in forming the parasitophorous vacuole. Identification of protein characteristics increases our knowledge about them and leads to develop the vaccine and diagnostic studies.

This paper gave a comprehensive definition of the important aspects of GRA12 protein, including physico-chemical features, a transmembrane domain, subcellular position, secondary and tertiary structure, potential epitopes of B-cells and T-cells, and other important features of this protein using different and reliable bioinformatics methods to determine potential epitopes for designing of a high-efficient vaccine.

The findings showed that GRA12 protein had 53 potential post-translational modification sites. Also, only one transmembrane domain was recognized for this protein. The secondary structure of GRA12 protein comprises 35.55% alpha-helix, 19.50% extended strand, and 44.95% random coil. Moreover, several potential B- and T-cell epitopes were identified for GRA12. Based on the results of the Ramachandran plot, 79.26% of amino acid residues were located in favored, 11.85% in allowed and 8.89% in outlier regions. Furthermore, the results of the antigenicity and allergenicity assessment noted that GRA12 is immunogenic and non-allergenic.

This research provided important basic and conceptual data on GRA12 to develop an effective vaccine against acute and chronic toxoplasmosis for further

investigations. More studies are required on vaccine development using the GRA12 alone or combined with other antigens in the future.

This research provided important basic and conceptual data on GRA12 to develop an effective vaccine against acute and chronic toxoplasmosis for further in vivo investigations. More studies are required on vaccine development using the GRA12 alone or combined with other antigens in the future.

N-acetylmuramoyl-l-alanine amidase known as lytA, is an immunogenic protein that plays an important role in the pathogenesis of

. It is highly conserved among

strains and is absent among other

species. In the present study, the level of antibodies against the lytA recombinant protein was evaluated in healthy individuals' sera.

DNA was extracted from

ATCC 49619 to amplify

A gene by polymerase chain reaction assay. The lytA amplicon and

ET28a vector were separately double digested using

-1 and

1 restriction enzymes and then ligated together with ligase enzyme. The recombinant plasmid was expressed in

BL21 strain and the lytA recombinant protein purified using nickel-nitrilotriacetic acid affinity chromatography. Western blot was carried to detect lytA recombinant protein. Sixty healthy individual's sera (at three age groups group 1, <2; group 2, 2-40; and group 3, 60-90 years old) were collected and the titers of anti-lytA antibodies were determined.

The

A gene was highly expressed in

BL21 host.