A new non-species dependent ELISA for detection of antibodies to Borrelia burgdorferi s. l. in zoo animals

Stöbel, Katrin; Schönberg, A.; Staak, C.

doi:10.1016/s1438-4221(02)80018-2

Cited by 46 publications

(44 citation statements)

References 13 publications

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“…The direct ELISA [14] demonstrated the interaction of SpA with the ostrich IgY. The positive control was human IgG and the negative control was chicken IgY which did not bind to SpA [15].…”

Section: Resultsmentioning

confidence: 99%

“…Direct ELISA: An ELISA was used to determine the presence of ostrich Immunoglobulins (IgY) with binding capacity to react to SpA as previously reported in literature [14]. 96 well microtitre plates were coated overnight at 4°C with 1 µg/ml in each well of ostrich IgY samples in carbonate-bicarbonate buffer pH 9.6.…”

Section: Methodsmentioning

confidence: 99%

“…The reaction was stopped with 25 µl of 3M sulphuric acid solution. The plates were read in a microplate reader at 492 nm using standardized procedures [14].…”

Section: Methodsmentioning

confidence: 99%

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Purification of Immunoglobulin Y (IgY) from the Ostrich (Struthio camelus) by Staphylococcal Protein A (SpA) Affinity Chromatography

Vaillant

Akpaka²,

McFarlane-Anderson³

et al. 2012

J Chromat Separation Techniq

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Immunoglobulin Y (IgY) is the major protein present in the avian egg yolk. This antibody fulfils important functions in the protection of Ostrich birds against infections. The aim of this study was to demonstrate the binding capacity of Staphylococcal proteins A (SpA) to Ostrich IgY and assess purification of the IgY by SpA affinity chromatography. Chloroform polyethylene glycol (Polson), affinity chromatography, Enzyme-Linked Immunosorbent Assay (ELISA) and Western blotting methods were used in the process. Results obtained revealed that Ostrich IgY has heavy chain of 70 kDa and light chain of 30 kDa confirming results by Western blot. In addition livetins (egg yolk proteins) were shown in the protein electrophoresis that preceded the Western blot. The binding capacity between SpA and Ostrich IgY is important because SpA can be used as a reagent in immunoassays for antibody detection against microbial agents that usually infect livestocks. This is the first time the use of SpA for purification of Ostrich IgY is being reported in literature.

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“…The direct ELISA [14] demonstrated the interaction of SpA with the ostrich IgY. The positive control was human IgG and the negative control was chicken IgY which did not bind to SpA [15].…”

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Purification of Immunoglobulin Y (IgY) from the Ostrich (Struthio camelus) by Staphylococcal Protein A (SpA) Affinity Chromatography

Vaillant

Akpaka²,

McFarlane-Anderson³

et al. 2012

J Chromat Separation Techniq

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“…adsorvidos na fase sólida . Esta proteína possui uma boa afinidade com IgG de diferentes espécies de mamíferos silvestres e exóticos (Kelly et al 1993, Stöbel et al 2002, Solano-Gallego et al 2003, Lima et al 2005.…”

Section: Introductionunclassified

Teste de ELISA indireto para diagnóstico sorológico de leishmaniose visceral em canídeos silvestres

et al. 2013

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In South America, some wild canids are considered natural reservoirs of Leishmania chagasi. The immunological response of wild canids to Leishmania is not well understood, and the development of diagnostic methods is necessary for such purpose. In the present study, the standardization of an enzyme-linked immunosorbent assay (ELISA) for the serodiagnosis of visceral leishmaniasis (VL) in Brazilian species of wild canids is described. Serum and plasma samples from 12 captive wild canids were studied: seven from maned wolves (Chrysocyon brachyurus), three from hoary foxes (Lycalopex vetulus), and two from crab-eating foxes (Cerdocyon thous). Samples from C. brachyurus and L. vetulus, both captive in an endemic area for VL, presenting clinical disease and positivity in Indirect Immunofluorescence Reaction and Polymerase Chain Reaction tests were used as positive controls. The antibody anti-dog IgG and Protein A, both conjugated with horseradish peroxidase, were compared in indirect ELISA tests which detected four (04/12) and three (03/12) seropositive C. brachyurus for anti-Leishmania antibodies, respectively. The ELISA tests were able to clearly distinguish negative from positive samples, as the mean optical density (OD) of the negative samples was 4.8 and 15.5 times lower than those of the positive ones either using anti-dog IgG and Protein A, respectively. Samples from three ELISA -positive C. brachyurus were analyzed by Western blotting and identified immunodominant bands of 19, 22, 24, 45 and 66 kDa, among 22 protein bands detected. The ELISAs with protein A and anti-dog IgG showed respectively excellent (Kappa = 1.0; p<0.001) and moderate (Kappa = 0.8; p<0.0015) agreement with the Western blotting assay. The ELISA tests showed to be adequate for screening studies to identify antibody responses, thus indicating contact with Leishmania infection by wild canids.INDEX TERMS: Wild canids, Leishmania, visceral leishmaniasis, ELISA, protein A.

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“…More recently using direct ELISA, some new interactions of SpG with free-ranging nondomestic hoofstock (order Artiodactyla) such as bison, muntjac, oryx, bontebok, elk, addax, antelope, impala, kudu/nyala, sheep, and white-tailed deer have been reported [5]. The binding of SpG to IgG from cervids, giraffes, and peccaries was successfully tested by direct enzyme-linked immunosorbent assay (ELISA) [6].…”

Section: Introductionmentioning

confidence: 99%

Inhibition of the Reactivity of Coombs Sera with Igg-Sensitized Human Erythrocytes by Streptococcal Protein-G (Spg)

Vaillant¹,

Smikle²,

Mohammed³

2018

Immunome Res

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Streptococcal protein-G (SpG), type III bacterial Fc receptor, is a small globular protein produced by several Streptococcal species and it is composed of two or three nearly identical domains, each of 55 amino acids. Streptococcal protein G has been shown to have high binding affinity to sera from various mammalian species including rabbit, human, pig, goat, sheep, cow and many other animal species. Of concern are patients with invasive infections by Streptococcus spp, where large amount of secreted SpG could interfere with the outcome of the gel technique by getting false negative tests. It has been shown and reported that the bacterial protein SpA was already found to inhibit the Coomb's test. We hypothesize that SpG as well as many other immunoglobulin-binding bacterial proteins with binding affinity to human IgG could cause false negative results in patients with bacteraemia. With the intention of proving this hypothesis we conducted two sets of experiments, which proved that SpG has the potential of inhibiting the gel test for the detection of sensitized erythrocytes in vitro. We concluded that is important to exercise caution, when evaluating a result of gel technique in patients with septicemia caused by SpG-producer Streptococci. The experiments used in this research were novel modifications of existent techniques and they proved reliable in demonstrating our hypothesis.

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A new non-species dependent ELISA for detection of antibodies to Borrelia burgdorferi s. l. in zoo animals

Cited by 46 publications

References 13 publications

Purification of Immunoglobulin Y (IgY) from the Ostrich (Struthio camelus) by Staphylococcal Protein A (SpA) Affinity Chromatography

Purification of Immunoglobulin Y (IgY) from the Ostrich (Struthio camelus) by Staphylococcal Protein A (SpA) Affinity Chromatography

Teste de ELISA indireto para diagnóstico sorológico de leishmaniose visceral em canídeos silvestres

Inhibition of the Reactivity of Coombs Sera with Igg-Sensitized Human Erythrocytes by Streptococcal Protein-G (Spg)

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