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Title: CONSTRUCTION OF HYBRIDOMAS WHICH SECRETE MONOCLONAL ANTIBODIES SPECIFIC FORANTIGENS OF THE SHEEP SCAB MITE, PSOROPTES OVIS

Author
item Temeyer, Kevin
item Pruett Jr, John

Submitted to: Veterinary Parasitology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 10/20/1998
Publication Date: N/A
Citation: N/A

Interpretive Summary: Thirty novel cell lines were constructed which secrete chemically pure antibodies in cell cultures. These antibodies recognize and bind to specific proteins produced by the sheep scab mite. Sheep scab mites are parasites of cattle and sheep which cause economic damage and can potentially lead to death of infested animals. Antibodies produced by the new cell lines can be used to determine which and how much of specific mit proteins are present at various stages of mite growth and development, or to compare the structural relatedness of these mite proteins (or allergens) with other proteins (or allergens) from which these or other mites, and to concentrate and purify these proteins for vaccine preparation or other uses. These new cell lines and their antibodies are useful tools to help us understand where and how these mite proteins (or allergens) are produced and how they are related to one another. The antibodies could also be used dto develop a monitoring method to test for the presence of specific mite proteins in environmental samples. Development of these antibodies and other tools will help us to better understand mite biology and may potentially provide information to help develop novel methods for control of psoroptic scabies of cattle, sheep or other animals.

Technical Abstract: Thirty murine hybidomas were constructed that secrete monoclonal antibodies (mAbs) specific for protein antigens of Psoroptes ovis (Hering). The panel of mAbs produced by the hybridoma cultures appeared to bind 19 different epitopes as represented by binding patterns against crude P. ovis extract, and two partially purified fractions. The complete panel of monoclonal antibodies appeared to bind a similar array of P. ovis proteins as did serum from an immunized mouse. Two of the mAbs appear to bind to the 16 kDa protein previously identified as a potential immunogen. The monoclonal antibodies are available to aid further immunochemical research studies of mite antigens.