The antibody response of pigs to dinitrophenylated bovine IgG administered with a novel type of adjuvant

Franěk, František; Simek, L

doi:10.1002/eji.1830010417

Cited by 28 publications

(5 citation statements)

References 5 publications

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“…Antiserum against purified lipopolysaccharide-binding protein was obtained as follows. Two rabbits (female, 4-6 months old) received the purified protein (0.75 mg per animal), emulsified in an inorganic adjuvant mixture [48], intramuscularly (legs), intracutaneously (back) and into the foot pads. Six weeks later the animals were boosted with the same dose.…”

Section: Antiseramentioning

confidence: 99%

A Lipopolysaccharide‐Binding Cell‐Surface Protein from Salmonella minnesota

Geyer¹,

Galanos²,

Westphal³

et al. 1979

European Journal of Biochemistry

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Protein extracts obtained from Salmonella minnesota Re mutant cells by treatment with EDTA/NaCl solution contain a protein which exhibits high affinity to bacterial lipopolysaccharides. The isolation and partial characterization of this lipopolysaccharide‐binding protein is described. The protein was purified from EDTA extracts by a two‐step procedure consisting of ion‐exchange chromatography on CM‐Sephadex and preparative polyacrylamide gel electrophoresis at pH 9.5. The yield of the total purification procedure was around 16%. The resulting protein preparation was homogeneous on the basis of disc gel electrophoresis, dodecylsulfate gel electrophoresis, isoelectric focusing in polyacrylamide gel and immunoelectrophoresis. The isoelectric point of the protein was found to be 10.3 at 4°C. Its molecular weight determined by dodecylsulfate gel electrophoresis is 15000. Its amino acid composition is characterized by the absence of histidine and proline, a low content in tyrosine and high amounts of alanine, lysine, aspartic and glutamic acid residues, or their respective amides. The lipopolysaccharide‐protein association was shown to be mainly due to ionic interactions of the basic protein with negatively charged groups (probably phosphate and pyrophosphate groups) of the lipid A moiety. Purified lipopolysaccharide‐binding protein is immunogenic in rabbits, thus enabling the preparation of specific antiserum. The protein is located at the surface of Salmonella minnesota Re mutant cells as revealed by antiserum absorption with total bacteria. Ferritin‐labelling studies further demonstrated that it is evenly spread over the entire cell surface. Comparative antiserum absorption studies using smooth and rough strains of Salmonella minnesota, Salmonella typhimurium, Escherichia coli, Klebsiella and Shigella revealed the presence of lipopolysaccharide‐binding protein (or a serologically cross‐reacting antigen) in most of the strains tested. From these results the protein can be considered as a common antigen of Enterobacteriaceae.

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Section: Antiseramentioning

confidence: 99%

A Lipopolysaccharide‐Binding Cell‐Surface Protein from Salmonella minnesota

Geyer¹,

Galanos²,

Westphal³

et al. 1979

European Journal of Biochemistry

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“…Immunization. Antisera against the ABA group (anti-ABA antibody) as well as against the DNP determinant (anti-DNP antibody) were prepared by immunizing pregnant Simmentaler cows, 2-3 yr of age (450-500 kg), with either 120 mg of ABA-Ed, DNP-Ed or (DNP)2-Gram, respectively, emulsified in an adjuvant composed of aluminium hydroxide gel, paraffin oil, and sorbitan trioleate (20). At appropriate times after priming (8 wk) a secondary challenge was performed after the immunization schedule as outlined previously (21).…”

Section: Bivalent Haptens An-(en-dnp-aminocaproyl-)-~n-dnp-l-lysinementioning

confidence: 99%

Experimental Studies on the Bridging Hypothesis of Anaphylaxis

Mossmann

Meyer‐Delius

Vortisch

et al. 1974

The Journal of Experimental Medicine

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The present study has established, that cows suitably immunized with either DNP-edestin (DNP-Ed), di-DNP-gramicidin-J [(DNP)2-Gram], respectively, or p-azobenzenearsonate-Ed (ABA-Ed) synthesized and secreted reaginic antibodies (IgE) into colostrum. Whereas ABA-Ed failed to elicit more than a low response, there was however a persistent and increased antibody synthesis between 10 and 56 days after priming with DNP-Ed. Bivalent and multivalent DNP haptens differing in molecular size, degree of substitution, and rigidity were compared for their effectiveness in eliciting Prausnitz-Küstner (P-K) reactions in either newborn colostrum-deprived calves or in those 4 wk of age. The sensitization with reaginic anti-DNP antibody has been accomplished either by feeding colostrum of the immunized dam or by intradermal injection of reaginic serum or colostral whey. It could be demonstrated that equimolar doses of the bivalent α,N-(ϵ,N-DNP-aminocaproyl-)-ϵ,N-DNP-L-lysine and the multivalent dinitrophenylated bovine serum albumin were equally effective in eliciting reactions in skin sites provided that a high affinity antibody was used for sensitization. By contrast, the comparatively rigid, bivalent hapten, (DNP)2-Gram consistently failed to induce comparable reactions. Furthermore, it was clearly shown that optimal distances of determinant groups on the haptenic molecule are a prerequisite for positive P-K reactions, since α,ϵ,N-bis-DNP-lysine failed to induce comparable reactions. Concurrent sensitization of skin sites with reaginic anti-DNP and anti-ABA antibodies provides the final proof that cross-linking of two adjacent reaginic molecules on the mast cell surface by a bivalent hapten is required for effective elicitation of immediate-type reactions. This has been accomplished by utilizing the bivalent ϵ,N-DNP-α,N-[(4-hydroxy-3-azobenzenearsonic acid)-phenacetyl]-L-lysine (DNP-ABA) carrying noncross-reactive haptenic groups, which was consistently effective in eliciting P-K reactions in doubly but never in singly sensitized skin sites. It is apparent from the results that equimolar doses of monovalent haptens could completely inhibit the response to DNP-ABA. The present studies finally establish that mast cells of newborn colostrum-deprived calves lack IgE molecules on their surface. Thus, mast cells of newborn calves may be unique, to investigate the molecular mechanisms involved in immediate-type reactions more precisely.

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“…Antisera to the deltin fraction were prepared by immunizing five New Zealand rabbits with the lyophilized deltin fraction administered with the Al-Span-Oil adjuvant (Franěk & S {imek 1971). Fifteen milligrams of the lyophilized material was dissolved in 3 ml of PBS and mixed with 3 ml of Willstätter's aluminium hydroxide suspension.…”

Section: Antiseramentioning

confidence: 99%

Deltins: immunochemical evidence for a novel population of peptides of the D cells of the gastro-entero-pancreatic endocrine system

Lomský

Pribysova²,

Jirkalová³

et al. 2001

Journal of Endocrinology

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Differences between the immunocytochemical behaviour of antisera to partially purified porcine gastrins and antisera to either synthetic human gastrin-17-I or highly purified porcine gastrin-17-I raised the hypothesis that hog antral gastrin extracts contain peptides different from somatostatin and gastrin that are responsible for the immunocytochemical reaction of the former antisera in the D (delta) cells of the gastro-entero-pancreatic (GEP) endocrine system. This study was performed to prove this hypothesis. A discard fraction obtained after gel filtration of hog antral gastrin extracts on Sephadex G-50 Superfine was employed to immunize five rabbits. The discard fraction is highly heterogeneous on two-dimensional electrophoresis and contains merely traces of somatostatin and gastrin in RIA. However, rabbit antisera to the discard fraction give strongly positive immunocytochemical reactions exclusively in the D cells of the human antroduodenal mucosa and of the pancreatic islets. Absorption of the antisera with the lyophilized discard fraction abolishes the staining of the D cells, whereas absorption of the antisera with several somatostatins does not affect the staining. Vice versa, staining of the D cells with antisera to cyclic somatostatin-14 is abolished by absorption of the antisera with somatostatin-14 but not by absorption with excess of the discard fraction. In RIA, antisera to the discard fraction do not bind radiolabelled (Tyr 1 )-somatostatin-14, Tyr-somatostatin-28 or synthetic human gastrin-17-I. Two-dimensional electrophoresis of acid extracts of isolated canine pancreatic islets followed by Western blotting shows different patterns of distribution of immunoreactive spots obtained with antisera to the discard fraction, to somatostatin-14, and to human proinsulin respectively. These results indicate the existence of a novel population of peptides of the D cells of the GEP endocrine system, for which we propose the term deltins.

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The antibody response of pigs to dinitrophenylated bovine IgG administered with a novel type of adjuvant

Cited by 28 publications

References 5 publications

A Lipopolysaccharide‐Binding Cell‐Surface Protein from Salmonella minnesota

A Lipopolysaccharide‐Binding Cell‐Surface Protein from Salmonella minnesota

Experimental Studies on the Bridging Hypothesis of Anaphylaxis

Deltins: immunochemical evidence for a novel population of peptides of the D cells of the gastro-entero-pancreatic endocrine system

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