EPR studies on model membranes of phospholipid and outer membrane proteins of <i>Proteus mirabilis</i>

Nixdorff, Kathryn; Martin, Hans Herbert; Rottem, Shlomo; Razin, Shmuel

doi:10.1016/0014-5793(78)80961-2

Cited by 4 publications

(4 citation statements)

References 11 publications

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“…The phenomenon whereby magnesium destabilizes the membrane vesicles has been noted by others using different bacterial outer membranes (24). We previously reported 7that magnesium was needed to prevent the leakage of P-lactamase from the periplasm of whole cells.…”

Section: Resultsmentioning

confidence: 78%

Transmembrane permeability channels across the outer membrane of Haemophilus influenzae type b

Vachon¹,

Lyew²,

Coulton³

1985

J Bacteriol

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Outer membranes of Haemophilus influenzae type b were fractionated to yield Triton X-100-insoluble material and lipopolysaccharide and phospholipids. Liposomes reconstituted from lipopolysaccharide and phospholipids were impermeable to sucrose (Mr, 342) and to a high-molecular-weight dextran (average Mr, 6,600). When the Triton X-100-insoluble material was introduced into the reconstituted liposomes, the vesicles became permeable to sucrose, raffinose (Mr, 504), and stachyose (Mr, 666) and fully retained dextrans of Mr greater than 1,500. Inulin (average Mr, 1,400) was tested for its efflux from the reconstituted outer membrane vesicles; 62% of the added inulin was trapped. The molecular weight exclusion limit for the outer membrane of H. influenzae type b was therefore estimated at approximately 1,400. A protein responsible for the transmembrane diffusion of solutes was purified from H. influenzae type b by extraction of whole cells with

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Section: Resultsmentioning

confidence: 78%

Transmembrane permeability channels across the outer membrane of Haemophilus influenzae type b

Vachon¹,

Lyew²,

Coulton³

1985

J Bacteriol

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“…Porins are among the predominant or major proteins found in the outer membranes of gramnegative bacteria. Their function is to form pores that allow the diffusion of small hydrophylic molecules across the outer membrane barrier (3,12,16,17,(20)(21)(22). The transmembrane nature of porins is demonstrated by their ability to serve as receptors for bacteriophages or colicins (3) and their tight, noncovalent association with peptidoglycan (3,(15)(16)(17)(18)29).…”

mentioning

confidence: 99%

Escherichia coli outer membrane protein K is a porin

Sutcliffe¹,

Blumenthal²,

Walter³

et al. 1983

J Bacteriol

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Protein K is an outer membrane protein found in pathogenic encapsulated strains of Escherichia coli. We present evidence here that protein K is structurally and functionally related to the E. coli K-12 porin proteins (OmpF, OmpC, and PhoE). Protein K was found to cross-react with antibody to OmpF protein and to share 8 out of 17 peptides in common with the OmpF protein. Strains that are OmpC porin- and OmpF porin- and contain protein K as their major outer membrane protein have increased rates of uptake of nutrients and a faster growth rate relative to the parental porin- strain. The protein K-containing strains are at least 1,000-fold more sensitive to colicins E2 and E3 than is the porin -deficient strain. These data suggest that protein K is a functional porin in E. coli. The porin function of protein K was also demonstrated in vitro, using black lipid membranes. Protein K increased the conductance in these membranes in discrete, uniform steps characteristic of channels with a size of about 2 nS.

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“…Pores of enteric bacteria such as E. coli and Salmonella, Proteus, or Enterobacter spp. were found to have exclusion limits of approximately 700 (21,29,30,35), while the pore size of Yersinia pestis porin allowed the diffusion of oligosaccharides with molecular weights of 500 to 600 (10). It was also reported that the exclusion limit of the OMP of Bacteroides fragilis was similar to the molecular weight of disaccharides, i.e., Mr of 340 to 400 (23).…”

Section: Discussionmentioning

confidence: 94%

Immunochemical and biological characterization of outer membrane proteins of Porphyromonas endodontalis

et al. 1992

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Outer membrane proteins (OMP) of Porphyromonas endodontalis HG 370 (ATCC 35406) were prepared from the cell envelope fraction of the organisms. The cell envelope that had been obtained by sonication of the whole cells was extracted in 2% lithium dodecyl sulfate and then successively chromatographed with Sephacryl S-200 HR and DEAE-Sepharose Fast Flow. Two OMP fractions, OMP-I and OMP-II, were obtained, and their immunochemical properties and induction of specific antibodies were examined. The OMP-I preparation consisted of a major protein with an apparent molecular mass of 31 kDa and other moderate to minor proteins of 40.3, 51.4, 67, and 71.6 kDa, while the OMP-II preparation contained 14-, 15.5-, 27-, and 44-kDa proteins as revealed by sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis. OMP-I was found to form 4528 on August 2, 2020 by guest http://iai.asm.org/ Downloaded from

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EPR studies on model membranes of phospholipid and outer membrane proteins of Proteus mirabilis

Cited by 4 publications

References 11 publications

Transmembrane permeability channels across the outer membrane of Haemophilus influenzae type b

Transmembrane permeability channels across the outer membrane of Haemophilus influenzae type b

Escherichia coli outer membrane protein K is a porin

Immunochemical and biological characterization of outer membrane proteins of Porphyromonas endodontalis

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