caa a22 4500 469042591 CHVBK 20180323132815.0 cr unu---uuuuu 170328e19920301xx s 000 0 eng 10.1007/BF01996321 doi (NATIONALLICENCE)springer-10.1007/BF01996321 Specificity of polycllonal and monoclonal antibodies for the identification of Xanthomonas campestris pv. campestris [Elektronische Daten] [A. Franken, J. Zilverentant, P. Boonekamp, A. Schots] Polyclonal and monoclonal antibodies (PCAs and MCAs), produced to whole cells and flagellar extracts ofXanthomonas campestris pv.campestris (Xcc), respectively, were tested for specificity. In immunofluorescence microscopy (IF) the three PCAs tested, reacted at low dilutions with all Xcc strains, some other xanthomonads and non-xanthomonads. At higher dilutions most cross-reactivity with non-xanthomonad strains disappeared. However, the cross-reactivity with strains ofX. c. pv.vesicatoria (Xcv),X. c. pv.amoraciae (Xca) andX. c. pv.phaseoli var. fuscans (Xcpf) remained. Six MCA-producing cell clones viz. 20H6, 2F4, 18G12, 10C5, 17C12 and 16B5 were selected for specificity tests with an enzyme immunoassay (EIA), IF and a dot-blot immunoassay (DBI). None of the MCAs reacted with all Xcc strains in IF and EIA. In DBI, only MCAs 17C12 and 16B5 reacted with all Xcc strains. All six MCAs tested, cross-reacted in one of either tests with other pathovars ofX. campestris, such as Xcv or Xca. The MCAs were also tested in immunoblotting experiments using total bacterial extracts, cell envelope and flagellar extracts. MCAs 20H6, 2F4, 18G12 and 10C5 reacted with the lipopolysaccharide (LPS) of Xcc. MCAs 16B5 and 17C12 reacted with a 39 kilodalton and a 29 kilodalton protein, respectively. It is concluded that the PCAs and MCAs discussed in this study may be used for routine identification and differentiation of (a group of) Xcc strains. The significance of the cross-reactions with other pathovars ofX. campestris needs to be determined by testing seed lots. Koninklijke Nederlandse Planteziektenkundige Vereniging, 1992 black rot nationallicence serology nationallicence sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) nationallicence proteinase K nationallicence Franken A. Centre for Plant Breeding and Reproduction Research (CPRO-DLO), P.O. Box 16, 6700 AA, Wageningen, the Netherlands aut Zilverentant J. Laboratory for Monoclonal Antibodies, P.O. Box 9060, 6700 GW, Wageningen, the Netherlands aut Boonekamp P. Bulb Research Centre, P.O. Box 85, 2160 AB, Lisse, the Netherlands aut Schots A. Laboratory for Monoclonal Antibodies, P.O. Box 9060, 6700 GW, Wageningen, the Netherlands aut Netherlands Journal of Plant Pathology Kluwer Academic Publishers 98/2(1992-03-01), 81-94 0028-2944 98:2<81 1992 98 10658 https://doi.org/10.1007/BF01996321 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF01996321 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Franken A. Centre for Plant Breeding and Reproduction Research (CPRO-DLO), P.O. Box 16, 6700 AA, Wageningen, the Netherlands aut NATIONALLICENCE 700 1- Zilverentant J. Laboratory for Monoclonal Antibodies, P.O. Box 9060, 6700 GW, Wageningen, the Netherlands aut NATIONALLICENCE 700 1- Boonekamp P. Bulb Research Centre, P.O. Box 85, 2160 AB, Lisse, the Netherlands aut NATIONALLICENCE 700 1- Schots A. Laboratory for Monoclonal Antibodies, P.O. Box 9060, 6700 GW, Wageningen, the Netherlands aut NATIONALLICENCE 773 0- Netherlands Journal of Plant Pathology Kluwer Academic Publishers 98/2(1992-03-01), 81-94 0028-2944 98:2<81 1992 98 10658 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer