Replication of the ampicillin resistance plasmid RSF1030 in extracts of Escherichia coli: Separation of the replication cycle into early and late stages

1977 ◽  
Vol 156 (1) ◽  
pp. 27-34 ◽  
Author(s):  
Walter L. Staudenbauer
Keyword(s):  
Escherichia Coli ◽  
Replication Cycle ◽  
Ampicillin Resistance ◽  
Resistance Plasmid ◽  
Late Stages

Clarification of the structure of the ampicillin-resistance plasmid RSF0885 from Haemophilus influenzae HR-885 serotype b

1994 ◽  
Vol 40 (2) ◽  
pp. 154-157 ◽  
Author(s):  
W. L. Albritton ◽  
P. A. Noble ◽  
K. D. Webster
Keyword(s):  
Escherichia Coli ◽  
Haemophilus Influenzae ◽  
Sequencing Data ◽  
Original Source ◽  
Ampicillin Resistance ◽  
Resistance Plasmid ◽  
Haemophilus Parainfluenzae ◽  
Serotype B ◽  
Restriction Enzyme Maps

The nonconjugative ampicillin-resistance plasmid RSF0885 has been reported to be as small as 2.9 MDa and as large as 4.1 MDa with at least two restriction enzyme maps reported. In addition, the source of the original plasmid has been reported to be Haemophilus influenzae and Haemophilus parainfluenzae. Characterization of the source strains and sequencing data of the plasmids revealed that H. influenzae serotype b was the original source strain and that ISI-K in the larger plasmid was presumably acquired when the smaller plasmid was maintained in Escherichia coli in S. Falkow's laboratory during the late 1970s.Key words: Haemophilus influenzae, Haemophilus parainfluenzae, RSF0885, ampicillin resistance, ISI-K

scholarly journals Specific phenotypic, genomic, and fitness evolutionary trajectories toward streptomycin resistance induced by pesticide co-stressors in Escherichia coli

2021 ◽  
Vol 1 (1) ◽  
Author(s):  
Yue Xing ◽  
Xiaoxi Kang ◽  
Siwei Zhang ◽  
Yujie Men
Keyword(s):  
Escherichia Coli ◽  
Antibiotic Resistance ◽  
Selective Pressure ◽  
Fold Increase ◽  
Streptomycin Resistance ◽  
Evolutionary Stage ◽  
Fitness Costs ◽  
Evolutionary Trajectories ◽  
K 12 ◽  
Late Stages

AbstractTo explore how co-occurring non-antibiotic environmental stressors affect evolutionary trajectories toward antibiotic resistance, we exposed susceptible Escherichia coli K-12 populations to environmentally relevant levels of pesticides and streptomycin for 500 generations. The coexposure substantially changed the phenotypic, genotypic, and fitness evolutionary trajectories, resulting in much stronger streptomycin resistance (>15-fold increase) of the populations. Antibiotic target modification mutations in rpsL and rsmG, which emerged and dominated at late stages of evolution, conferred the strong resistance even with less than 1% abundance, while the off-target mutations in nuoG, nuoL, glnE, and yaiW dominated at early stages only led to mild resistance (2.5–6-fold increase). Moreover, the strongly resistant mutants exhibited lower fitness costs even without the selective pressure and had lower minimal selection concentrations than the mildly resistant ones. Removal of the selective pressure did not reverse the strong resistance of coexposed populations at a later evolutionary stage. The findings suggest higher risks of the selection and propagation of strong antibiotic resistance in environments potentially impacted by antibiotics and pesticides.

Large-scale production of citrate synthase from a cloned gene

1982 ◽  
Vol 60 (12) ◽  
pp. 1143-1147 ◽  
Author(s):  
Harry W. Duckworth ◽  
Alexander W. Bell
Keyword(s):  
Escherichia Coli ◽  
Large Scale ◽  
Citrate Synthase ◽  
Specific Activity ◽  
Tetracycline Resistance ◽  
Scale Production ◽  
Ampicillin Resistance ◽  
Colicin E1 ◽  
Large Scale Production ◽  
Cloned Gene

Starting with a colicin E1 resistance recombinant plasmid which contains gltA, the gene for citrate synthase in Escherichia coli, we have constructed an ampicillin-resistance plasmid containing the gltA region as a 2.9-kilobase-pair insert in the tetracycline-resistance region of pBR322. Escherichia coli HB101 harbouring this plasmid, when grown on rich medium containing ampicillin, contains citrate synthase as about 8% of its soluble protein. The enzyme has been purified from this rich source and is identical to the chromosomal enzyme prepared previously in every property tested, except for specific activity, which is 64 U∙mg−1 as compared with 45–50 U∙mg−1 previously obtained. The N-terminal sequences of both enzymes are reported, and they are identical up to residue 16 at least. The overall yield of pure enzyme, starting with the cells grown in 15 L of medium, is 600–800 mg.

scholarly journals Human cytomegalovirus exploits TACC3 to control microtubule dynamics and late stages of infection

2021 ◽  
Author(s):  
Colleen Furey ◽  
Helen Astar ◽  
Derek Walsh
Keyword(s):  
Virus Replication ◽  
Human Cytomegalovirus ◽  
Coiled Coil ◽  
Microtubule Dynamics ◽  
Replication Cycle ◽  
Microtubule Organizing Center ◽  
Viral Particles ◽  
Organizing Center ◽  
Assembly Compartment ◽  
Late Stages

While it is well established that microtubules (MTs) facilitate various stages of virus replication, how viruses actively control MT dynamics and functions remains less-well understood. Recent work has begun to reveal how several viruses exploit End-Binding (EB) proteins and their associated microtubule plus-end tracking proteins (+TIPs), in particular to enable loading of viral particles onto MTs for retrograde transport during early stages of infection. But distinct from other viruses studied to date, at mid-to-late stages of its unusually protracted replication cycle human cytomegalovirus (HCMV) increases the expression of all three EB family members. This occurs coincident with the formation of a unique structure termed the Assembly Compartment (AC), which serves as a Golgi-derived MT organizing center. Together, the AC and distinct EB proteins enable HCMV to increase the formation of dynamic and acetylated microtubule subsets to regulate distinct aspects of the viral replication cycle. Here, we reveal that HCMV also exploits EB-independent +TIP pathways by specifically increasing the expression of Transforming Acidic Coiled Coil protein 3 (TACC3) to recruit the MT polymerase, chTOG from initial sites of MT nucleation in the AC out into the cytosol, thereby increasing dynamic MT growth. Preventing TACC3 increases or depleting chTOG impaired MT polymerization, resulting in defects in early versus late endosome organization in and around the AC as well as defects in viral trafficking and spread. Our findings provide the first example of a virus that actively exploits EB-independent +TIP pathways to regulate MT dynamics and control late stages of virus replication. Importance Diverse viruses rely on host cell microtubule networks in order to transport viral particles within the dense cytoplasmic environment and to control the broader architecture of the cell to facilitate their replication. Yet precisely how viruses regulate the dynamic behavior and function of microtubule filaments remains poorly defined. We recently showed that the Assembly Compartment (AC) formed by human cytomegalovirus (HCMV) acts as a Golgi-derived microtubule organizing center. Here, we show that at mid-to-late stages of infection, HCMV increases the expression of Transforming Acidic Coiled Coil protein 3 (TACC3) in order to control the localization of the microtubule polymerase, chTOG. This in turn enables HCMV to generate dynamic microtubule subsets that organize endocytic vesicles in and around the AC and facilitate the transport of new viral particles released into the cytosol. Our findings reveal the first instance of viral targeting of TACC3 to control microtubule dynamics and virus spread.

Effects of Halides on Plasmid-Mediated Silver Resistance in Escherichia coli

1998 ◽  
Vol 64 (12) ◽  
pp. 5042-5045 ◽  
Author(s):  
Amit Gupta ◽  
Maria Maynes ◽  
Simon Silver
Keyword(s):  
Escherichia Coli ◽  
Growth Medium ◽  
Silver Sulfadiazine ◽  
Resistance Plasmid ◽  
Low Concentrations ◽  
Resistant Strains ◽  
High Concentrations

ABSTRACT Silver resistance of sensitive Escherichia coli J53 and resistance plasmid-containing J53(pMG101) was affected by halides in the growth medium. The effects of halides on Ag+ resistance were measured with AgNO3 and silver sulfadiazine, both on agar and in liquid. Low concentrations of chloride made the differences in MICs between sensitive and resistant strains larger. High concentrations of halides increased the sensitivities of both strains to Ag+.

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