Products of aminolysis and enzymic hydrolysis of the cephalosporins

Hamilton‐Miller, J. M. T.; Newton, G. G. F.; Abraham, E. P.

doi:10.1042/bj1160371

Cited by 99 publications

(50 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, these results indicate the importance of the acyl side chains in cross-reactions of AB-specific antibodies. This is supported by the report that the produced epitope is un stable, undergoing elimination of the C-3 side chain, dur ing the reaction of a cephalosporin AB and a protein [13]. CAZ and CPZ, which have a bulky group other than an allyl group in the acyl side chains such as tertiary butyric acid group and hydroxylphenyl group, showed little cross-reac tivity.…”

Section: Discussionsupporting

confidence: 55%

Immunogenicity of Various Beta-Lactam Antibiotic-Protein Conjugates and Cross-Reactivity of the Antibodies Produced in Guinea Pig

Katsutani¹,

Shionoya²

1993

Int Arch Allergy Immunol

View full text Add to dashboard Cite

Immunogenic properties of bovine serum albumin (BSA) conjugates of various β-lactam antibiotics (ABs) and cross-reactivity of the produced antibodies were investigated in guinea pigs. Each AB-BSA conjugate was immunized with complete Freund’s adjuvant. Following the second injection, AB-specific antibodies were detected with high titers. Produced antibodies showed concentration-dependent inhibition by the corresponding AB. Cross-reactivity between the produced antibodies and ABs was evaluated with two methods, i.e. by testing for reactivity with the various AB-ovalbumin conjugates, and by assaying for inhibition of enzyme-linked immunosorbent assay (ELISA) by the various ABs. The latter method could detect minor cross-reactions more sensitively than the former one. The results suggested that similarity of the acyl side chain of a cephalosporin nucleus or a penicillin nucleus contributes to immunological cross-reactivity.

show abstract

Section: Discussionsupporting

confidence: 55%

Immunogenicity of Various Beta-Lactam Antibiotic-Protein Conjugates and Cross-Reactivity of the Antibodies Produced in Guinea Pig

Katsutani¹,

Shionoya²

1993

Int Arch Allergy Immunol

View full text Add to dashboard Cite

show abstract

“…Despite the similarity in structure between these two major groups of antibacterials, important differences in chemical reactivity and stability exist. In particular, unlike penicillins, alkali treatment of cephalosporins leads to aminolysis via unstable intermediates that decompose to penaldate and ultimately penamaldate structures [12,21,22], that is, structures comprising only the R 1 side chain, the attached amide and parts of the original β-lactam ring remain. By employing a solid phase prepared by alkali treatment of some frequently used cephalosporins, IgE antibodies specific for R 1 side chains of some cephalosporins were demonstrated in the sera of patients who experienced immediate allergic reactions, including anaphylaxis, following administration of a cephalosporin ( Figure 5b).…”

Section: Recognition Of Cephalosporin R 1 and R 2 Side Chains By Ige mentioning

confidence: 99%

IgE and Drug Allergy: Antibody Recognition of ‘Small’ Molecules of Widely Varying Structures and Activities

Baldo

2014

Antibodies

View full text Add to dashboard Cite

Abstract:The variety of chemically diverse pharmacologically-active compounds administered to patients is large and seemingly forever growing, and, with every new drug released and administered, there is always the potential of an allergic reaction. The most commonly occurring allergic responses to drugs are the type I, or immediate hypersensitivity reactions mediated by IgE antibodies. These reactions may affect a single organ, such as the nasopharynx (allergic rhinitis), eyes (conjunctivitis), mucosa of mouth/throat/tongue (angioedema), bronchopulmonary tissue (asthma), gastrointestinal tract (gastroenteritis) and skin (urticaria, eczema), or multiple organs (anaphylaxis), causing symptoms ranging from minor itching and inflammation to death. It seems that almost every drug is capable of causing an immediate reaction and it is unusual to find a drug that has not provoked an anaphylactic response in at least one patient. These facts alone indicate the extraordinary breadth of recognition of IgE antibodies for drugs ranging from relatively simple structures, for example, aspirin, to complex molecules, such as the macrolide antibiotics composed of a large macrocyclic ring with attached deoxy sugars. This wide recognition profile is borne out at the molecular level by results of quantitative immunochemical studies where hapten inhibition investigations have identified structural determinants complementary to IgE antibodies in the sera of allergic subjects. Allergenic determinants have been identified on a variety of drugs including neuromuscular blockers, penicillins, cephalosporins, opioids, thiopentone, sulfonamides, trimethoprim, quinolones, chlorhexidine and the non-steroidal anti-inflammatory drug aspirin. It is already clear that IgE can distinguish fine structural differences on a wide variety of molecules, determinants OPEN ACCESSAntibodies 2014, 3 57 may be at least as small as an amino group or encompass the whole molecule, and individual drugs may demonstrate allergenic heterogeneity.

show abstract

“…In penicillins, release is preceded by (enzymatic) fragmentation [7,23] while in cephalosporins it is accompanied 17) (chemical) fragmentation [24,25], making the identifical ion of initial release products difficult in both cases. The release of penicillins is further complicated by the fact that [lie fragmentation preceding deacylation is rate-limiting, and by the instability of the thiazolidine-derived release product.…”

Section: Discussionmentioning

confidence: 99%

Interaction between Monobactams and Streptomyces R61 dd‐Carboxypeptidase

Georgopapadakou¹,

Smith²,

Cimarusti³

1982

European Journal of Biochemistry

View full text Add to dashboard Cite

The monobactams are a novel family of monocyclic /I-lactam antibiotics characterized by the 2-oxoazetidine-1 -sulfonic acid moiety. A series of monobactams bind covalently to the Streptorn~~ces R6 I vD-carboxypeptidase in a manner similar to that for bicyclic /?-lactams, especially cephalosporins. The similaint5 of interaction wits established by the following criteria : inhibition of binding by diisopropylfluorophosphatc. and K-dicarbonyls; stoichiometry of binding; similarity of partial proteolysis products of radiolabelled enzq me: rates of release of bound /j-lactams ; nature of hydrolysis and hydroxylaminolysis products.Monobactams are monocyclic b-lactam antibodies, characterized by the 2-oxoazetidine-1 -sulfonic acid moiety (Fig.

show abstract

Products of aminolysis and enzymic hydrolysis of the cephalosporins

Cited by 99 publications

References 23 publications

Immunogenicity of Various Beta-Lactam Antibiotic-Protein Conjugates and Cross-Reactivity of the Antibodies Produced in Guinea Pig

Immunogenicity of Various Beta-Lactam Antibiotic-Protein Conjugates and Cross-Reactivity of the Antibodies Produced in Guinea Pig

IgE and Drug Allergy: Antibody Recognition of ‘Small’ Molecules of Widely Varying Structures and Activities

Interaction between Monobactams and Streptomyces R61 dd‐Carboxypeptidase

Contact Info

Product

Resources

About