Anti-enteropathogenic Escherichia coli immunoglobulin Y isolated from eggs laid by immunised Leghorn chickens

Amaral, José Araujo; Franco, Milene Tino De; Carneiro‐Sampaio, Magda; Carbonare, S B

doi:10.1053/rvsc.2002.0551

Cited by 26 publications

(20 citation statements)

References 22 publications

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“…The products demonstrated high yield and relative purity values in agreement with previously published reports (Akita & Nakai, 1993;Devi et al, 2002;Amaral et al, 2002). We verified their reactivity to each specific bacterial strain and to the two heterologous bacteria, and examined the effect of these antibodies on the growth of the three organisms.…”

Section: Discussionsupporting

confidence: 87%

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In vitro reactivity and growth inhibition of EPEC serotype O111 and STEC serotypes O111 and O157 by homologous and heterologous chicken egg yolk antibody

et al. 2007

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IgY is a chicken egg yolk antibody which has been used for treatment and prophylaxis of gastrointestinal infections. Our aim was to verify if IgY obtained from chickens immunized with EPEC O111, STEC O111 and STEC O157 is able to show in vitro reactivity and biological activity towards the three bacteria. IgY was obtained from eggs laid before and after immunization with each bacterium. The preparations of IgY anti-EPEC O111 and anti-STEC O111 shared high reactivity detected by ELISA and growth inhibition ability towards both bacteria EPEC O111 and STEC O111. Nevertheless, the preparation of IgY anti-STEC O157 showed high reactivity and growth inhibitory effect only towards the homologous strain. Our results showing in vitro biological activity of IgY reinforce its use as an alternative for the treatment or prophylaxis of E. coli infections and encourage the development of in vivo studies for a possible future human therapeutic use.

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Section: Discussionsupporting

confidence: 87%

“…The IgY purification procedure was performed as previously described by Amaral et al (2002), with some modifications. Briefly, the egg yolk was carefully separated from the white, washed, and the liquid content inside the egg yolk membranes were pooled in eight different pools (pre-and post-immunization).…”

Section: Egg Yolk Separation and Igy Purificationmentioning

confidence: 99%

In vitro reactivity and growth inhibition of EPEC serotype O111 and STEC serotypes O111 and O157 by homologous and heterologous chicken egg yolk antibody

et al. 2007

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“…Oral administration of IgY antibodies has been tested for many years with promising results [80] to different pathogens as human rotavirus [81]; dental plaque formation by Streptococcus mutans [82,83]; enteropathogenic E. coli [84]; Helicobacter pylori [85,86]; Cryptosporidium parvum [87,88]; canine parvovirus [89]; Porphyromonas gingivalis [90]; Pseudomonas aeruginosa [91]; shrimp's white spot syndrome virus [92]; Eimeria acervulina [93]; E. tenella and E. maxima [94,95]; H5N1 e H1N1 in mice [96]; Vibrio cholerae [97]; rotavirus and norovirus [98]; Campylobacter jejuni [99][100][101]; and botulinum neurotoxins [102]. Immunotherapy as a passive immunization method to neutralize venom using purified IgY proved to be efficient for therapy protocol [103][104][105][106][107].…”

Section: Using Igy For Passive Immunizationmentioning

confidence: 99%

IgY-Technology Applied to Studies of Toxoplasma gondii Infection

Júnior¹,

Santos²,

Bassi³

et al. 2017

Toxoplasmosis

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In this chapter, we describe relevant aspects of immunoglobulin Y (IgY) technology for Toxoplasma gondii applications, including comparison of avian IgY antibody with mammalian IgG antibody, egg yolk IgY production and isolation procedures, important applications for IgY antibody, and state of the art and perspectives for IgY-technology in T. gondii studies. T. gondii is a worldwide public health problem. IgY-technology provides an alternative antibody (IgY) to mammalian Immunoglobulin G (IgG) antibody. IgY-technology involves the chicken immunization, yolk IgY isolation, antibody characterization, and purified IgY application to several kinds of methods. Immunized chicken transfers a specific IgY from blood to egg yolk. Phylogenetic distance between chickens and mammals influences the generation of antibody repertoires recognizing an antigen profile. IgY is not bound to rheumatoid factor or mammalian complement protein and thus avoids the false-positive results. Yolk IgY isolation is carried out by simple procedures that are accessible for any laboratory and, also, for IgY isolation at large-scale production. IgY-technology provides antibodies for proteomic studies, diagnostic assays, and immunotherapy. Although IgY-technology is promising, there is a reduced number of investigations with IgY and T. gondii. Future perspectives involve the use of IgY-technology for the screening of new T. gondii antigens for diagnostics, therapy, or vaccine, development of innovative techniques for toxoplasmosis diagnostics and may be an immunotherapy for toxoplasmosis.

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“…There is an increasing interest in the use of chicken egg yolk for polyclonal antibody production for practical and economical reasons (Bollen and Hau, 1996;Svendsen et al, 1994;Tini et al, 2002). The egg yolk antibodies (IgY) in recent years remarkably used for scientific (Schade et al, 1997), diagnostic (Di Lonardo et al, 2001), prophylactic (Almeida et al, 1998;Sarker et al, 2001) and therapeutic purposes (Lemamy et al, 1999), and n the other hand for veterinarian therapy against bacteria such as enteropathogenic Escherichia coli (Amaral and Franco, 2002). Several advantages of IgY like, the phylogenetic distance between birds and mammals, help to increase immune response in host body (birds) in comparison to mammalian hosts (Leslie and Clem, 1969;Hau et al, 1980;Hau et al, 1981).…”

Section: Introductionmentioning

confidence: 99%

Apoptotic Killing of Breast Cancer Cells by IgYs Produced Against a Small 21 Aminoacid Epitope of the Human TRAIL-2 Receptor

Amirijavid¹,

Entezari²,

Movafagh³

et al. 2016

Asian Pacific Journal of Cancer Prevention

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TRAIL, tumor necrosis factor (TNF)-related apoptosis-inducing ligand belongs to one of important cytokine superfamilIES, tumor necrosis factor (TNFα) . TRAIL-2 receptor agonists activate several cell signaling pathways in cells in different manners and could lead to apoptosis or necrosis. Agonistic egg yolk antibodies like IgY which have been developed in a selective manner could activate TRAIL death receptors such as TRAIL-2 (DR5) and thus apoptosis signaling. We here investigated induction of apoptosis in human breast cancer cells (MCF7 cell line) by an IgY produced against an 21 aminoacid epitope of the human TRAIL-2 receptor. As the first step a small peptide of 21 aminoacids choosen from the extracellular domain of DR5 protein was produced with a peptide synthesizer. After control assays and confirmation of the correct amino acid sequence, it was injected to hens immunized to achieve high affinity IgYs. At the next step, the produced IgYs were extracted and examined for specificity against DR5 protein by ELISA assay. Subsequently, the anticancer effect of such IgYs was determined by MTT assay in the MCF7 human breast cancer cell line. The produced peptides successfully immunized hens and the produced antibodies which accumulated in egg yolk specifically recognized the DR5 protein. IgYs exerted significant toxicity and killed MCF7 cells as shown by MTT assay.

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Anti-enteropathogenic Escherichia coli immunoglobulin Y isolated from eggs laid by immunised Leghorn chickens

Cited by 26 publications

References 22 publications

In vitro reactivity and growth inhibition of EPEC serotype O111 and STEC serotypes O111 and O157 by homologous and heterologous chicken egg yolk antibody

In vitro reactivity and growth inhibition of EPEC serotype O111 and STEC serotypes O111 and O157 by homologous and heterologous chicken egg yolk antibody

IgY-Technology Applied to Studies of Toxoplasma gondii Infection

Apoptotic Killing of Breast Cancer Cells by IgYs Produced Against a Small 21 Aminoacid Epitope of the Human TRAIL-2 Receptor

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