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1.
Appl Biochem Biotechnol ; 188(2): 491-497, 2019 Jun.
Article in English | MEDLINE | ID: mdl-30536031

ABSTRACT

Antibodies against foot-and-mouth disease virus serotypes A, O and Asia-1 were detected by ELISA in liquid and strip-dried samples from vaccinated bovines. The results showed high concordance of the results in both types of serum samples (coefficient of correlation varied from 0.89 to 0.96). Stability studies showed that anti-foot-and-mouth disease virus antibodies can be detected in strip-dried serum samples stored at different temperatures on a level of that in native samples. Preliminary study in strip-dried whole blood samples demonstrated good potential of this sample pretreatment procedure for the following anti-foot-and-mouth virus antibodies testing.


Subject(s)
Antibodies, Viral/blood , Dried Blood Spot Testing/veterinary , Foot-and-Mouth Disease Virus/classification , Foot-and-Mouth Disease Virus/immunology , Animals , Biotechnology , Cattle , Cattle Diseases/immunology , Cattle Diseases/prevention & control , Dried Blood Spot Testing/methods , Enzyme-Linked Immunosorbent Assay , Foot-and-Mouth Disease/immunology , Foot-and-Mouth Disease/prevention & control , Serogroup , Vaccination/veterinary
2.
Biochim Biophys Acta ; 1808(10): 2374-89, 2011 Oct.
Article in English | MEDLINE | ID: mdl-21756874

ABSTRACT

The interaction of the extra-membranous domain of tetrameric inwardly rectifying Kir2.1 ion channels (Kir2.1NC(4)) with the membrane associated guanylate kinase protein PSD-95 has been studied using Transmission Electron Microscopy in negative stain. Three types of complexes were observed in electron micrographs corresponding to a 1:1 complex, a large self-enclosed tetrad complex and extended chains of linked channel domains. Using models derived from small angle X-ray scattering experiments in which high resolution structures from X-ray crystallographic and Nuclear Magnetic Resonance studies are positioned, the envelopes from single particle analysis can be resolved as a Kir2.1NC(4):PSD-95 complex and a tetrad of this unit (Kir2.1NC(4):PSD-95)(4). The tetrad complex shows the close association of the Kir2.1 cytoplasmic domains and the influence of PSD-95 mediated self-assembly on the clustering of these channels.


Subject(s)
Cytoplasm/metabolism , Intracellular Signaling Peptides and Proteins/metabolism , Membrane Proteins/metabolism , Potassium Channels, Inwardly Rectifying/metabolism , Disks Large Homolog 4 Protein , Humans , Intracellular Signaling Peptides and Proteins/chemistry , Membrane Proteins/chemistry , Microscopy, Electron, Transmission , Models, Molecular , Nuclear Magnetic Resonance, Biomolecular , Potassium Channels, Inwardly Rectifying/chemistry , Protein Binding , Reproducibility of Results , Scattering, Radiation
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