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Immunology in Weed Science

Published online by Cambridge University Press:  12 June 2017

Timothy D. Sherman and
Kevin C. Vaughn
Timothy D. Sherman
Affiliation:
U.S. Dep. Agric., Agric. Res. Serv., South. Weed Sci. Lab., P.O. Box 350, Stoneville, MS 38776
Kevin C. Vaughn
Affiliation:
U.S. Dep. Agric., Agric. Res. Serv., South. Weed Sci. Lab., P.O. Box 350, Stoneville, MS 38776
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Abstract

Many problems in weed science may be solved by utilizing immunochemical techniques, although these techniques are currently underutilized by weed scientists. In this review, we describe some of the methods of greatest use to weed scientists. Antibodies may be raised against proteins, such as the targets of herbicide action or against the herbicide itself which can be linked to a larger molecule so that antibodies are elicited. Once specific antibodies are obtained, several techniques may be performed utilizing the binding phenomena of antibody-antigen interactions. Immunofluorescence and immunogold electron microscopy are utilized to obtain tissue and subcellular distributions of the protein or herbicide of interest. Quantitation of either protein or herbicide in a given sample may be performed by ELISA or “slot” and “dot” blotting. These protocols are less costly, more sensitive, and much less labor-intensive than most analytical methods. Molecular mass or charge alterations may be determined by electrophoresis and subsequent immunoblotting. With the increased exposure to immunological techniques by weed scientists and their potential utility, we predict that many more weed science problems will be addressed using these protocols.

Keywords

Herbicideimmunoblottingimmunogoldimmunocytochemistry

Information

Type
Special Topics
Information
Weed Science , Volume 39 , Issue 3 , September 1991, pp. 514 - 520
Copyright
Copyright © 1991 by the Weed Science Society of America 

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References

Literature Cited

1. Clarke, A. E., Knox, R. B., and Jermyn, M. A. 1975. Localization of lectins in legume cotyledons. J. Cell Sci. 19:157–167.CrossRefGoogle ScholarPubMed
2. Hall, J. C., Deschamps, R.J.A., and McDermott, M. R. 1990. Immunoassays to detect and quantitate herbicides in the environment. Weed Technol. 4:226–234.Google Scholar
3. Huber, S. J. and Sautter, C. 1986. Immunofluorescence localization of conjugated atrazine in leaf pieces of corn (Zea mays). J. Plant Dis. and Prot. 93:608–613.Google Scholar
4. Huse, W. D., Sastry, L., Iverson, S. A., Kang, A. S., Alting-Mees, M., Burton, D. R., Benkovic, S. J., and Lerner, R. A. 1989. Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda. Science 246:1275–1281.CrossRefGoogle ScholarPubMed
5. Knox, R. B., Heslop-Harrison, J., and Reed, C. E. 1970. Immunolocalization of antigen associated with the pollen grain wall by immunofluorescence. Nature 229:1066–1068.Google Scholar
6. Knox, R. B., Vithanage, H.I.M.V., and Howlett, B. J. 1980. Botanical immunocytochemistry: a review with special reference to pollen antigens and allergens. Histochem. J. 12:247–272.Google Scholar
7. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.Google Scholar
8. Laine, A.-C. and Faye, L. 1988. Significant immunological cross-reactivity of plant glycoproteins. Electrophoresis 9:844–845.CrossRefGoogle ScholarPubMed
9. Lehnen, L. P. Jr., Vaughan, M. A., and Vaughn, K. C. 1990. Terbutol affects spindle microtubule organizing centres. J. Exp. Bot. 41:537–546.CrossRefGoogle Scholar
10. Lehnen, L. P. Jr. and Vaughn, K. C. 1991. Immunofluorescence and electron microscopic investigations of the effects of dithiopyr on onion root tips. Pestic. Biochem. Physiol. 40:58–67.CrossRefGoogle Scholar
11. Lehnen, L. P. Jr. and Vaughn, K. C. 1991. Immunofluorescence and electron microscopic of DCPA-treated oat roots. Pestic. Biochem. Physiol. 40:47–57.Google Scholar
12. Linskens, H. F. and Jackson, J. F., eds. 1986. Immunology in Plant Sciences. Springer-Verlag, Berlin. 263 pp.Google Scholar
13. Ouchterlony, Ö. 1968. Pages 33–48 in Handbook of immunodiffusion and Immunoelectrophoresis. Ann Arbor Science Publisher, Inc., Ann Arbor, MI.Google Scholar
14. Robins, R. J. 1986. The measurement of low-molecular-weight, non-immunogenic compounds by immunoassay. Pages 86–141 in Linskens, H. F. and Jackson, J. F., eds. Immunology in Plant Sciences. Springer-Verlag, Berlin.Google Scholar
15. Sherman, T. D. and Funkhouser, E. A. 1989. Induction and synthesis of nitrate reductase in Chlorella vulgaris . Arch. Biochem. Biophys. 274:525–531.Google Scholar
16. Stegink, S. J. and Vaughn, K. C. 1990. Immunotaxonomy of nodule-specific proteins. Cytobios 61:7–19.Google Scholar
17. Stegink, S. J., Vaughn, K. C., and Verma, D. P. 1987. Antigenic similarity in urate oxidases of major ureide producing legumes and its correlation with the type of peroxisome in uninfected cells of nodules. Plant Cell Physiol. 28:387–396.Google Scholar
18. Towbin, H., Staehelin, T., and Gordon, J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76:4350–4354.CrossRefGoogle ScholarPubMed
19. Vaughan, M. A. and Vaughn, K. C. 1987. Pronamide disrupts mitosis in a unique manner. Pestic. Biochem. Physiol. 28:182–193.CrossRefGoogle Scholar
20. Vaughn, K. C. 1986. Characterization of triazine-resistant and -susceptible isolines of canola (Brassica napus L.). Plant Physiol. 82:859–863.Google Scholar
21. Vaughn, K. C. 1987. Two immunological approaches to the detection of ribulose-1,5-bisphosphate carboxylase in guard cell chloroplasts. Plant Physiol. 84:188–196.Google Scholar
22. Vaughn, K. C. 1989. Subperoxisomal localization of glycolate oxidase. Histochemistry 91:99–105.Google Scholar
23. Wang, M. 1990. Anti-idiotypes used in immunohistochemistry. Histochem. J. 22:519–525.CrossRefGoogle ScholarPubMed
24. Wang, T. L. 1986. Immunology in Plant Science. Cambridge University Press, Cambridge. 228 pp.Google Scholar
25. Wick, S. M., Seagull, R. W., Osborn, M., Weber, K., and Gunning, B.E.S. 1981. Immunofluorescence microscopy of organized microtubule arrays in structurally stabilized meristematic plant cells. J. Cell Biol. 89:605–609.CrossRefGoogle ScholarPubMed