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Probing Morbillivirus Antisera Neutralization Using Functional Chimerism between Measles Virus and Canine Distemper Virus Envelope Glycoproteins.

Measles virus (MeV) is monotypic. Live virus challenge provoke extensive protective humoral immune response that neutralizes all known genotypes of measles. Both surface glycoproteins, H and F, mediates viral attachment and entry, respectively, and neutralizing antibodies to H is considered a major correlate of protection. 

Here, we make improvements to MeV system of reverse genetics and Rabbit Recombiant Proteins

 generated a panel MeVs recombinant where the head domain globular or region stems from H glycoproteins or whole protein F, or both, are replaced with the domain corresponding protein of canine distemper virus (CDV), morbillivirus closely linked that resists neutralization by measles-immune sera. Virus tested sensitivity to human or guinea pig anti-MeV neutralizing antiserum and anti-CDV to ferret antisera. 

Virus neutralization mediated by antibodies to both H and F protein, with H being immunodominant in the case MeV and F that is so in the case of CDV. In addition, the globular head domain of the MeV and CDV H protein immunodominant more regions of their stalks. These data shed more light on the factors that hinder the evolution of new morbillivirus serotypes.
Probing Morbillivirus Antisera Neutralization Using Functional Chimerism between Measles Virus and Canine Distemper Virus Envelope Glycoproteins.

Optimization and Diagnostic Evaluation Blocking monoclonal antibody-based ELISA format for the detection of Hendra Virus Neutralizing Antibodies in Sera mammals.


Maintenance Hendra virus (HEV) at pteropid bat populations have been associated with spillover events in horses, humans and dogs. Experimental studies have demonstrated the infection for several other species including guinea pigs, cats and ferrets. Criteria for sensitive and specific serologic tests are effective for a variety of species, but which does not require the use of a live virus, has not been satisfactorily addressed by currently available tests. 

We have evaluated the use of two HEV neutralizing monoclonal antibodies (mAbs) in a format block the enzyme-linked immunosorbent assay (Belisa) to detect serum antibodies Sheep Recombinant Protein against expressed HEV recombinant protein G (sol G) in several animal species. The human mAb neutralizes m102.4 both HEV and closely related Nipah virus (BIS); mouse mAb 1.2 neutralize HEV only. Given the functional differences, we have investigated both antibodies using Belisa format. 

diagnostic sensitivity (DSe) and diagnostic specificity (DSP) optimized use individual thresholds for mAb 1.2 and m102.4. Positive threshold for mAb 1.2> 33% inhibition DSe and DSP generates a value of 100% (95% CI 95.3 to 100.0) and 99.5 (95% CI 98.8 to 99.8) respectively; for mAb m102.4 positive threshold> 49% inhibition provides DSe and DSP value of 100 (95% CI 95.3 to 100.0) and 99.8 (95% CI 99.2 to 100.0) respectively.

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