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and emotional burden for pet guardians and families. In response to the need for improved targeted CPV-2 treatment, a monoclonal antibody product was developed. This product, known as canine parvovirus monoclonal antibody (CPMA), is a chimera made up

Open access
in Journal of the American Veterinary Medical Association

/dL) was present on serum biochemical analysis, with the remainder of the results within respective reference ranges. The hyperglobulinemia was further evaluated by SPEP, b which revealed monoclonal gammopathy with a pronounced narrow peak in the γ region

Full access
in Journal of the American Veterinary Medical Association

evidence of a monoclonal gammopathy was described. Findings on IFE a,b of sera revealed a single, distinct band within the IgA lane, which was interpreted as evidence of a neoplastic serum M protein. The presence of the M-protein was determined by use of

Full access
in Journal of the American Veterinary Medical Association

SUMMARY

Spleen cells from a calf immunized with bovine herpesvirus-1 (BHV-1) were fused with the nonsecreting murine cell line SP2/0. Several bovine-murine hybridomas secreting bovine immunoglobulins were stabilized. Of these, 9 hybridomas secreted bovine monoclonal antibodies that specifically bound to BHV-1 in a radioimmunoassay. Two of these monoclonal antibodies reacted specifically with BHV-1 in an indirect fluorescent antibody test and immunoprecipitated a BHV-1 glycoprotein with molecular mass of 97 kilodaltons.

Free access
in American Journal of Veterinary Research

Summary

A murine IgM monoclonal antibody, which recognizes dog erythrocyte antigen (dea) 1.1, has been produced. The antibody correctly identified canine rbc possessing dea 1.1 in a panel of rbc typed by an independent laboratory. Reactivity of the monoclonal antibody was compared with canine anti-dea 1.1 antiserum with 163 rbc samples from 145 dogs. Results of agglutination tests with the 2 reagents were in agreement for all samples. A card agglutination test that uses the monoclonal antibody with blood is described. A monoclonal antibody-based test should facilitate blood typing for dea 1.1 in clinical practice.

Free access
in Journal of the American Veterinary Medical Association

administration. These results suggested improvements in scores were attributable to the anti-NGF mAb. Monoclonal antibody treatments have several purported advantages, compared with conventional chemical drug treatments, including good safety, high specificity

Full access
in American Journal of Veterinary Research

SUMMARY

Two monoclonal antibodies against Actinobacillus pleuropneumoniae serotype 5, designated as 5MAb-l and 5MAb-6, were characterized. Enzyme-linked immunosorbent assay-inhibition tests with whole-cell antigens obtained from strains of serotype 1 through 12 of A pleuropneumoniae revealed that 5 MAb-1 bound to only serotype-5 strains. The epitope recognized by 5MAb-l was a carbohydrate that was sensitive to periodate oxidation and resided on the structure of β-l,6-linked d-galactose in an O-antigen polysaccharide of serotype-5 lipopolysaccharide. Analysis of these results revealted that the O-antigen polysaccharide of lipopolysaccharide was 1 of the antigenic determinants responsible for the serotype specificity of A pleuropneumoniae. On the other hand, 5MAb-6 reacted with strains of serotype 1 through 10 in varying degrees and its epitope was located on polypeptides sensitive to proteinase K. In an immunoblotting analysis, 5MAb-6 reacted with 2 polypeptide bands, with molecular weights of approximately 41,500 and 28,000, in the outer membrane protein-rich fraction obtained from strains of serotype 1 through 10. These results indicated that outer membrane proteins from several serotype strains of A pleuropneumoniae possessed common antigenic determinants.

Free access
in American Journal of Veterinary Research

SUMMARY

Bovine immunoglobulin isotype-specific murine monoclonal antibodies were used in sandwich radioimmunoassays to detect and quantitate bovine IgG1, IgG2, IgM, and IgA in culture fluids. The concentrations of bovine immunoglobulins in unknown samples were extrapolated from standard curves generated with bovine monoclonal immunoglobulins. The lowest detection limits for the bovine immunoglobulin isotypes ranged from 65 to 270 ng/ml.

Free access
in American Journal of Veterinary Research

Summary

The main objective of the study reported here was to generate a panel of monoclonal antibodies (mab) to bovine neutrophil surface antigens, and to identify mab that modulate neutrophil chemotaxis, respiratory burst, and phagocytosis. A further objective was to study mab reactivity with resting and activated neutrophils, to identify activation antigens and adhesion molecules.

A panel of 14 mab was generated by producing murine hybridomas. Neutrophils incubated with mab at 4 C for 2 hours were used in chemotaxis, respiratory burst, and phagocytosis assays. Chemotaxis was evaluated in Boyden chambers, using Escherichia coli endotoxin-activated fetal bovine serum as the chemoattractant. Respiratory burst was determined by measuring chemoluminescence of neutrophils incubated with 5-amino-2,3-dihydro-l,4-phthalazinedione, and serum opsonized zymosan. Phagocytosis was determined by flow cytometry, using fluorescein-labeled Staphylococcus aureus. The mab S7G8, S5F8G10, S7E10, and S5F8B8 enhanced chemotaxis (to > 125% of control). The mab S7E10 and S8D9 enhanced respiratory burst activity (to > 125% of control), whereas mab S2G8, S4G10, S8G10, and S5F8B8 caused inhibition (to < 75% of control). The mab S2G8, S4G10, S8G10, and S5F8G10 enhanced phagocytosis (to > 125% of control). Chemotaxis, respiratory burst, and phagocytosis values of neutrophils not bound with mab served as controls for comparison.

The mab binding for nonactivated neutrophils (at 4 C) ranged from 9 to 100%, and for activated neutrophils (at 37 C; at 37 C with phorbol myristate acetate) from 90 to 100%. Binding of mab S4F5, S5F8B8, S6C6, S7E10, S8D9, and S5F8G10 increased when neutrophils had been incubated at 37 C. Binding of these mab was further increased after incubation with phorbol myristate acetate (100 ng/ml) at 37 C, indicating recognition of activation antigens by mab. The mab generated in this study appeared to be potential candidates for studying mechanisms of neutrophil function and for enhancing neutrophil function in vitro and in vivo.

Free access
in American Journal of Veterinary Research

Summary

A panel of monoclonal antibodies (MAb) developed against Mycoplasma gallisepticum strain PG31 was used to probe the antigenic profiles of 5 recognized strains (PG31, R, S6, F, A5969) and 6 field isolates of M gallisepticum. Monoclonal antibody G9 predominantly recognized antigens at apparent molecular mass positions of 90 to 98 kDA. The MAb reacted with all strains and isolates, but the molecular mass position of the antigens varied among some mycoplasmas. Monoclonal antibody G12 reacted with all strains and isolates of M gallisepticum and had an identical banding pattern. However, MAb G10 and G11 reacted selectively only with a limited number of strains and/or isolates. Surface distribution of the MAb-recognized antigens was revealed by immunoelectron microscopy.

Partial physicochemical characterization of MAb G9-recognized antigens identified glycopeptide characteristics. Monoclonal antibody G9 reacted with surface antigens and, hence, participated in agglutination of M gallisepticum. However, the degree of agglutination varied among the various strains and isolates, indicating a quantitative or conformational limitation or an alteration in the anomeric expression of the epitopes. Antigenic variation in M gallisepticum may be mediated by immunologic selective pressures, or a proclivity for habit niche in the host.

Free access
in American Journal of Veterinary Research