Search Results
immunogenicities of PRRSV vaccines were enhanced by using recombinant porcine IFN-γ (poIFN-γ) and porcine GM-CSF (poGM-CSF). In this study, a recombinant fusion protein incorporating both of these cytokines was generated (poIFN-γ-linker-poGM-CSF) and expressed
Objective
To determine whether animals had serologic evidence of infection with Sin Nombre virus (SNV).
Design
Prospective serosurvey.
Sample Population
Serum samples were obtained from 145 cats, 85 dogs, 120 horses, and 24 cattle between April 1993 and August 1994 and 54 coyotes between December 1994 and February 1995.
Procedure
Serum samples were analyzed by western immunoblot assays for reaction with SNV nucleocapsid antigen. Samples with reactivity to SNV nucleocapsid proteins were used to probe multiple-antigen blots containing recombinant fusion proteins derived from prototypic hantaviruses. Lung tissue or blood clots were used in nested reverse-transcriptase polymerase chain reaction assays for a 320-nucleotide portion of the SNV G1 gene.
Results
Sera from 4 of 145 (2.8%) cats and 4 of 85 (3.5%) dogs had trace reactivity to full-length SNV-encoded nucleocapsid proteins. All samples from horses, cattle, and coyotes were nonreactive. Sera from cats and dogs that had trace IgG-antibody reactivity to nucleocapsid proteins were then tested for IgG-antibody reactivity to nucleocapsid proteins of prototypic hantaviruses. One cat had multiple cross-reactivities with these hantaviruses, consistent with exposure to a hantavirus; however, epitope mapping studies did not support this conclusion. Reverse-transcriptase polymerase chain reaction studies of blood clots or lung tissue from 2 animals that had weak reactivity to SNV failed to amplify any hantavirus sequence.
Clinical Implications
Domestic animals, particularly dogs and cats, as well as coyotes do not appear to have a major role in the maintenance and transmission of SNV. (J Am Vet Med Assoc 1998;212:970–973)
assay that uses a recombinant fusion protein for capture of the 1,25(OH) 2 D molecule and a murine monoclonal antibody that specifically recognizes the complex formed by the recombinant fusion protein with the 1,25(OH) 2 D molecule. The solid phase
, 9.6). Plates were washed twice with PBST, and alternate rows were incubated with 100 μL of recombinant fusion protein GSH-p24 ([6 μg/mL]/well; GSH fused to BLVp24) diluted in protein diluent (PBS solution, 10% tryptose, f 1% Tween 20, and 0
