Application of radioimmunologic techniques to studies of the epidemiologic involvement of bovine leukemia virus in lymphosarcoma of domestic cattle.
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Animals↗
Biomedical subjects
S G Devare
Publications and source records attributed to S G Devare.
Biochemical and immunological properties of gag genecoded structural proteins of endogenous tyep C RNA tumor viruses of diverse mammalian species.
The major nonglycosylated structure proteins of mammalian type C RNA tumor viruses are synthesized in the form of a high molecular weight precursor coded for by a viral gene disignated "gag". Previous genetic analysis of a prototype virus isolated of mouse origin has led to a determination of the internal arragnement of the regions within the gag gene coding for individual structural proteins. In the present study, the biochemical properties of structural proteins of type C virus isolates of additional mammalian species were analyzed. The results obtained indicate that the biochemical properties of immunologically cross-reactive proteins have been highly conserved throughout the evolution of this group of viruses. Moreover, these findings provide a means of mapping the gag genes of a broad range of mammalian type C viruses. In view of the results obtained, a new nomenclature system for type C viral gag gene-coded translational products is proposed.
Animals↗
Bovine leukemia virus specific antibodies among French cattle. II. Radioimmunoassay with the major structural protein (BLV p24).
A radioimmunoassay (RIA) for the major internal protein of the bovine leukemia virus (BLV p24) was established using anti-BLV p24 natural antibodies and purified 125I-labelled BLV p24. The final precipitation of the immune complexes was realized by a preparation of inactivated Staphylococcus aureau Cowan I. Sera from 363 cows belonging to (1) leukemic herds, (2) non-leukemic but BLV-exposed herds, and (3) apparently unexposed herds were studied comparatively in BLV p24 RIA, complement fixation and immunodiffusion. The BLV p24 RIA appeared much more senstive than the two other methods in the detection of positive sera. With this method 100% of the leukemic animals, excluding those with juvenile lymphosarcoma, presented very high antibody titers (greater than or equal to 10,000). Practically all cows with persistent lymphocytosis were also positive with slightly lower levels of antibodies, confirming the relationship between BLV infection and the persistent lymphycytosis. Moreover, about two-thirds of the hematologically suspect animals and one-third of the normal animals from BLV-exposed herds were found positive, whereas 100% of the sera from unexposed cows remained negative for anti-BLV p24 antibodies.
Animals↗
Simplified radioimmunoassay for viral antigens: use of Staphylococcus aureus as an adsorbent for antigen-antibody complexes.
In a rapid method for the radioimmunoassay (RIA) of viral antigens, Staphylococcus aureus was used as the adsorbent for antigen-antibody complexes ("protein A" molecules on the cell walls of certain strains of staphylococci have a strong affinity toward IgG molecules). The results showed that this method could be used instead of the double-antibody technique, with the same or probably higher sensitivity in precipitation as well as competition RIA's.
Adsorption↗
Biochemical and immunological characterization of the major envelope glycoprotein of bovine leukemia virus.
The major envelope glycoprotein of bovine leukemia virus was isolated by lectin-bound Sepharose and DEAE-cellulose column chromatography. This protein was shown to have a molecular weight of about 41,000 and to lack detectable immunological cross-reactivity with glycoproteins of other oncornaviruses. Sera obtained from 100% of cattle examined with clinically diagnosed lymphosarcoma contained high-titered antibody to 125I-labeled bovine leukemia virus glycoprotein, whereas sera from animals in a disease-free herd were antibody negative.
Animals↗
Evaluation of radioimmunoprecipitation for the detection of bovine leukemia virus infection in domestic cattle.
The potential application of a recently developed radioimmunoprecipitation test for antibody directed against the major structural protein of bovine leukemia virus was evaluated for use in detection of BLV-infection in domestic cattle. This technique was found to be considerably more sensitive than serologic procedures currently being utilized for this purpose. Radioimmunoprecipitation was also shown to have distinct advantages as compared to hematologic criteria, such as specified by Bendixen's index, for identification of BLV-infected animals. By the use of radioimmunoprecipitation, high levels of antibody to BLV were demonstrated in sera of animals with confirmed adult lymphosarcoma, but not in animals with a less common sporadic form of the disease which occurs in calves.
Aging↗
Bovine lymphosarcoma: development of a radioimmunologic technique for detection of the etiologic agent.
A highly sensitive and specific radioimmunoassay has been developed for the major structural protein of an oncornavirus etiologically associated with bovine lymphosarcoma. This test can be used to identify cattle which have been exposed to the bovine leukemia virus and may thus develop or transmit the disease. Analysis of randomly obtained serums indicates that infection that infection with this virus is widespread among cattle.
Animals↗
Differential synthesis of proteins by T4 phage & its head protein amber mutant.
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Coliphages↗
Differential synthesis of proteins by T4 phage and its head protein amber mutant.
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Coliphages↗
Synthesis of the late proteins of bacteriophage T 4 amber mutant.
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Amino Acids↗
Structural and immunological similarities between simian sarcoma virus gene product(s) and human platelet-derived growth factor.
The predicted amino acid sequence of the simian sarcoma virus (SSV) transforming gene product, p28sis, closely corresponds to that of human platelet-derived growth factor (PDGF). We demonstrate that p28sis rapidly undergoes a series of discrete processing steps including dimer formation and proteolytic digestion to yield molecules structurally and immunologically resembling biologically active PDGF.
Amino Acid Sequence↗