Analysis of outer membrane proteome of <b><i>Escherichia coli</i></b> related to resistance to ampicillin and tetracycline

Xu, Changxin; Lin, Xiangmin; Ren, Haixia; Zhang, Yueling; Wang, Sanying; Peng, Xuan‐xian

doi:10.1002/pmic.200500219

Cited by 118 publications

(132 citation statements)

References 51 publications

Supporting

Mentioning

125

Contrasting

Unclassified

Order By: Relevance

“…The deletion of BamC also has no physiological effect on the targeting of OMP proteins (11). From previous observations, it appears that this factor may be involved in the response to rifampin (specific for RNA polymerase), tetracycline (ribosome), and ampicillin (␤-lactamase) resistance (15). Some of these functions are reoccurring as functional attributes of the BamE protein (see below).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Structural Basis of Outer Membrane Protein Biogenesis in Bacteria

Albrecht

Zeth

2011

Journal of Biological Chemistry

104

View full text Add to dashboard Cite

In Escherichia coli, a multicomponent BAM (␤-barrel assembly machinery) complex is responsible for recognition and assembly of outer membrane ␤-barrel proteins. The functionality of BAM in protein biogenesis is mainly orchestrated through the presence of two essential components, BamA and BamD. Here, we present crystal structures of four lipoproteins (BamB-E). Monomeric BamB and BamD proteins display scaffold architectures typically implied in transient protein interactions. BamB is a ␤-propeller protein comprising eight WD40 repeats. BamD shows an elongated fold on the basis of five tetratricopeptide repeats, three of which form the scaffold for protein recognition. The rod-shaped BamC protein has evolved through the gene duplication of two conserved domains known to mediate protein interactions in structurally related complexes. By contrast, the dimeric BamE is formed through a domain swap and indicates fold similarity to the ␤-lactamase inhibitor protein family, possibly integrating cell wall stability in BAM function. Structural and biochemical data show evidence for the specific recognition of amphipathic sequences through the tetratricopeptide repeat architecture of BamD. Collectively, our data advance the understanding of the BAM complex and highlight the functional importance of BamD in amphipathic outer membrane ␤-barrel protein motif recognition and protein delivery.Gram-negative bacteria are surrounded by two membranes, an inner membrane and the protective outer membrane (OM) 2 layer. The outer membrane architecture is highly asymmetric and composed by integral outer membrane ␤-barrel proteins, lipoproteins, lipopolysaccharides, and phospholipids (1). These components are entirely synthesized in the cytoplasm, translocated over the inner membrane, and finally delivered through the periplasm to the outer membrane by specific shuttle factors that transport their cargo to membrane receptor complexes (1, 2). In Escherichia coli, lipoproteins are targeted to the OM through the LolABCDE complex system via a series of membrane and periplasmic transfer steps (3, 4). Integral OMPs are translocated by the secretion (Sec) machinery and stabilized against premature precipitation or mislocalization in the periplasm by the three major chaperones PpiD, Skp, and SurA (4 -7). These chaperones presumably act sequentially with PpiD at an early stage, early after the OMP release into the periplasm (5). This initial rescue event is followed by Skp and SurA chaperoning at a later stage (8). Various experimental studies describing OMP folding through SurA show the particular importance of this chaperone. Phage display combined with peptide binding studies indicated SurA interactions with amphipathic OMP peptides (9, 10). Furthermore, the importance of SurA in vivo is underlined by the observation that E. coli cells being deleted in surA exhibit reduced levels of folded OmpA, OmpC, OmpF, and LamB porins (11).After the unfolded outer membrane protein is delivered through the periplasmic space, the final steps are the tetherin...

show abstract

Section: Discussionmentioning

confidence: 99%

“…These lipoproteins express a rather unspecific influence on the stability of the complex (BamE) and the kinetic folding of selected OMP proteins (BamB, e.g. on the monomer/trimer transition of LamB) (13)(14)(15).…”

mentioning

confidence: 99%

Structural Basis of Outer Membrane Protein Biogenesis in Bacteria

Albrecht

Zeth

2011

Journal of Biological Chemistry

104

View full text Add to dashboard Cite

show abstract

“…Contamination of membrane fractions with cytosolic proteins is not uncommon. Several studies reported that proteins spots other than membrane proteins were identified by 2-DE of membrane protein extracts (40,45,60). Rhomberg et al identified 53 proteins from the sarcosin-insoluble outer membrane fraction, and among them, 37 were cytoplasmic or of unknown subcellular origin (45).…”

Section: Vol 73 2007mentioning

confidence: 99%

Characterization of an Escherichia coli O157:H7 Plasmid O157 Deletion Mutant and Its Survival and Persistence in Cattle

Lim

Sheng

Seo

et al. 2007

Appl Environ Microbiol

View full text Add to dashboard Cite

Escherichia coli O157:H7 causes hemorrhagic colitis and hemolytic-uremic syndrome in humans, and its major reservoir is healthy cattle. An F-like 92-kb plasmid, pO157, is found in most E. coli O157:H7 clinical isolates, and pO157 shares sequence similarities with plasmids present in other enterohemorrhagic E. coli serotypes. We compared wild-type (WT) E. coli O157:H7 and an isogenic ⌬pO157 mutant for (i) growth rates and antibiotic susceptibilities, (ii) survival in environments with various acidity, salt, or heat conditions, (iii) protein expression, and (iv) survival and persistence in cattle following oral challenge. Growth, metabolic reactions, and antibiotic resistance of the ⌬pO157 mutant were indistinguishable from those of its complement and the WT. However, in cell competition assays, the WT was more abundant than the ⌬pO157 mutant. The ⌬pO157 mutant was more resistant to acidic synthetic bovine gastric fluid and bile than the WT. In vivo, the ⌬pO157 mutant survived passage through the bovine gastrointestinal tract better than the WT but, interestingly, did not colonize the bovine rectoanal junction mucosa as well as the WT. Many proteins were differentially expressed between the ⌬pO157 mutant and the WT. Proteins from whole-cell lysates and membrane fractions of cell lysates were separated using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and two-dimensional gel electrophoresis. Ten differentially expressed ϳ50-kDa proteins were identified by quadrupole-time of flight mass spectrometry and sequence matching with the peptide fragment database. Most of these proteins, including tryptophanase and glutamate decarboxylase isozymes, were related to survival under salvage conditions, and expression was increased by the deletion of pO157. This suggested that the genes on pO157 regulate some chromosomal genes.

show abstract

“…due to overuse of antibiotics in chemotherapy, food source, agriculture, and animal husbandry (20)(21)(22)(23). Bacterial resistance to one or more antibiotics occurs by various mechanisms (24)(25)(26).…”

Section: Introductionmentioning

confidence: 99%

Evaluation of the 900 MHz Radiofrequency Radiation Effects on the Antimicrobial Susceptibility and Growth Rate of Klebsiella pneumoniae

et al. 2017

View full text Add to dashboard Cite

Introduction: Drug resistance to one or more antibiotics is mainly believed to be a serious threat to global public health which occurs by various mechanisms. The electromagnetic field as a nonchemical tool is capable of altering the antimicrobial susceptibility of bacteria. The aim of this study is the evaluation of the antimicrobial susceptibility of the Klebsiella pneumoniae to antibiotics before and after exposure to 900 MHz radiofrequency (RF) radiation produced by a mobile phone.Methods: Antimicrobial susceptibility of the bacteria to antibiotics disks were performed after exposure to 900 MHz radiofrequency radiation. Antimicrobial susceptibility was carried out by Kirby-Bauer and the inhibition zone of each antibiotic disk was measured (as mean). Additionally, growth variations under exposure were recorded and an outgrowth curve was drawn.Results: Based on the results, after 12 hours of exposure to 900MHz radiofrequency, there was observed a maximum increase in the sensitivity of K. pneumoniae and shown that radiofrequency (RF) radiation can change antimicrobial sensitivity significantly (P < 0.05). Also, the radiofrequency radiation effect on the bacterial proliferation was evaluated and showed that exposure enables the bacteria to grow faster in the exponential phase than the non-exposed bacteria. Conclusions:The findings of the study indicated that the sensitivity of K. pneumoniae was significantly increased to the various antibiotics after 12 hours of exposure to 900 MHz radiofrequency radiation. These observations could be interpreted by the concept of non-linearity in the responses of K. pneumoniae to different antibiotics after exposure to electromagnetic radiofrequency radiation and can be useful in the management of serious infectious diseases.

show abstract

Analysis of outer membrane proteome of Escherichia coli related to resistance to ampicillin and tetracycline

Cited by 118 publications

References 51 publications

Structural Basis of Outer Membrane Protein Biogenesis in Bacteria

Structural Basis of Outer Membrane Protein Biogenesis in Bacteria

Characterization of an Escherichia coli O157:H7 Plasmid O157 Deletion Mutant and Its Survival and Persistence in Cattle

Evaluation of the 900 MHz Radiofrequency Radiation Effects on the Antimicrobial Susceptibility and Growth Rate of Klebsiella pneumoniae

Contact Info

Product

Resources

About