Molecular Stability of Chicken and Rabbit Immunoglobulin G

Shimizu, Makoto; Nagashima, Hitoshi; Sano, Keisuke; Hashimoto, Kei; Ozeki, Makoto; Tsuda, Ken; Hatta, Hajime

doi:10.1271/bbb.56.270

Cited by 112 publications

(80 citation statements)

References 11 publications

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“…The subsequent larger IgY Fc region comprised by additional amino acid residues renders the IgY more hydrophobic than equivalent mammalian IgG. Indeed, IgY-coated latex microspheres are more hydrophobic than corresponding IgG-coated microspheres (46), and based on comparisons of the molecular stabilities of different immunoglobulins by using a fluorescence technique, IgY was observed to be more hydrophobic than mammalian IgG (47). When immunoglobulins interact with recognized antigens, the hydrophobic Fc portion is orientated opposite the antigen and is exposed to an Fc-receptor interaction; thus, IgY opsonization may confer increased surface hydrophobicity.…”

Section: Discussionmentioning

confidence: 99%

Anti-Pseudomonas aeruginosa IgY Antibodies Induce Specific Bacterial Aggregation and Internalization in Human Polymorphonuclear Neutrophils

et al. 2015

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bPolymorphonuclear neutrophils (PMNs) are essential cellular constituents in the innate host response, and their recruitment to the lungs and subsequent ubiquitous phagocytosis controls primary respiratory infection. Cystic fibrosis pulmonary disease is characterized by progressive pulmonary decline governed by a persistent, exaggerated inflammatory response dominated by PMNs. The principal contributor is chronic Pseudomonas aeruginosa biofilm infection, which attracts and activates PMNs and thereby is responsible for the continuing inflammation. Strategies to prevent initial airway colonization with P. aeruginosa by augmenting the phagocytic competence of PMNs may postpone the deteriorating chronic biofilm infection. Anti-P. aeruginosa IgY antibodies significantly increase the PMN-mediated respiratory burst and subsequent bacterial killing of P. aeruginosa in vitro. The mode of action is attributed to IgY-facilitated formation of immobilized bacteria in aggregates, as visualized by fluorescence microscopy and the induction of increased bacterial hydrophobicity. Thus, the present study demonstrates that avian egg yolk immunoglobulins (IgY) targeting P. aeruginosa modify bacterial fitness, which enhances bacterial killing by PMN-mediated phagocytosis and thereby may facilitate a rapid bacterial clearance in airways of people with cystic fibrosis.

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Section: Discussionmentioning

confidence: 99%

Anti-Pseudomonas aeruginosa IgY Antibodies Induce Specific Bacterial Aggregation and Internalization in Human Polymorphonuclear Neutrophils

et al. 2015

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“…IgY is stable at pH 4-9 and up to 65ºC in aqueous condition. However, high salt conditions or the addition of stabilizing reagents increase its resistance to heat, acid extreme pH and high pressure (SHIMIZU et al, 1992).…”

Section: Structural and Functional Features Of Igymentioning

confidence: 99%

Avian IgY antibodies: characteristics and applications in immunodiagnostic

et al. 2014

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“…As we know, IgY is considered a useful candidate to conventional mammalian antibodies. 5 Researchers have successfully produced IgY against a number of antigens, including microbial species and biotoxins. Furthermore, IgY has unique binding characteristics and is more useful in many applications, including immunotherapy and immunodiagnostics.…”

Section: Introductionmentioning

confidence: 99%