A pyridinium-substituted semisynthetic, broad-spectrum antibacterial used especially for Pseudomonas infections in debilitated patients.
One of the CEPHALOSPORINS that has a broad spectrum of activity against both gram-positive and gram-negative microorganisms.
A group of broad-spectrum antibiotics first isolated from the Mediterranean fungus ACREMONIUM. They contain the beta-lactam moiety thia-azabicyclo-octenecarboxylic acid also called 7-aminocephalosporanic acid.
Semisynthetic penicillin-type antibiotic.
A semisynthetic ampicillin-derived acylureido penicillin.
Semisynthetic ampicillin-derived acylureido penicillin. It has been proposed for infections with certain anaerobes and may be useful in inner ear, bile, and CNS infections.
A hexosyltransferase involved in the transfer of disaccharide molecules to the peptidoglycan structure of the CELL WALL SKELETON. It plays an important role in the genesis of the bacterial CELL WALL.
A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection.
An antibiotic derived from penicillin similar to CARBENICILLIN in action.
Four-membered cyclic AMIDES, best known for the PENICILLINS based on a bicyclo-thiazolidine, as well as the CEPHALOSPORINS based on a bicyclo-thiazine, and including monocyclic MONOBACTAMS. The BETA-LACTAMASES hydrolyze the beta lactam ring, accounting for BETA-LACTAM RESISTANCE of infective bacteria.
Enzymes found in many bacteria which catalyze the hydrolysis of the amide bond in the beta-lactam ring. Well known antibiotics destroyed by these enzymes are penicillins and cephalosporins.
Substances that reduce the growth or reproduction of BACTERIA.

Fast lysis of Escherichia coli filament cells requires differentiation of potential division sites. (1/46)

Periodic activation of zonal peptidoglycan (murein) synthesis at division sites in Escherichia coli has been reported recently. Zonal synthesis is responsible for septum formation, whereas elongation of the cell sacculus is performed by diffuse insertion of precursors. Zonal synthesis can be triggered in ftsA, ftsQ and ftsI (pbpB) division mutants growing as filaments at the restrictive temperature, but not in ftsZ mutant strains. The lytic response to beta-lactams of cells able or unable to periodically trigger a zonal mode of murein synthesis could be substantially different. Therefore, we investigated the response to the bacteriolytic beta-lactam cefsulodin of ftsZ and ftsI mutants growing at the restrictive (42 degrees C) temperature. The ftsI cells lysed early and quickly after addition of the antibiotic. Sacculi of lysed cells were transversely cut in a very sharp way. In contrast the ftsZ strain lysed late and slowly after addition of the antibiotic and sacculi showed a generalized weakening of the murein network and extended breaks with a frayed appearance. No transversely cut sacculi comparable to those seen in the ftsI samples were found. Our results strongly support that beta-lactam-induced lysis occurs preferentially at division sites because of the activation of zonal murein synthesis at the initiation of septation.  (+info)

Comparative in vitro activities of SCE-129, sulbenicillin, gentamicin, and dibekacin against Pseudomonas. (2/46)

Against sulbenicillin- and gentamicin-susceptible strains of Pseudomonas aeruginosa, SCE-129 was about 10 times more active than sulbenicillin and had a similar activity to gentamicin and dibekacin. Sulbenicillin-resistant strains of P. aeruginosa were moderately resistant to SCE-129, whether these strains were gentamicin-resistant or not. Gentamicin-resistant strains of P. aeruginosa were resistant to dibekacin but not to SCE-129. Against P. maltophilia, the minimum inhibitory concentration of SCE-129 resembled those of sulbenicillin, gentamicin, and dibekacin. Most strains of P. cepacia were moderately resistant to SCE-129 and sulbenicillin and highly resistant to gentamicin and dibekacin.  (+info)

Cross-resistance to meropenem, cephems, and quinolones in Pseudomonas aeruginosa. (3/46)

Multiple-drug-resistant mutants were isolated from Pseudomonas aeruginosa PAO1 on agar plates containing ofloxacin and cefsulodin. These mutants were four to eight times more resistant to meropenem, cephems, carbenicillin, quinolones, tetracycline, and chloramphenicol than the parent strain was. In contrast, these mutants showed no significant changes in their susceptibilities to all carbapenems except meropenem. In these mutants, the amounts of an outer membrane protein with an apparent molecular weight of 49,000 (designated OprM) were increased compared with the amount in PAO1. Multiple-drug-resistant mutants of this type were also isolated from PAO1 on agar plates containing meropenem. Approximately 5% of clinical isolates showed cross-resistance to meropenem, cephems, and quinolones, concomitant with overproduction of OprM. Moreover, these two phenotypes, i.e., multiple-drug resistance and overproduction of OprM, were cotransferable by transduction. These data suggest that overproduction of OprM is associated with cross-resistance to meropenem, cephems, and quinolones in P. aeruginosa. The ofloxacin-cefsulodin-resistant mutant required higher concentrations of meropenem to induce beta-lactamase than PAO1 did, indicating the possibility that this mutation involves decreased outer membrane permeability to meropenem.  (+info)

Unstable Escherichia coli L forms revisited: growth requires peptidoglycan synthesis. (4/46)

Growing bacterial L forms are reputed to lack peptidoglycan, although cell division is normally inseparable from septal peptidoglycan synthesis. To explore which cell division functions L forms use, we established a protocol for quantitatively converting a culture of a wild-type Escherichia coli K-12 strain overnight to a growing L-form-like state by use of the beta-lactam cefsulodin, a specific inhibitor of penicillin-binding proteins (PBPs) 1A and 1B. In rich hypertonic medium containing cefsulodin, all cells are spherical and osmosensitive, like classical L forms. Surprisingly, however, mutant studies showed that colony formation requires d-glutamate, diaminopimelate, and MurA activity, all of which are specific to peptidoglycan synthesis. High-performance liquid chromatography analysis confirmed that these L-form-like cells contain peptidoglycan, with 7% of the normal amount. Moreover, the beta-lactam piperacillin, a specific inhibitor of the cell division protein PBP 3, rapidly blocks the cell division of these L-form-like cells. Similarly, penicillin-induced L-form-like cells, which grow only within the agar layers of rich hypertonic plates, also require d-glutamate, diaminopimelate, and MurA activity. These results strongly suggest that cefsulodin- and penicillin-induced L-form-like cells of E. coli-and possibly all L forms-have residual peptidoglycan synthesis which is essential for their growth, probably being required for cell division.  (+info)

The Rcs phosphorelay is a cell envelope stress response activated by peptidoglycan stress and contributes to intrinsic antibiotic resistance. (5/46)

 (+info)

Cell cycle-independent lysis of Escherichia coli by cefsulodin, an inhibitor of penicillin-binding proteins 1a and 1b. (6/46)

Cefsulodin lyses actively growing Escherichia coli by binding specifically to penicillin-binding proteins (PBPs) 1a and 1b. Recent findings (F. Garcia del Portillo, M. A. de Pedro, D. Joseleau-Petit, and R. D'Ari, J. Bacteriol. 171:4217-4221, 1989) have linked cefsulodin-induced lysis to septation during the first division cycle after a nutritional shift-up or chromosome replication realignment. We synchronized cells by membrane filtration to determine whether cefsulodin-induced lysis depended on septation in normally growing cells. Populations of newly divided cells were allowed to grow for variable lengths of time. Cefsulodin was added to these synchronous cultures, which represented points in two to three rounds of the cell cycle. Since the cell numbers were small, a new lysis assay was developed that was based on the release of DNA measured by fluorometry. Lysis occurred at a constant time after addition of the antibiotic, regardless of the time in the cell cycle at which the addition was made. Thus, cefsulodin-induced lysis is not linked to septation or to any other cell cycle-related event.  (+info)

Lysis of Escherichia coli by beta-lactams which bind penicillin-binding proteins 1a and 1b: inhibition by heat shock proteins. (7/46)

The heat shock proteins (HSPs) of Escherichia coli were artificially induced in cells containing the wild-type rpoH+ gene under control of a tac promoter. At 30 degrees C, expression of HSPs produced cells that were resistant to lysis by cephaloridine and cefsulodin, antibiotics that bind penicillin-binding proteins (PBPs) 1a and 1b. This resistance could be reversed by the simultaneous addition of mecillinam, a beta-lactam that binds PBP 2. However, even in the presence of mecillinam, cells induced to produce HSPs were resistant to lysis by ampicillin, which binds all the major PBPs. Lysis of cells induced to produce HSPs could also be effected by imipenem, a beta-lactam known to lyse nongrowing cells. These effects suggest the existence of at least two pathways for beta-lactam-dependent lysis, one inhibited by HSPs and one not. HSP-mediated lysis resistance was abolished by a mutation in any one of five heat shock genes (dnaK, dnaJ, grpE, GroES, or groEL). Thus, resistance appeared to depend on the expression of the complete heat shock response rather than on any single HSP. Resistance to lysis was significant in the absence of the RelA protein, implying that resistance could not be explained by activation of the stringent response. Since many environmental stresses promote the expression of HSPs, it is possible that their presence contributes an additional mechanism toward development in bacteria of phenotypic tolerance to beta-lactam antibiotics.  (+info)

Isolation of Neisseria meningitidis mutants deficient in class 1 (porA) and class 3 (porB) outer membrane proteins. (8/46)

The class 1 major outer membrane protein of Neisseria meningitidis is a serious candidate for a meningococcal vaccine. To facilitate studies on the function of this protein, mutants were isolated that lacked this protein or the structurally related class 3 protein. These mutants were obtained by using the antibody-dependent bactericidal action of the complement system. The class 1 protein-deficient strain grew normally in vitro, whereas growth of the class 3 protein-deficient strain was slightly retarded. The class 3 protein-deficient strain displayed increased resistance to the antibiotics tetracycline and cefsulodin, which is consistent with the proposed role of the protein as a pore-forming protein. The class 1 protein was purified to homogeneity from the class 3 protein-deficient strain. Lipid bilayer experiments revealed that this protein also formed pores. The class 1 protein pores were cation selective.  (+info)

... is most commonly used in cefsulodin-irgasan-novobiocin agar to select for Yersinia microorganisms. This agar is most ... Cefsulodin is a third-generation cephalosporin antibiotic that is active against Pseudomonas aeruginosa and was discovered by ... "BAM Media M35: Cefsulodin-Irgasan Novobiocin Agar or Yersinia Selective Agar". Food and Drug Administration. Retrieved 2 ... "Cefsulodin , the Antimicrobial Index Knowledgebase - TOKU-E". (CS1: long volume value, Articles with changed EBI identifier, ...
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If Yersinia infection is suspected, the clinical laboratory should be notified and instructed to culture on cefsulodin-irgasan- ... CDC recommends the use of cefsulodin-irgasan-novobiocin (CIN) agar for isolation of Yersinia spp. from nonsterile sites. ...
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This led to the discovery of cefsulodin as an inhibitor of SHP2, an oncogenic phosphatase in the PTP family. Crystal structure ... analysis of SHP2 interaction with cefsulodin identified sulfophenyl acetic amide (SPAA) as a novel phosphotyrosine (pTyr) ...
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Mester, U.; Krasemann, C.; Werner, H. 1982: Cefsulodin concentrations in rabbit eyes after intravenous and subconjunctival ...
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Cefsulodin Sodium Narrower Concept UI. M0330934. Registry Number. 2D087186PY. Terms. Cefsulodin Sodium Preferred Term Term UI ... Cefsulodin Monosodium Salt Cefsulodin Sodium Monaspor Pyocefal SCE-129 Pharm Action. Anti-Bacterial Agents. Registry Number. ... Cefsulodin Monosodium Salt Term UI T361128. Date09/13/1999. LexicalTag NON. ThesaurusID NLM (1999). ... Cefsulodin Preferred Term Term UI T007115. Date01/01/1999. LexicalTag NON. ThesaurusID ...
Cefsulodin Sodium Narrower Concept UI. M0330934. Registry Number. 2D087186PY. Terms. Cefsulodin Sodium Preferred Term Term UI ... Cefsulodin Monosodium Salt Cefsulodin Sodium Monaspor Pyocefal SCE-129 Pharm Action. Anti-Bacterial Agents. Registry Number. ... Cefsulodin Monosodium Salt Term UI T361128. Date09/13/1999. LexicalTag NON. ThesaurusID NLM (1999). ... Cefsulodin Preferred Term Term UI T007115. Date01/01/1999. LexicalTag NON. ThesaurusID ...
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Hydrolysis of cefsulodin was not detectable in assays used and enzyme binding (Ki) was poor, ensuring a very low physiological ... Cefsulodin MICs against SAI+ and SAI- organisms were similar and no difference existed in activity, over long periods against ... aeruginosa strains but cefsulodin against only a minority (2/14). Cephaloridine/cefotaxime antagonism was lost in uninducible ( ... Overall, results indicated that SA enzyme, if induced, constituted a defense against cefotaxime but not cefsulodin and this ...
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  • CDC recommends the use of cefsulodin-irgasan-novobiocin (CIN) agar for isolation of Yersinia spp. (cdc.gov)
  • blood agar supplemented with ampicillin and a selective media, CIN (cefsulodin-irgasan-novobioci) agar, were used. (cdc.gov)
  • Under the low-power magnification of 10X, using a digital Keyence scope, this photograph depicts the colonial growth displayed by Gram-negative, Yersinia pseudotuberculosis bacteria, which were cultured on a Cefsulodin-Irgasan-Novobiocin (CIN) agar medium, for a 24-hour time period, at a temperature of 37 ° C. (cdc.gov)
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  • If Yersinia infection is suspected, the clinical laboratory should be notified and instructed to culture on cefsulodin-irgasan-novobiocin (CIN) or other specific for growing it. (cdc.gov)