Multiple facets of bacterial porins

Achouak, Wafa; Heulin, Thierry; Pagès, Jean‐Marie

doi:10.1111/j.1574-6968.2001.tb10642.x

Cited by 205 publications

(112 citation statements)

References 40 publications

(62 reference statements)

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“…Consistent with this observation, the application of immunolabeled phage TG1 receptor binding protein Gp37 to Y. enterocolitica cells showed decoration of the surfaces of Y. enterocolitica O:3, O:5,27, and O:9 cells when these were cultured at 25°C but not at 37°C. The decoration of the cell surface agrees with a highlevel expression of this major outer membrane protein class, depending on the bacterial species and the environmental conditions, which can reach about 10 4 to 10 6 copies per cell (74). It is reasonable to suggest then that the phage TG1 distal LTF protein Gp37 (and by extension, its homolog in R1-RT) is specifically involved in binding to OmpF while presumably the STF protein Gp12 binds to the inner core of LPS, as is reported to occur in other T even phages as a secondary receptor (70,71).…”

Section: Discussionmentioning

confidence: 63%

“…S9). The porin loops are plausible binding sites for bacteriophages, as demonstrated by the interaction of E. coli OmpF and K20 phages, which bind to the L5, L6, and L7 external loops (74)(75)(76). Thus, it is likely that the loop 4 sequence is targeted by the R1-RT or TG1 receptor binding proteins, but experimental evidence is necessary to confirm this.…”

Section: Discussionmentioning

confidence: 99%

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Yersinia enterocolitica-Specific Infection by Bacteriophages TG1 and ϕR1-RT Is Dependent on Temperature-Regulated Expression of the Phage Host Receptor OmpF

León-Velarde

Happonen

Pajunen

et al. 2016

Appl Environ Microbiol

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Bacteriophages present huge potential both as a resource for developing novel tools for bacterial diagnostics and for use in phage therapy. This potential is also valid for bacteriophages specific for Yersinia enterocolitica. To increase our knowledge of Y. enterocolitica-specific phages, we characterized two novel yersiniophages. The genomes of the bacteriophages vB_YenM_TG1 (TG1) and vB_YenM_R1-RT (R1-RT), isolated from pig manure in Canada and from sewage in Finland, consist of linear double-stranded DNA of 162,101 and 168,809 bp, respectively. Their genomes comprise 262 putative coding sequences and 4 tRNA genes and share 91% overall nucleotide identity. Based on phylogenetic analyses of their whole-genome sequences and large terminase subunit protein sequences, a genus named Tg1virus within the family Myoviridae is proposed, with TG1 and R1-RT (R1RT in the ICTV database) as member species. These bacteriophages exhibit a host range restricted to Y. enterocolitica and display lytic activity against the epidemiologically significant serotypes O:3, O:5,27, and O:9 at and below 25°C. Adsorption analyses of lipopolysaccharide (LPS) and OmpF mutants demonstrate that these phages use both the LPS inner core heptosyl residues and the outer membrane protein OmpF as phage receptors. Based on RNA sequencing and quantitative proteomics, we also demonstrate that temperature-dependent infection is due to strong repression of OmpF at 37°C. In addition, R1-RT was shown to be able to enter into a pseudolysogenic state. Together, this work provides further insight into phage-host cell interactions by highlighting the importance of understanding underlying factors which may affect the abundance of phage host receptors on the cell surface. IMPORTANCEOnly a small number of bacteriophages infecting Y. enterocolitica, the predominant causative agent of yersiniosis, have been previously described. Here, two newly isolated Y. enterocolitica phages were studied in detail, with the aim of elucidating the host cell receptors required for infection. Our research further expands the repertoire of phages available for consideration as potential antimicrobial agents or as diagnostic tools for this important bacterial pathogen.Y ersinia enterocolitica, a facultative anaerobic, Gram-negative, nonsporulating, short bacillus isolated frequently from soil, water, animals, and foods, is an important zoonotic pathogen leading to human and animal enteric infection (1). The main animal reservoir for Y. enterocolitica is pigs, and pork-derived products are thought to be the main source of human infections, in addition to the drinking of contaminated water and blood transfusions (1, 2). Symptoms of yersiniosis may include diarrhea, terminal ileitis, mesenteric lymphadenitis, and septicemia (3). Among the species within the genus Yersinia, Y. enterocolitica is highly heterogeneous and is grouped into six phylogroups (4). The widely used bioserotype groups form the basis of the phylogroups such that phylogroup 1 contains the biotype 1A strains,...

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Section: Discussionmentioning

confidence: 63%

Section: Discussionmentioning

confidence: 99%

Yersinia enterocolitica-Specific Infection by Bacteriophages TG1 and ϕR1-RT Is Dependent on Temperature-Regulated Expression of the Phage Host Receptor OmpF

León-Velarde

Happonen

Pajunen

et al. 2016

Appl Environ Microbiol

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“…Note that the func tional properties of the loops are still not clearly under stood. Most often they act as binding sites for bacterio phages, bactericides, the complement subcomponents, and antibodies [18]. Thus, the L7 loop of the OprD from P. aeruginosa is involved in regulation of the OM perme ability for β lactam antibiotics [19].…”

Section: Resultsmentioning

confidence: 99%

Molecular Characteristics of OmpF-Like Porins from Pathogenic Yersinia

Guzev

Isaeva

Novikova

et al. 2005

Biochemistry (Moscow)

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Nonspecific pore-forming proteins (porins) are the major proteins of the outer membrane of Gram-negative bacteria responsible for diffusion of low-molecular-weight compounds. Nucleotide sequences of the OmpF-like porins from the pathogenic bacteria Yersinia pseudotuberculosis (YPS) and Yersinia enterocolitica (YE) were cloned and determined. Values of molecular weights (MW) and isoelectric points (IEP) calculated for these proteins (for OmpF-YPS: MW 37.7 kD, IEP 4.45; for OmpF-YE: MW 39.5 kD, IEP 4.34) are in good agreement with experimental data. The OmpF-like Yersinia porins are highly homologous to each other (83-92%) and also to the OmpF protein from Serratia marcescens (70%); the homology to the OmpF porin from E. coli is significantly lower (52-58%). Multiple alignment of the amino acid sequences of mature OmpF proteins provided the distribution of conservative amino acid residues typical for porins. Moreover, the OmpF-like porins from Yersinia are characterized by the presence of extended regions with high and low homologies, which coincide with the transmembrane domains and "external" loops, respectively, of the topological model of the OmpF porin from E. coli. By predictive methods, the secondary structure of the OmpF-like porins from Yersinia was obtained. This structure is represented by 16 beta-strands connected by short "periplasmic" and longer "external" loops with unordered structure.

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“…Porins from OM of pathogenic bacterium are pathogenesis effectors, suppress the defense reactions, and act as targets for the host immune cells. Antibodies to porins are detected in the serum after vaccination and in natural development of the infection [5].…”

mentioning

confidence: 99%

“…Nonspecifi c porins forming channels for diffusion of lowmolecular compounds through the membrane are the main proteins of the outer membrane (OM) in gram-negative bacteria [5]. Porins from OM of pathogenic bacterium are pathogenesis effectors, suppress the defense reactions, and act as targets for the host immune cells.…”

mentioning

confidence: 99%

Immunogenic Characteristics of Recombinant OMPF-Like Porin from Yersinia Pseudotuberculosis Outer Membrane

et al. 2009

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We studied the capacity of outer membrane pore-forming recombinant protein from Yersinia pseudotuberculosis to initiate the development of immune response in CBA mice. Immunization with the recombinant protein induces the production of IgG antibodies with and without adjuvants. High-avidity immune serum was obtained as a result of immunization. Bactericidal activity of peritoneal macrophages from mice immunized with recombinant protein was significantly higher than that of intact mouse macrophages. The use of recombinant porin instead of native porin as the antigen in enzyme immunoassay system for the diagnosis of acute and secondary focal pseudotuberculosis does not reduce the efficiency of detection of specific antibodies in the sera of patients.

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Multiple facets of bacterial porins

Cited by 205 publications

References 40 publications

Yersinia enterocolitica-Specific Infection by Bacteriophages TG1 and ϕR1-RT Is Dependent on Temperature-Regulated Expression of the Phage Host Receptor OmpF

Yersinia enterocolitica-Specific Infection by Bacteriophages TG1 and ϕR1-RT Is Dependent on Temperature-Regulated Expression of the Phage Host Receptor OmpF

Molecular Characteristics of OmpF-Like Porins from Pathogenic Yersinia

Immunogenic Characteristics of Recombinant OMPF-Like Porin from Yersinia Pseudotuberculosis Outer Membrane

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