Molecular basis of bacterial outer membrane permeability

Nikaido, Hiroshi; Vaara, Martti

doi:10.1128/mr.49.1.1-32.1985

Cited by 1,544 publications

(387 citation statements)

References 330 publications

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“…In addition, the production of PpIX may also be enhanced due to the increased uptake of ALA by PA. In another study, Nikaido et al treated Gram-negative bacteria with Tris-EDTA and found that divalent cations were removed from the outer membrane, allowing small molecules (1000-2000 Da) to better penetrate the inner membrane and enter the cellular compartments [31]. There are also reports from Bertoloni et al that the sterilization of Escherichia coli or Klebsiella pneumoniae by PDT is more effective after combined treatment with Tris-EDTA and hematoporphyrin [32].…”

Section: Discussionmentioning

confidence: 99%

Enhanced sterilization and healing of cutaneous pseudomonas infection using 5-aminolevulinic acid as a photosensitizer with 410-nm LED light

Katayama

Ozawa

Morimoto

et al. 2018

Journal of Dermatological Science

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Section: Discussionmentioning

confidence: 99%

Enhanced sterilization and healing of cutaneous pseudomonas infection using 5-aminolevulinic acid as a photosensitizer with 410-nm LED light

Katayama

Ozawa

Morimoto

et al. 2018

Journal of Dermatological Science

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“…One such subgroup contains the porins, which provide the molecular basis for membrane permeability. These porins are found in bacteria and allow promiscuous or specific transport through the outer membrane (33). CHUNNEL was used to analyze the porin family, as defined by the b-barreled porin fold (34).…”

Section: Application To the Porin Membrane Protein Familymentioning

confidence: 99%

Finding and Characterizing Tunnels in Macromolecules with Application to Ion Channels and Pores

Coleman

Sharp

2009

Biophysical Journal

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We describe a new algorithm, CHUNNEL, to automatically find, characterize, and display tunnels or pores in proteins. The correctness and accuracy of the algorithm is verified on a constructed set of proteins and used to analyze large sets of real proteins. The verification set contains proteins with artificially created pores of known path and width profile. The previous benchmark algorithm, HOLE, is compared with the new algorithm. Results show that the major advantage of the new algorithm is that it can successfully find and characterize tunnels with no a priori guidance or clues about the location of the tunnel mouth, and it will successfully find multiple tunnels if present. CHUNNEL can also be used in conjunction with HOLE, with the former used toprime HOLE and the latter to track and characterize the pores. Analysis was conducted on families of membrane protein structures culled from the Protein Data Bank as well as on a set of transmembrane proteins with predicted membrane-aqueous phase interfaces, yielding the first completely automated examination of tunnels through membrane proteins, including tunnels that exit in the membrane bilayer.

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“…The D, D Hep and L, D Hep are the main components of the LPS core and the D, D Hep also forms a heptan repeat unit in the O-antigen region. Previous researches have shown that the lack of heptose would result in LPS truncation in many Gram negative bacteria and cause profound effects on bacterial invasion, outer membrane integrity and surface hydrophilicity [18][19][20]. Recently, there has been a growing number of publications demonstrating that several precursors of heptose can also be a pathogen-associated molecular pattern (PAMP), a molecule derived from pathogens and recognized by pattern recognition receptors (PRRs) of host cells, in addition to being a part of LPS.…”

Section: Introductionmentioning

confidence: 99%

Helicobacter pylori GmhB enzyme involved in ADP-heptose biosynthesis pathway is essential for lipopolysaccharide biosynthesis and bacterial virulence

et al. 2021

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Helicobacter pylori infection is linked to serious gastric-related diseases including gastric cancer. However, current therapies for treating H. pylori infection are challenged by the increased antibiotic resistance of H. pylori. Therefore, it is in an urgent need to identify novel targets for drug development against H. pylori infection. In this study, HP0860 gene from H. pylori predicted to encode a D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB) involved in the synthesis of ADP-L-glycero-D-manno-heptose for the assembly of lipopolysaccharide (LPS) in the inner core region was cloned and characterized. We reported HP0860 protein is monomeric and functions as a phosphatase by converting D-glycero-D-manno-heptose-1,7-bisphosphate into D-glycero-D-manno-heptose-1-phosphate with a preference for the β-anomer over the α-anomer of sugar phosphate substrates. Subsequently, a HP0860 knockout mutant and its complementary mutant were constructed and their phenotypic properties were examined. HP0860 knockout mutant contained both mature and immature forms of LPS and could still induce significant IL-8 secretion after gastric AGS cell infection, suggesting other enzymatic activities in HP0860 knockout mutant might be able to partially compensate for the loss of HP0860 activity. In addition, HP0860 knockout mutant was much more sensitive to antibiotic novobiocin, had decreased adherence abilities, and caused less classic hummingbird phenotype on the infected AGS cells, indicating H. pylori lacking HP0860 is less virulent. Furthermore, the disruption of HP0860 gene altered the sorting of cargo proteins into outer membrane vesicles (OMVs). The above findings confirm the importance of HP0860 in LPS core biosynthesis and shed light on therapeutic intervention against H. pylori infection.

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Molecular basis of bacterial outer membrane permeability

Cited by 1,544 publications

References 330 publications

Enhanced sterilization and healing of cutaneous pseudomonas infection using 5-aminolevulinic acid as a photosensitizer with 410-nm LED light

Enhanced sterilization and healing of cutaneous pseudomonas infection using 5-aminolevulinic acid as a photosensitizer with 410-nm LED light

Finding and Characterizing Tunnels in Macromolecules with Application to Ion Channels and Pores

Helicobacter pylori GmhB enzyme involved in ADP-heptose biosynthesis pathway is essential for lipopolysaccharide biosynthesis and bacterial virulence

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