Disease relevance of Serratia

• Deletions were generated in vitro in the leader region of the tryptophan operon of Serratia marcescens and subsequently incorporated into the Escherichia coli chromosome in single copy form [1].
• In striking contrast, retinol-depleted rats immunized with lipopolysaccharides from Pseudomonas aeruginosa and Serratia marcesens produced an antibody response indistinguishable from retinol-sufficient animals [2].
• A comparison of the NH2-terminal sequence of the enzyme with the (previously determined) homologue from Serratia marcescens, a monomer with a molecular weight of 45,000, showed that the larger Serratia subunit came into register with amino acid 14 of the Erwinia subunit [3].
• Resistance can develop in methicillin-resistant Staphylococcus aureus, Pseudomonas aeruginosa, and Serratia marcescens, albeit infrequently [4].
• Several of these new antibiotics have an exceedingly broad spectrum of activity that includes Pseudomonas aeruginosa, as well as Enterobacteriaceae, Serratia, Citrobacter, indole-positive Proteus, and anaerobes (including Bacteroides fragilis) [5].

High impact information on Serratia

• Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase [6].
• Superattenuation in the tryptophan operon of Serratia marcescens [1].
• Investigation suggested that pediatric-sized vacuum tubes containing ethylenediamine tetraacetic acid (EDTA) were the source of the organisms, and the epidemic strain of Serratia was recovered from 41 (35%) of the 116 tubes cultured [7].
• When anti-Gal bound onto the lipopolysaccharide of a representative blood isolate, Serratia marcescens #21, it blocked its alternative complement pathway (ACP) lysis and made the organism serum resistant [8].
• In contrast, when anti-Gal bound to the capsular polysaccharide of a serum sensitive Serratia, #7, it increased ACP killing of this strain [8].

Chemical compound and disease context of Serratia

• The mechanism of blockade of ACP lysis by anti-Gal did not involve a decrease in the number of C3 molecules deposited onto Serratia #21 or an inhibition of the binding of C3b to its LPS, nor did it change the iC3b and C3d degradation products of bound C3b or prevent membrane attack complex formation on this organism [8].
• Gentamicin-resistant Serratia [9].
• Serratia sensitivity to ampicillin and tetracycline was an epidemiological marker of a common-source outbreak [10].
• The crystal structure of anthranilate synthase (AS) from Serratia marcescens, a mesophilic bacterium, has been solved in the presence of its substrates, chorismate and glutamine, and one product, glutamate, at 1.95 A, and with its bound feedback inhibitor, tryptophan, at 2.4 A [11].
• The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan [11].

Biological context of Serratia

• DNA sequence of the Serratia marcescens lipoprotein gene [12].
• However, Serratia treatment almost completely abolished the increase in platelet surface GMP-140 induced by low concentrations of alpha-thrombin (0.5 nmol/L) and diminished the downregulation of platelet surface GPIX by 60.9% +/- 5.6% (mean +/- SEM, n = 3) [13].
• Human fibroblast collagenase contains an amino acid sequence homologous to the zinc-binding site of Serratia protease [14].
• The aspartate transcarbamoylases (ATCase) from Serratia marcescens and Escherichia coli exhibit unique regulatory and kinetic properties and were dissociated into their constituent regulatory and catalytic subunits [15].
• Previously, we constructed a plasmid in which the ColE1 RNAI was separated from the primer and placed under transcriptional control of the Serratia marcesens tryptophan promoter [16].

Anatomical context of Serratia

• Treatment of Serratia polyribosomes with RNase or pronase reduced the number of survivors [17].
• We evaluated the safety, efficacy, and microbiologic activity of combination amdinocillin and cefoxitin treatment in 17 patients with complicated urinary tract infections caused by multiply-resistant Serratia marcescens [18].
• Lysozyme-tris-EDTA spheroplast preparations of the Serratia isolates were also tested for potassium ion leakage following exposure to chlorhexidine and it was found that the inner membrane was responsible for the decreased susceptibility of the organism of chlorhexidine [19].
• The anticomplement properties of two chromatographically distinct fractions of a phenol-extracted lipopolysaccharide isolated from Serratia marcescens were assessed by means of the standard sheep erythrocyte hemolytic assay and an alternative pathway-selective kinetic assay using rabbit erythrocytes [20].
• Substrates with extreme structural features, like poly(dA).poly(dT) or poly(dG).poly(dC), are cleaved by the Serratia nuclease with a 50 times higher or 10 times lower K(m), respectively, as salmon testis DNA [21].

Gene context of Serratia

• The cecropin genes were also induced when the flies were kept on food with the Drosophila pathogenic bacterium Serratia marcescens Db10 or its non-pathogenic derivative Db1140 [22].
• Flow cytometric studies, using a panel of monoclonal antibodies (MoAbs), showed that Serratia marcescens protease treatment removed greater than 97% of the glycocalicin portion of GPIb but did not affect the changes in the expression of GPIX or GMP-140 that were induced by high concentrations of alpha-thrombin (10 nmol/L) [13].
• Experiments with Serratia protease-treated and Bernard-Soulier platelets showed that neither platelet surface GPIb nor cathepsin G-induced proteolysis of GPIb were required for the cathepsin G-induced redistribution of the remnant of the GPIb-IX complex or the cathepsin G-induced increase in platelet surface P-selectin [23].
• Three distinct fragments, the 38-kDa fragment produced by Serratia marcescens protease as well as the 45- and 35-kDa fragments produced by trypsin, had the same NH2 terminus as the intact GPIb alpha-chain (apparent molecular mass = 140 kDa) [24].
• The regulatory significance of these sequence features is discussed with respect to the rbs operon. rbsK has been cloned downstream from the Serratia marcescens trp promoter on a multicopy plasmid [25].

Analytical, diagnostic and therapeutic context of Serratia

• Analysis of sequence alignments between the recently published sequence of human fibroblast collagenase and a computer file of published protease sequences has revealed a previously unrecognized homology to the 11 amino acids flanking the zinc-binding site of Serratia protease, a bacterial metalloprotease [14].
• The Serratia marcescens haemophore (HasA) is folded into a globular form and tyrosine and histidine are involved in haem ligation [26].
• Using high-performance liquid chromatography (HPLC), high resolution mass spectrometry and nuclear magnetic resonance (NMR) spectroscopy, we identified N-butanoyl-L-homoserine lactone (BHL) and N-hex anoyl-L-homoserine lactone (HHL) in cell-free Serratia culture supernatants [27].
• Cloning and sequence analysis of the gene for a carbapenem-hydrolyzing class A beta-lactamase, Sme-1, from Serratia marcescens S6 [28].
• In a multicenter study, the MICs of FK-037 for 90% of the strains tested (MIC90s) were < or = 1 microgram/ml for members of the family Enterobacteriaceae other than Citrobacter freundii, Enterobacter spp., and Serratia marcescens [29].

References