Sequence of oving la γ2 constant region heavy chain cDNA and molecular modelling of ruminant IgG isotypes

Clarkson, C A; Beale, D.; Coadwell, John; Symons, D.B.A.

doi:10.1016/0161-5890(93)90138-2

Cited by 29 publications

(22 citation statements)

References 26 publications

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“…Apparently, in the case of rabbit IgG reduction, reduction to H and L and reoxidation occur faster and result in a mixed population of different components. This might be influenced by the fact that there are two subclasses in sheep IgG with different amino acid sequences in the hinge region and only one IgG subclass in rabbit (Clarkson et al 1993). …”

Section: Figure 2 Sds-page Analysis Of Sheep Polyclonal Anti-digoxinmentioning

confidence: 99%

“…Both rabbit and sheep IgG have a single interheavy chain disulfide bond in the hinge region and one disulfide bridge between each of the H and L chains (Clarkson et al 1993, Rayner et al 2013. A mild reductant, 2-MEA and a slightly stronger reductant, TCEP were used for preferential antibody reduction and the obtained products were analyzed by SDS-PAGE.…”

Section: Introductionmentioning

confidence: 99%

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Considerations in producing preferentially reduced half-antibody fragments

Makaraviciute

Jackson

Millner

et al. 2016

Journal of Immunological Methods

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Half-antibody fragments are a promising reagent for biosensing, drug-delivery and labeling applications, since exposure of the free thiol group in the Fc hinge region allows oriented Preferential reduction of rabbit anti-myoglobin IgG antibodies was optimized and the highest half-antibody yield was obtained with 35 mM TCEP. Finally, it has been demonstrated that produced anti-myoglobin half-IgG fragments retained their binding activity.

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Section: Figure 2 Sds-page Analysis Of Sheep Polyclonal Anti-digoxinmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Considerations in producing preferentially reduced half-antibody fragments

Makaraviciute

Jackson

Millner

et al. 2016

Journal of Immunological Methods

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“…Conversely, bIgG2 binds poorly, or not at all, to other bovine Fc␥Rs (10). The reason for this may be that bIgG2 carries a 6-amino acid deletion within the lower hinge region at a site considered to form an Fc␥R binding motif within all IgG molecules in which it is present, including bIgG1 (19,34). Thus, bIgG2 has clearly evolved an FcR binding site distinct from other mammalian IgG molecules.…”

Section: Fig 2 Alignment Of the Protein Sequences Of Bfc␥2r And P58mentioning

confidence: 99%

“…Supporting this theory is the recent observation that IgA1 may in fact adopt a more "T"-like shape, in contrast to the more "Y" shape more readily associated with IgG molecules, suggesting that the hinge region of IgA1 is (at least partly) obscured by the Fab arms hindering binding to this region (38). Moreover, molecular modeling of bovine IgG2 predicts that because of the deletion in the hinge region, bIgG2 is a highly compact molecule with a close positioning of the Fab and Fc domains; this would allow only very little or no angular or rotational movement of the Fab arms in relation to the Fc domain (34). Interestingly, IgA2, the second subclass of human IgA (which readily binds to CD89) also possesses a very short hinge region, and the structure and flexibility of this isotype probably more closely resembles that of bIgG2 (39).…”

Section: Fig 2 Alignment Of the Protein Sequences Of Bfc␥2r And P58mentioning

confidence: 99%

Identification of Residues within the Extracellular Domain 1 of Bovine Fcγ2R Essential for Binding Bovine IgG2

Morton

Howard²,

Storset

et al. 2001

Journal of Biological Chemistry

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Neutrophils and monocytes in cattle express a novel class of immunoglobulin Fc receptor, specific for bovine IgG2 (bIgG2), termed bFc␥2R. In cows, the ability of neutrophils to kill immunoglobulin-opsonized microorganisms appears to depend largely on this subclass, whose interaction with bFc␥2R initiates the killing process. bFc␥2R is a transmembrane glycoprotein consisting of two extracellular immunoglobulin-like domains, followed by a 19-amino acid membrane-spanning region and a short cytoplasmic tail. Although related to other mammalian Fc␥Rs, bFc␥2R belongs to a novel gene family that includes the human killer cell inhibitory receptor and Fc␣RI (CD89) proteins. We have shown previously (Morton, H. C., van Zandbergen, G., van Kooten, C., Howard, C. J., van de Winkel, J. G., and Brandtzaeg, P. (1999) J. Exp. Med. 189, 1715-1722) that like these proteins (and unlike other Fc␥Rs), bFc␥2R binds bIgG2 via the membrane-distal extracellular domain 1 (EC1). In this present study, we introduced mutations into the predicted loop regions of the EC1 domain and assayed the resulting bFc␥2R mutants for their ability to bind bIgG2. Our results indicated that the bIgG2 binding site lies within the predicted F-G loop region of the EC1 domain. Furthermore, single amino acid mutational analysis of this region identified Phe-82 and Trp-87 as being critical for bIgG2 binding.

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“…The constant regions identified in sheep are IgD, IgM (possibly two IgM allotypes), IgG1, IgG2, IgE and IgA [18,24,31,45,86,114,121].…”

Section: Molecular Mechanisms Of B-cell Diversity and Ig Isotypesmentioning

confidence: 99%

The sheep and cattle Peyer’s patch as a site of B-cell development

et al. 2006

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-In sheep and cattle, the ileal Peyer's patch (PP), which extends one-two meters along the terminal small intestine, is a primary lymphoid organ of B-cell development. B-cell diversity in the ileal PP is thought to develop by combinatorial mechanisms, gene conversion and/or point mutation. These species also have jejunal PP that function more like secondary lymphoid tissues concerned with mucosal immune reactions. These two types of PP differ significantly in their histology, ontogeny and the extent of lymphocyte traffic. The prenatal development of follicles in the PP begins first in the jejunum during the middle of gestation and then in the ileum during late gestation. B-cells proliferate rapidly in the ileal PP follicle; up to five percent of these cells survive while the majority dies by apoptosis, perhaps driven by the influence of environmental antigen and/ or self-antigen. The surviving cells migrate from the ileal PP and populate the peripheral B-cell compartment. By adolescence, the ileal PP has involuted but the function of jejunal PP, compatible with a role as secondary lymphoid organ, continues throughout life. In this review, we focus on the development of PP as a site of B-cell repertoire generation, positive and negative B-cell selection, and the differences between ileal PP and jejunal PP.

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Sequence of oving la γ2 constant region heavy chain cDNA and molecular modelling of ruminant IgG isotypes

Cited by 29 publications

References 26 publications

Considerations in producing preferentially reduced half-antibody fragments

Considerations in producing preferentially reduced half-antibody fragments

Identification of Residues within the Extracellular Domain 1 of Bovine Fcγ2R Essential for Binding Bovine IgG2

The sheep and cattle Peyer’s patch as a site of B-cell development

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