The Detection of Viruses by Enzyme-Linked Immunosorbent Assay (ELISA)

Voller, A.; Bartlett, A.; Bidwell, D. E.; Clark, M. F.; Adams, A. N.

doi:10.1099/0022-1317-33-1-165

Cited by 284 publications

(143 citation statements)

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“…Rapid and accurate diagnosis is often possible directly on crude preparations using precipitin tests, immunosorbent assays (Voller et al, 1976(Voller et al, , 1979 and various versions of immunoelectron microscopy (Milne & Luisoni, 1977). This is highly cost-effective and renders many of the other diagnostic tests redundant, providing of course that a clear positive answer can be obtained.…”

Section: Reactions With Likely Antiseramentioning

confidence: 99%

Guidelines for the Identification and Characterization of Plant Viruses

Hamilton

Edwardson

Francki

et al. 1981

Journal of General Virology

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Section: Reactions With Likely Antiseramentioning

confidence: 99%

Guidelines for the Identification and Characterization of Plant Viruses

Hamilton

Edwardson

Francki

et al. 1981

Journal of General Virology

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“…Virus accumulation in infected tobacco plants was monitored by ELISA using anti-PVY N605 antibodies conjugated to alkaline phosphatase (Voller et al, 1976). Where indicated, 4-week-old tobacco plants were treated with 100 L L Ϫ1 ethylene in a closed chamber for 48 h. Control plants were incubated in a similar chamber without ethylene.…”

Section: Inoculation Of Plants and Treatment With Ethylenementioning

confidence: 99%

NopL, an Effector Protein ofRhizobiumsp. NGR234, Thwarts Activation of Plant Defense Reactions

et al. 2004

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Bacterial effector proteins delivered into eukaryotic cells via bacterial type III secretion systems are important virulence factors in plant-pathogen interactions. Type III secretion systems have been found in Rhizobium species that form symbiotic, nitrogen-fixing associations with legumes. One such bacterium, Rhizobium sp. NGR234, secretes a number of type III effectors, including nodulation outer protein L (NopL, formerly y4xL). Here, we show that expression of nopL in tobacco (Nicotiana tabacum) prevents full induction of pathogenesis-related (PR) defense proteins. Transgenic tobacco plants that express nopL and were infected with potato virus Y (necrotic strain 605) exhibited only very low levels of chitinase (class I) and ␤-1,3-glucanase (classes I and III) proteins. Northern-blot analysis indicated that expression of nopL in plant cells suppresses transcription of PR genes. Treatment with ethylene counteracted the effect of NopL on chitinase (class I). Transgenic Lotus japonicus plants that expressed nopL exhibited delayed development and low chitinase levels. In vitro experiments showed that NopL is a substrate for plant protein kinases. Together, these data suggest that NopL, when delivered into the plant cell, modulates the activity of signal transduction pathways that culminate in activation of PR proteins.Plants have evolved many defenses against invading pathogens. Among them are preformed antimicrobial compounds, as well as inducible defense proteins, the so-called pathogenesis-related (PR) proteins (van Loon, 1997). It has been shown, for example, that pathogen-induced chitinases (EC 3.2.1.14) and ␤-1,3-glucanases (EC 3.2.1.39) synergistically lyse fungal cell walls (Mauch et al., 1988). Specific recognition of pathogens often induces a hypersensitive response, which is characterized by an oxidative burst and localized death of the host cells. In most cases, the induction of a hypersensitive response arrests invasion by the pathogen (Dangl and Jones, 2001).Virulence in gram-negative bacteria often depends on proteins injected into eukaryotic cells. Some bacteria elaborate a specialized protein secretion apparatus, the type III secretion system (TTSS). The TTSS exports a set of proteins from the bacteria, some of which are delivered directly into the eukaryotic cells-a process called translocation (Cornelis and van Gijsegem, 2000;Plano et al., 2001). Most translocated type III effectors act on the cytoskeleton or interfere with intracellular signaling cascades of the host cell. Yersinia pestis, for example, injects at least six type III effectors into host cells, where they thwart the signaling machinery of the immune system (Cornelis, 2002). Plant pathogens such as Pseudomonas syringae and Xanthomonas campestris also use TTSSs (Kjemtrup et al., 2000; Lahaye and Bonas, 2001). Mounting evidence suggests that type III effectors translocated into plant cells (Casper-Lindley et al., 2002;Szurek et al., 2002) act as virulence factors in susceptible hosts. One likely function of type III effectors is ...

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“…Supernatants of hybridoma cultures or ascitic fluids were assayed for antibody activity by solid-phase ELISA against antigens coated by overnight incubation at 37 "C after dilution in fivefolddiluted GBS in water (Voller et al, 1979). The antigens used to coat the plates consisted of CW (20pg ml-l), CE (diluted 1 in 10oO), S-LPS (4 pg ml-I), R-LPS (10 pg ml-l), OPS (4 pg ml-I) and whole bacterial cells (OD,,o 1.5).…”

Section: Mabsmentioning

confidence: 99%

O-chain expression in the rough Brucella melitensis strain B115: induction of O-polysaccharide-specific monoclonal antibodies and intracellular localization demonstrated by immunoelectron microscopy

Cloeckaert

Zygmunt²,

Nicolle³

et al. 1992

Journal of General Microbiology

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Spleen cells from mice infected with the rough Brucella melitensis strain B115 were fused with NSO myeloma cells.Hybridoma supernatants were screened in ELISA with cell walls (CW), sonicated cell extracts (CE) and rough lipopolysaccharide (R-LPS) of B. melitensis strain B115 and whole B. melitensis B115 cells. Surprisingly, 22 monoclonal antibodies (mAbs) reacting in ELISA with both CW and CE but not with R-LPS and bacterial cells were shown by immunoblot analysis and ELISA to react with smooth lipopolysaccharide (S-LPS). These mAbs also reacted in ELISA with 0 polysaccharides (OPS) from the smooth Brucellu abortus strain 99 and the smooth B. melitensis strain 16M and thus recognize epitopes present on the 0-chain. Proteinase K LPS preparations from B. melitensis B115 analysed by immunoblotting with one mAb (12G12) recognizing S-LPS of both A and M specificity displayed the typical S-LPS high-molecular-mass ladder pattern but no S-LPS was detected in the phenol/water/chloroform/light petroleum LPS preparation of the same strain. mAb 12G12, specific for S-LPS, and a mAb (A68/03F03/DO5) specific for R-LPS were used to localize the 0-chain and R-LPS expressed in B. melitensis strain B115 by immunoelectron microscopy. Immunogold labelling was observed at the surface of B. melitensis B115 cells with the anti-R-LPS mAb but not with the anti-S-LPS mAb. In ultrathin sections, immunogold labelling with the S-LPS specific mAb was observed in the cytoplasm and in the periphery of the cytoplasm, probably at the cytoplasmic membrane. Immunogold labelling with the R-LPS specific mAb was observed at the outer membrane, outside the cells and on R-LPS vesicles. These results indicate that 0-chain expressed in the rough B. melitensis strain B115 is immunogenic in mice, not exposed at the cell surface but present in the cytoplasm and most probably at the cytoplasmic membrane.

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The Detection of Viruses by Enzyme-Linked Immunosorbent Assay (ELISA)

Cited by 284 publications

References 0 publications

Guidelines for the Identification and Characterization of Plant Viruses

Guidelines for the Identification and Characterization of Plant Viruses

NopL, an Effector Protein ofRhizobiumsp. NGR234, Thwarts Activation of Plant Defense Reactions

O-chain expression in the rough Brucella melitensis strain B115: induction of O-polysaccharide-specific monoclonal antibodies and intracellular localization demonstrated by immunoelectron microscopy

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