Structural and functional properties of mouse-human chimeric IgD

Shin, Seung Uon; Wei, Chao Fan; Amin, Ashok R.; Thorbecke, G. J.; Morrison, Sherie L.

doi:10.3233/hab-1992-3202

Cited by 10 publications

(12 citation statements)

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“…To compute molar concentrations of IgD, IgD⌬h1, and IgMC575S, an accurate molecular mass determination was conducted by MS. The molecular mass of IgD and IgMC575S was estimated to 174.1 and 190.8 kDa, respectively, which are in agreement with previously published results (43)(44)(45). As for IgD⌬h1, it was found to be 158.8 kDa, which is 15.3 kDa less than the wt molecule.…”

Section: Structural Analysissupporting

confidence: 80%

Differential Segmental Flexibility and Reach Dictate the Antigen Binding Mode of Chimeric IgD and IgM: Implications for the Function of the B Cell Receptor

Løset

Roux

Zhu

et al. 2004

The Journal of Immunology

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Mature, naive B cells coexpress IgD and IgM with identical binding sites. In this study, the binding properties of such IgM and IgD are compared to determine how size and shape may influence their ability to bind Ag and thus function as receptors. To dissect their intrinsic binding properties, recombinant IgM and IgD were produced in soluble form as monomers of the basic H2L2 Ab architecture, each with two Ag binding sites. Since these sites are connected with a hinge region in IgD and structural Ig domains in IgM, the two molecules differ significantly in this region. The results show that IgD exhibited the larger angle and longer distance between its binding sites, as well as having the greater flexibility. Relative functional affinity was assessed on two antigenic surfaces with high or low epitope density, respectively. At high epitope density, IgM had a higher functional affinity for the Ag compared with IgD. The order was reversed at low epitope density due to a decrease in the functional affinity of IgM. Studies of binding kinetics showed similar association rates for both molecules. The dissociation rate, however, was slower for IgM at high epitope density and for IgD at low epitope density. Taken together, the results show that IgM and IgD with identical Ag binding regions have different Ag binding properties.

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Section: Structural Analysissupporting

confidence: 80%

Differential Segmental Flexibility and Reach Dictate the Antigen Binding Mode of Chimeric IgD and IgM: Implications for the Function of the B Cell Receptor

Løset

Roux

Zhu

et al. 2004

The Journal of Immunology

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“…Only one disulfide bond, located within the hinge at Cys-290, links the IgD heavy chains. In an earlier study, we showed that the order of assembly for IgD is 2 HL 3 H 2 L 2 (21). It appears that assembly is arrested between these two steps when the Asn-354 carbohydrate is missing.…”

Section: Fig 6 Secretion Of Iga1 and Igd Lacking O-linked Carbohydrmentioning

confidence: 88%

“…IgD-The initial human IgD heavy chain gene expression vector constructed in this laboratory (21) contained the IgD heavy chain gene in its genomic form with six exons. For the current study, a new IgD heavy chain vector was constructed in which the introns within the coding sequence of the constant region were removed using a combination of PCR and cloning.…”

Section: Cloning Mutagenesis and Production Of Murine-human Chimericmentioning

confidence: 99%

“…Murine-human chimeric IgD was not secreted from a transfectant myeloma cell line when produced in the presence of tunicamycin (Tm), an inhibitor of N-linked glycosylation. IgD lacking N-linked glycans was assembled into HL half-molecules rather than fully formed H 2 L 2 antibodies (21), and these remained within the cell. Although this study did not identify the role of individual carbohydrate molecules, it was hypothesized that the glycan at Asn-354 may be critical for the proper conformation of the hinge region in which a single disulfide bond links the two heavy chains at Cys-290.…”

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confidence: 99%

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The Role of Constant Region Carbohydrate in the Assembly and Secretion of Human IgD and IgA1

Gala

Morrison

2002

Journal of Biological Chemistry

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“…The IgD H chain sequences used were derived from the vector pAZ6812, encoding human IgD H chain with murine V H containing dansyl chloride (DNS) specificity (19). The nucleotide sequences used for IgD and IgG have GenBank files (accession numbers 2168527 and 6110571, respectively).…”

Section: Construction Of Recombinant Igd and Igd/igg Chimerasmentioning

confidence: 99%

Characterization of the IgD Binding Site of Encapsulated Haemophilus influenzae Serotype b

Samuelsson

Hallström

Forsgren

et al. 2007

The Journal of Immunology

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Encapsulated Haemophilus influenzae is a causative agent of invasive disease, such as meningitis and septicemia. Several interactions exist between H. influenzae and the human host. H. influenzae has been reported to bind IgD in a nonimmune manner, but the responsible protein has not yet been identified. To define the binding site on IgD for H. influenzae, full-length IgD and four chimeric IgDs with interspersed IgG sequences and Ag specificity for dansyl chloride were expressed in stably transfected Chinese hamster ovary cells. The binding of recombinant IgD to a panel of encapsulated H. influenzae serotype b (Hib) and nontypeable strains were investigated using a whole cell ELISA and flow cytometry. IgD binding was detected in 50% of the encapsulated Hib strains examined, whereas nontypeable H. influenzae did not interact with IgD. Finally, mapping experiments using the chimeric IgD/IgG indicated that IgD CH1 aa 198–224 were involved in the interaction between IgD and H. influenzae. Thus, by using recombinant IgD and chimeras with defined Ag specificity, we have confirmed that Hib specifically binds IgD, and that this binding involves the IgD CH1 region.

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Structural and functional properties of mouse-human chimeric IgD

Cited by 10 publications

References 0 publications

Differential Segmental Flexibility and Reach Dictate the Antigen Binding Mode of Chimeric IgD and IgM: Implications for the Function of the B Cell Receptor

Differential Segmental Flexibility and Reach Dictate the Antigen Binding Mode of Chimeric IgD and IgM: Implications for the Function of the B Cell Receptor

The Role of Constant Region Carbohydrate in the Assembly and Secretion of Human IgD and IgA1

Characterization of the IgD Binding Site of Encapsulated Haemophilus influenzae Serotype b

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