Anti‐hapten antibodies in normal sera

Jormalainen, Seija; Mãkelä, O.

doi:10.1002/eji.1830010613

Cited by 52 publications

(23 citation statements)

References 19 publications

(9 reference statements)

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“…There are some indications that the normal pool of immunoglobu lins reflects the total repertoire of antibodies. Natural antibody titers show great variation between individuals of the same strain or species, but average titers are characteristic of a given strain or species (75,76 limited repertoires such as the Tl5 idiotype (42) and heteroclitic antibody (77) are also expressed in a natural pool of immunoglobulins.…”

Section: Selective Expression Of Antibody Diversitymentioning

confidence: 99%

The Biological Origin of Antibody Diversity

Williamson¹

1976

Annu. Rev. Biochem.

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Antibody diversity has a compelling fascination for many scientists and over the years speculations have sometimes seemed more numerous than facts. Now the structural basis of antibody specificity is well defined. Amino acid sequences and recently three-dimensional structures of various immunoglobulins provide the most solid basis for discussing the origin of diversity. The novel pattern of variable (V) and Constant (C) regions of amino acid sequence has been resolved further to show the functional pattern of variability. Inheritance of separate V and C genes is accepted, but attempts to define more than one gene coding for each V region are considered here to be unnecessary. The pattern of variability is still best understood in terms of mutation and the presence or absence of various selective pressures. The major area of debate still hinges around the extent to which mutation and selection operate during evolution or somatically. Sequence data have now been generally interpreted to require multiple V genes carried in the germ line. A few individual VH genes have been mapped in close linkage to CH genes in the mouse. The apparent existence of three VH alleles in rabbits was a strong argument against multiple V genes. Now the three phenotypes have been shown to be due to alleles controlling the expression of three sets of VH genes all present on the same chromosome. That V-gene expression requires rejoining of V and C genes at the DNA level is now almost certain. Models for the joining process can draw on the precedents of transposable genetic elements, which are widespread in Nature. The total extent of antibody diversity remains a philosophical point. Estimates of the number of antibody molecules required for observed diversity are reduced by two recently documented proposals. Each antibody combining site apparently has many (estimated at 100) different specificities and most combinations of VH and VL regions probably form a viable site. A given combining site can be defined by its pattern of shared specificities. Several specific antibody repertoires have been measured and the size in each case is consistent with the stringency with which the specificity is selected. Repertoire size appears to be under genetic control, but there are problems in viewing the genotype through the veil of clonal selection. Molecular hybridization has been used recently in an attempt to count V and C genes directly. C genes are seen in DNA having nonreiterated sequences, as formal genetics predicts. Each V-region probe hybridizes at a similar rate to C-region probes. Interpretation of this result depends on the extent to which one V-region probe will reveal nonhomologous V genes. Previous estimates that many cross-hybridizing genes should have been seen if present are possibly exaggerated. It is argued here that the data are compatible with a germ-line gene for each probe studied. Maximum estimates for the number of germ-line genes are sufficient to account for antibody diversity...

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Section: Selective Expression Of Antibody Diversitymentioning

confidence: 99%

The Biological Origin of Antibody Diversity

Williamson¹

1976

Annu. Rev. Biochem.

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“…For determination of anti-hapten antibody serum titer, the equilibrium method was employed. Approximately 200 PFU were incubated with varying serum concentrations and the concentration causing 50 % phage inactivation was determined by interpolation as described previously [9]. Results are expressed as the geometric mean of the reciprocals of the antisera dilutions resulting in 50 % hapten-T4 inactivation after 5 h at 3 7 O C .…”

Section: Antibody Assaysmentioning

confidence: 99%

p‐Azobenzenearsonate‐L‐tyrosine‐mediated helper function in immune responses of guinea pigs and rats

et al. 1975

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A small bifunctional antigen (4-hydroxy-5-iodo-3-nitrophenyl)acetyl-epsilon-aminocaproyl-L-tyrosine-azobenzene-p-arsonate [NIP-cap-TYR(ABA)] was found to induce fair humoral antibody formation against NIP-cap but very little anti-ABA-TYR. This was observed in rats and guinea pigs. Prior immunization with ABA-TYR, either as such or coupled to dodecanoylated bovine serum albumin (lipid-BSA), primed rats for an enhanced anti-NIP response to NIP-cap-TYR(ABA). An attempt to encourage rats to produce anti-ABA-TYR in response to the bifunctional antigen by priming them with NIP-cap-lipid-BSA failed. Priming with ABA-TYR was dose-dependent. An injection of 1.5-15 nanomoles per rat primed for an increased production of anti-NIP while 150 nanomoles did not. Adult thymectomized x-irradiated rats had a poor anti-NIP response to the bifunctional antigen if they were reconstituted with T-enriched lymphoid cells from control mice, but a good response if reconstituted with similar cells from ABA-TYR-primed syngeneic rats.

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“…Hapten specificity of these antibodies was confirmed by absorption with DNP coupled to key hole-limpet hemocyanin (KLH) but not with KLH alone. Similar 'natural' DN P-specific antibodies have been detected in rabbit and human sera [14,15]. Epi cutaneous application of a single sensitizing dose of DNCB resulted in a small, but definite rise in IgM, and marked IgGl and IgG2 anti-DNP antibody pro duction.…”

Section: Hapten-specific Antibody Production Following Contact Sensitmentioning

confidence: 65%

Hapten-Specific Antibodies in Allergic Contact Dermatitis in the Guinea Pig

Bril¹,

Scheper²

1988

Int Arch Allergy Immunol

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A guinea pig model was used to investigate the potential role of hapten-specific antibodies in allergic contact dermatitis. Hapten-specific antibodies of both the IgG1, IgG2 and IgM (sub)classes could be readily detected by ELISA in sera obtained after single or repeated exposure to the allergens 2,4-dinitrochlorobenzene (DNCB) or 4-ethoxymethylene-2-phenyloxazolone. Experiments in which animals were strongly boostered with Freund’s complete adjuvant support previous reports that hapten-specific antibodies are able to transfer contact skin reactions with a delayed time course into naive recipients. In contrast, epicutaneous sensitization procedures never allowed transfer of such reactivity. Upon transfer of immune sera to previously sensitized animals, existing allergic contact dermatitis was unaffected, except for a distinct suppression of induration, but not erythema, in the DNCB system. In actively sensitized animals, antibody-related suppression of induration was never observed. Hapten-specific hyposensitivity, as induced by repeated epicutaneous exposure, was also not related to circulating antibody levels. Our findings do not support the view that hapten-specific antibodies should be reconsidered as playing a potentially important role in allergic contact dermatitis.

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Anti‐hapten antibodies in normal sera

Cited by 52 publications

References 19 publications

The Biological Origin of Antibody Diversity

The Biological Origin of Antibody Diversity

p‐Azobenzenearsonate‐L‐tyrosine‐mediated helper function in immune responses of guinea pigs and rats

Hapten-Specific Antibodies in Allergic Contact Dermatitis in the Guinea Pig

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