Last edited by Mut

2 edition of Beta-lactamase as a vehicle for the secretion of foreign gene products found in the catalog.

Beta-lactamase as a vehicle for the secretion of foreign gene products

Elizabeth S Haas

Beta-lactamase as a vehicle for the secretion of foreign gene products

by Elizabeth S Haas

  • 10 Want to read
  • 39 Currently reading

Published .
Written in English

    Subjects:
  • Beta lactamases,
  • Molecular cloning

  • Edition Notes

    Statementby Elizabeth S. Haas
    The Physical Object
    Pagination34 leaves :
    Number of Pages34
    ID Numbers
    Open LibraryOL14630963M

    Fusobacterium nucleatum (Fn) is generally an opportunistic oral pathogen that adheres to mammalian mucosal sites, triggering a host inflammatory response. In general, Fn is normally found within the human oral cavity; however, it was previously reported that Fn is a risk factor for certain respiratory diseases. Surprisingly, this was never fully elucidated. Here, we investigated the virulence. Streptomyces clavuligerus is a filamentous Gram-positive bacterial producer of the β-lactamase inhibitor clavulanic acid. Antibiotics biosynthesis in the Streptomyces genus is usually triggered by nutritional and environmental perturbations. In this work, a new genome scale metabolic network of Streptomyces clavuligerus was reconstructed and used to study the experimentally observed.

    HB cells that have been successfully transformed with the pGLO plasmid will constitutively (continuously) produce a product (beta-lactamase) that will cleave the ampicillin and render it useless as an antibiotic. The beta lactamase is the product of the AmpR gene of the pGLO plasmid. In the K. pneumoniae YC isolate from the United States, the beta-lactamase bla KPC-2 gene was located on a novel Tn3-based transposon, Tn Tn was 10 kb in size, was delimited by two bp imperfect inverted repeat sequences, and harbored, in addition to the beta-lactamase bla KPC-2 gene, a transposase gene, a resolvase gene, and two.

    The plasmid-encoded, constitutively produced $\beta$-lactamase gene from Enterococcus faecalis strain HH22 was genetically characterized. A restriction endonuclease map of the kb EcoRI fragment encoding the enterococcal $\beta$-lactamase was prepared and compared with the restriction map of a cloned staphylococcal $\beta$-lactamase gene (from the naturally-occurring staphylococcal $\beta. Learn beta lactamase with free interactive flashcards. Choose from different sets of beta lactamase flashcards on Quizlet.


Share this book
You might also like
Sulfur dyes from India

Sulfur dyes from India

The Fireside Book of Fun and Game Songs

The Fireside Book of Fun and Game Songs

Deadmans Cave

Deadmans Cave

The forms of autobiography

The forms of autobiography

A devil and her love song

A devil and her love song

Communists and national unity

Communists and national unity

In the trenches with the 9th Devons

In the trenches with the 9th Devons

Clue for murder.

Clue for murder.

The Lost Ones

The Lost Ones

house divided

house divided

Onto a comprehensive employment service.

Onto a comprehensive employment service.

Statistical models for the evaluation and interpretation of educational criteria

Statistical models for the evaluation and interpretation of educational criteria

Brownsville

Brownsville

All of Us Are Dying and Other Stories

All of Us Are Dying and Other Stories

Beta-lactamase as a vehicle for the secretion of foreign gene products by Elizabeth S Haas Download PDF EPUB FB2

The reaction is partly diffusion controlled and the rate constants are such that there is no single RDS for β-lactamase action (Table ), a sign of fully efficient enzymes with good r class A enzyme, β-lactamase I of B.

cereus, has rate constants for benzylpenicillin similar to those of TEM β-lactamase and S. aureus β-lactamase PCI (29, 30).

Beta-lactamases are enzymes (EC ) produced by bacteria that provide multi-resistance to β-lactam antibiotics such as penicillins, cephalosporins, cephamycins, and carbapenems (), although carbapenems are relatively resistant to beta-lactamase.

Beta-lactamase provides antibiotic resistance by breaking the antibiotics' structure. These antibiotics all have a common element in their InterPro: IPR   Gene ID:updated on 5-Jan Summary.

This gene encodes a mitochondrially-localized protein that has sequence similarity to prokaryotic beta-lactamases. Many of the residues responsible for beta-lactamase activity are not conserved in this protein, suggesting it may have a different enzymatic function.

In transformed minicells from B. subtilis, the products of alpha-amylase, beta-lactamase, and E1 genes accumulated at similar rates. We conclude that the expression of the three genes cloned in the secretion vector was similar at the levels of transcription and translation in B.

by:   Immunofluorescence microscopy, the accessibility of the fusion protein to externally added proteases, and the rates of hydrolysis of nitrocefin and penicillin G by whole cells demonstrated that a substantial fraction (%) of the beta-lactamase domain of the fusion protein was exposed on the external surface of E.

by: Some antimicrobials (eg, cefazolin and cloxacillin) are naturally resistant to certain beta-lactamases. The activity of the beta-lactams: amoxicillin, ampicillin, piperacillin, and ticarcillin, can be restored and widened by combining them with a beta-lactamase inhibitor.

Clavulanic acid, sulbactam, and tazobactam are all beta-lactamase inhibitors. Cell. Jul;20(3) Secretion of beta-lactamase requires the carboxy end of the protein.

Koshland D, Botstein D. Synthesis and secretion of beta-lactamase were studied in Salmonella typhimurium infected with P22 phage carrying the structural gene for beta-lactamase (the bla gene) in mutant or wild-type form. Synthesis and secretion of β-lactamase were studied in Salmonella typhimurium infected with P22 phage carrying the structural gene for β-lactamase (the bla gene) in mutant or wild-type form.

The wild-type gene was shown to specify two forms of β-lactamase which differ in molecular weight by about daltons. This difference is consistent with removal, predicted on other grounds, of Plasmid Beta-Lactamase from Dr.

Niels Geijsen's lab contains the insert Beta-Lactamase and is published in Cell. Apr 23;(3) doi: / This plasmid is available through Addgene.

The structural part of Bacillus licheniformis α-amylase gene and a L. lactis secretion signal sequence were amplified by PCR from pGAL9 plasmid using AL93 (5'AAT-GAGAGCATTAATGTTTC) and. Xanthomonas campestris is one of bacteria carrying a type III secretion system which transports their effector proteins into host plant cells to disturb host defense system for their infection.

To establish a genome editing system without introducing any foreign gene, we attempted to introduce genome editing enzymes through the type III secretion system.

In a test of protein transfer, X. An in frame gene fusion containing the coding region for mature beta-lactamase and the 3'-end of hylA encoding the haemolysin secretion signal, was constructed under the control of a lac promoter.

The resulting 53 kDa hybrid protein was specifically secreted to the external medium in the presence of the haemolysin translocator proteins, HlyB. In fact, beta-lactamase is the main mechanism of clinical resistance against many beta-lactam compounds, even at the present time.

At the same time, however, these enzymes are also produced by nonpathogenic bacteria such as Streptomyces (2,3) and the cyanobacteria (4). The role of the beta-lactamase signal sequence in the secretion of proteins by Escherichia coli. J T Kadonaga, contains both a unique EcoRI restriction site right at the beginning of the signal codons of the beta-lactamase (bla) gene and a unique BstEII site just at the end of the bla signal codons.

Although the signal peptide encoded by. Some bacteria have developed resistance to these now by producing beta-lactamase - which breaks down the DD-transpeptidase causing it to be ineffective. This ability has spread though the mixing of bacterial genes, which occurs though a number of mechanisms including gene transfer and 'picking up' genes from lysed cells.

Suicide gene therapy consist in the incorporation of a foreign gene, which encodes for an enzyme, that metabolizes a non-toxic prodrug into a toxic metabolite capable to kill the tumoral cell. The phase I research studied a recombinant Ad that carries a suicide gene (TK, presumably) and a reporter gene and infects patients with ovarian and.

The pIN-II and pIN-III vectors produce the foreign gene product only in the presence of an inducer. Once a gene has been inserted properly into one of these vectors it can easily be moved to the other vectors, like a cassette, with the use of several possible unique restriction-enzyme sites on either side of the gene.

Liras, J.F. Martín, in Encyclopedia of Microbiology (Third Edition), β-Lactam antibiotics are one of the best tools in the fight against bacterial infections. The resistance of many bacteria has been overcome by the introduction of novel β-lactams and the combination of classical penicillins (particularly amoxicillin) with clavulanic acid, a β-lactamase inhibitor.

Tn was 10 kb in size, was delimited by two bp imperfect inverted repeat sequences, and harbored, in addition to the beta-lactamase bla KPC-2 gene, a transposase gene, a resolvase gene, and two novel insertion sequences, ISKpn6 and ISKpn7.

Tn has been identified in all isolates. Beta-Lactamase and Ambler classification. β-lactamase enzymes are capable of hydrolysing the β-lactam rings (the active site) of β-lactam antibiotics; thereby deactivating their antibacterial properties.

It is observed in both gram-positive and gram-negative bacteria. This book is an excellent one. I recommend it strongly for bacteriologists and biochemists or chemists involved in design of novel molecules, or working in the mechanism of action of beta-lactams (penicillins and related molecules).

I repeat: excellent book, Roger Labia s: 2.Antibiotics can damage the gut microbiome leading to opportunistic infections and the emergence of antibiotic resistance. Microbiome protection via antibiotic inactivation in the gastrointestinal (GI) tract represents a strategy to limit antibiotic exposure of the colonic microbiota.

Proof of concept for this approach was achieved with an orally-administered beta-lactamase enzyme, SYNfrom book Bacterial Protein Secretion utilizes fusions of effector genes to the beta-lactamase reporter gene, positioned under the effector's native promoter and chromosomal location.