Effector Sites on Antibodies

Calvanico, Nickolas J.; TomasiJr., T. B.

doi:10.1007/978-1-4613-2922-0_1

Cited by 4 publications

(3 citation statements)

References 484 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is generally conceded that a multiplicity ol' determinants on a molecule or aggregate favours immunogenicity and that complement is most efficiently fixed by antigen complexed with a number of antibodies from a population of reasonably balanced concentrations [44,45]. Although these conditions may be scarcely achieved with small or partially disorganized histones, multivalency should not be needed for inhibition of aggregate formation in complement fixation assays.…”

Section: Discussionmentioning

confidence: 99%

“…Although these conditions may be scarcely achieved with small or partially disorganized histones, multivalency should not be needed for inhibition of aggregate formation in complement fixation assays. With soluble antigens and immunoglobulin G [45], such as histones and antihistones [43], complement fixation is more efficient at 4 "C than at the 37 "C used for pre-incubation with prospective inhibitor. Since change in temperature also alters conformation of the antigenic or inhibitory H5 [46] with probable consequences on its immunochemical behaviour [9,47], the antibody complex formed with histone H5 or its peptides at 37 "C may be incapable of accommodating more complement-fixing H5 after the temperature is lowered.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Distribution of Antigenicity in Chicken Erythrocyte Histone H5

et al. 1980

View full text Add to dashboard Cite

We have compared the inhibitory strengths of eight peptides from chicken histone H5 to that of the parent protein (189 residues) in complement fixation by guinea pig anti-H5 serum complexed with the homologous histone. Two precisely delineated regions (residues 59 to 65 and 94 to 99) and two less-defined regions (between 66 and 93; 100 and 189) are depicted. The sequences of particular consequences are quite conserved in avian histone H5 while the most variable N-terminal portion of 31 residues has no inhibitory effect.It is now well established that specific antibodies can be raised in rabbits against histones complexed with nucleic acid [1][2][3][4][5][6], and against free histones' in either rabbits [6-111 or guinea pigs [6,12,13] Antisera against the lysine-rich histones have been used to survey immunological homologies among histone H1 sub-types [2,5 -7,25 -271, to probe conformational changes in isolated H1 [9] or its accessibility in chromatin [28,29], as well as to locate histones H1 and H5 in various cells and metabolic conditions [23,. When specific antisera are used as probes of molecular or subcellular structure, it is valuable to appreciate what regions, or even what precise antigenic determinants, are interacting with the antibodies [6].Using inhibition of complement fixation by a series of peptides from chicken histone H5, we establish that guinea-pig anti-H5 immunoglobulins react primarily but not exclusively with the globular domain near the middle of the H.5 peptide chain. At least two precise antigenic determinants, one of them perhaps exerting a conformational rather than a direct influence, are located in this region. MATERIALS AND METHODSThe lysine-rich histones H1 and H5 were selectively extracted from isotonic-saline-washed nuclei after saponin lysis of saline-washed erythrocytes from normal, adult White Leghorn chickens [12]. Nuclei were stirred at 4 *C for 1 -2 h in trichloroacetic acid [34] at a final concentration of 5 % (w/v) and sedimented at 10000 x g for 10 min. After reextraction the combined supernatants were exhaustively dialyzed against distilled water, lyophilized, and histone H5 was purified by cation-exchange chromatography on a column of Amberlite CG-50 (Rohm and Haas), eluted with a linear gradient of 8 to 20% (w/v) guanidinium chloride buffered in 0.1 M sodium phosphate pH 6.8 [12,35]. Proteins in the extracts and in each purified fraction were identified by electrophoresis in polyacrylamide gel according to Panyim and Chalkley [36].Chicken H5 peptidic fragments, the compositions or sequences of which have been published [37,38], were obtained by cation-exchange or exclusion chromatography after treatment of the parent protein as follows: fragments 1-31 and 32-189', after CNBr cleavage at the methionine [37], fragment 59 -189 after N-bromosuccinimide cleavage at tyrosine [37], fragments 1 -99, 1 -6.5, 66-99 and 100-189 after acetic acid hydrolysis at aspartyl groups [38,39] and fragment 94-189 after pepsin treatment [40]. The molecular weight of the intact protein is ...

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Distribution of Antigenicity in Chicken Erythrocyte Histone H5

et al. 1980

View full text Add to dashboard Cite

show abstract

“…While the Fab fragment selectively binds to the antigen, the Fc fragment -separated by a hinge -appears to be involved in triggering complement system activation through complexation of the C1q subcomponent. Notably, the Fab-antigen interaction is independent of Fc and proceeds even when the Fc fragment has been removed by digestion [1,2]. The complement system is a collection of proteins which attack and destroy cells recognized as alien by the immune complex.…”

Section: Looking For Evidence Of Postulated Intra-molecular Immunologmentioning

confidence: 99%

Supramolecular Congo Red as Specific Ligand of Antibodies Engaged in Immune Complex

Jagusiak

Rybarska

Piekarska

et al. 2017

Self-Assembled Molecules – New Kind of Protein Ligands

View full text Add to dashboard Cite

Supramolecular Congo red has been used to validate long-lasting theories regarding intramolecular signaling in antibodies and its relation to activation of the complement system. Strong enhancement of antigen-antibody complexation resulting from the binding of supramolecular ligands enables also polyclonal antibodies having intermediate affinity to trigger complement cascade apart of high affinity antibody fraction. This would not have been possible in the absence of Congo red. The property of antibodies provides specifically their ability to trigger the complement system allowed when sufficient structural strain is produced by antigen complexation provides an evidence of intramolecular signaling.The selective complexation of supramolecular ligands with antibodies engaged in immune complexes enables their using as carriers of drugs in immunotargeting system. Self-associating organic molecules which form ribbonlike micellar structures may, owing to their structural characteristics, penetrate inside proteins and form stable complexes. Such penetration is possible in areas of the protein which have been destabilized, either temporarily or permanently -such as antibody/antigen complexes. Since Congo red (CR) has been used in research as the most typical Keywords

show abstract