Fc receptors and their interaction with antibodies

Woof, Jenny M.

doi:10.1042/bst0180217

Cited by 5 publications

(4 citation statements)

References 2 publications

(2 reference statements)

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“…In addition, full Fc,,RI binding activity was restored to the inactive mouse IgG2b subclass by reconstructing the LLGGP motif with a single L for E substitution at position 235 (16). Moreover, recent reports (26,27) showed that the binding activity of human IgG3 was lost in a panel of single point mutants where L234, L235, and G237 were replaced with A residues. Together, these observations led us to engineer a panel of IgGi and IgG2 chimeras containing single and sequential point mutations in this region.…”

Section: Discussionmentioning

confidence: 96%

Identification of the Fc gamma receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies.

Chappel

Isenman

Everett

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

113

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Section: Discussionmentioning

confidence: 96%

Identification of the Fc gamma receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies.

Chappel

Isenman

Everett

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

113

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“…FcRγ –/– mice lack the common γ chain and so are deficient in FcγRII and FcγRIII, but there is some residual expression of FcγRI 30. However, rat IgG2a lacks the Leu‐Leu‐Gly‐Gly‐Pro in the hinge region for binding FcγRI 31. It also does not bind mouse complement 32.…”

Section: Discussionmentioning

confidence: 99%

Antigen delivery via two molecules on the CD8^– dendritic cell subset induces humoral immunity in the absence of conventional “danger”

et al. 2005

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Targeting antigen to dendritic cells (DC) in vivo might be an effective method of modulating immune responses. Given the functional specializations among DC subsets, we investigated how targeting different receptors on different DC subsets may influence antibody (Ab) production. We show here that targeting FIRE (F4/80-like receptor) or CIRE (C-type lectin receptor), two molecules expressed on the surface of immature CD8 -DC in the mouse, increases Ab production 100-1000-fold over a non-targeted control. This response was equivalent to that achieved with CpG adjuvant. In contrast, targeting CD205, which is primarily expressed on CD8 + DC, did not elicit an Ab response unless an adjuvant was added. Strong Ab responses in FcRc -/-mice, and with the use of F(ab') 2 fragments, confirmed that FIRE and CIRE targeting was due to specific rather than FcR or complement binding. Our findings may reflect differences in the ability of CD8 + and CD8 -DC subsets to stimulate immune responses in vivo. Although the consensus view is that Ag presentation on DC in their steady state leads to tolerance, the Ab enhancement from FIRE and CIRE targeting in the apparent absence of any "danger" or inflammatory signal would suggest that targeting certain DC molecules can supplant the need for external adjuvants for eliciting immune responses.

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“…IgGI and IgG3 and mouse IgG2a that binds to the high-affinity FcyRI receptor in macrophages [2,10,45]. Although the statistical error of the RG determination is + 0.45 nm, the porcine RG value appears slightly smaller than those for bovine IgG.…”

Section: Figure 5 Comparison Of Experimental and Calculated Curves Fomentioning

confidence: 93%

“…The two Fab fragments (VH, VL CHI and CL domains) and one Fc fragment (two CH2 and two CH3 domains) in IgG are linked by a disulphide-linked polypeptide hinge. An association of the hinge region-CH2 domain of IgG with effector sites in IgG has been described [2]. In order to understand the differences in effector function presented by different IgG isotypes, knowledge is required of the structural features of the hinge regions in these isotypes.…”

Section: Introductionmentioning

confidence: 99%

Demonstration by pulsed neutron scattering that the arrangement of the Fab and Fc fragments in the overall structures of bovine IgG1 and IgG2 in solution is similar

Mayans

Coadwell

Beale

et al. 1995

Biochemical Journal

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The bovine IgG1 and IgG2 isotypes exhibit large differences in effector functions. To examine the structural basis for this, the 12-domain structures of IgG1 and IgG2 were investigated by pulsed neutron scattering using a recently developed camera LOQ. This method reports on the average relative disposition in solution of the Fab and Fc fragments in IgG. The radii of gyration (RG) were found to be similar at 5.64 and 5.71 nm for IgG1 and IgG2 respectively in 100% 2H2O buffers. The two cross-sectional radii of gyration (RXS) were also similar at 2.38-2.41 and 0.98-1.02 nm. Similar values were obtained for porcine IgG. Both bovine IgG1 and IgG2 possess similar overall solution structures, despite sequence differences at the hinge region at the centre of their structures. An automated computer survey of possible IgG structures was developed, in which coordinates for the two Fab fragments were displaced in a two-dimensional plane relative to those of the Fc fragment in 0.25 nm steps. The scattering curves calculated from these structures were found to be sensitive to relative displacements of the three fragments, but not on their rotational orientation about their longest axes. Good agreement with the solution scattering data was obtained with a planar IgG model in which the C-terminus of the CH1 domain of Fab was 3.6 nm from the N-terminus of Fc in both IgG1 and IgG2, with a precision of 0.7 nm. Energy refinement showed that this spatial separation is compatible with the hinge sequences of bovine IgG1 and IgG2. The results show that multidomain protein structures can be modelled using LOQ data, and that a long hinge sequence does not necessarily reflect a large distance between Fab and Fc. The steric accessibility of Fc sites for interactions with cell-surface Fc receptors and C1q of complement is shown to be generally similar for IgG1 and IgG2, and the difference in effector function between IgG1 and IgG2 is probably based on deletions in the IgG2 hinge sequence.

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Fc receptors and their interaction with antibodies

Cited by 5 publications

References 2 publications

Identification of the Fc gamma receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies.

Identification of the Fc gamma receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies.

Antigen delivery via two molecules on the CD8^– dendritic cell subset induces humoral immunity in the absence of conventional “danger”

Demonstration by pulsed neutron scattering that the arrangement of the Fab and Fc fragments in the overall structures of bovine IgG1 and IgG2 in solution is similar

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Fc receptors and their interaction with antibodies

Cited by 5 publications

References 2 publications

Identification of the Fc gamma receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies.

Identification of the Fc gamma receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies.

Antigen delivery via two molecules on the CD8– dendritic cell subset induces humoral immunity in the absence of conventional “danger”

Demonstration by pulsed neutron scattering that the arrangement of the Fab and Fc fragments in the overall structures of bovine IgG1 and IgG2 in solution is similar

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Antigen delivery via two molecules on the CD8^– dendritic cell subset induces humoral immunity in the absence of conventional “danger”