Microbe-Host Interactions: Structure and Role of Gram-Negative Bacterial Porins (885 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 843-854.
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Paper type: Journal Article,
Impact factor: 2.326, 5-year impact factor: 3.148
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84874850186&partnerID=40&md5=8bb221fcb760d60daed2fc2a9ceedfd4
Keywords: Bacteria, Immunobiology, Porin, Signaling Pathways, Structure, Antibiotic Agent, Bacteriorhodopsin, Cd11 Antigen, Cd14 Antigen, Cd18 Antigen, Immunoglobulin Enhancer Binding Protein, Interleukin 6, Lipopolysaccharide, Mitogen Activated Protein Kinase Kinase 1, Myeloid Differentiation Factor 88, Outer Membrane Protein F, Toll Like Receptor 1, Tumor Necrosis Factor Alpha, Antibiotic Resistance, Bacterial Infection, Bacterial Membrane, Gram Negative Bacterium, Haemophilus Influenzae, Host Pathogen Interaction, Human, Nonhuman, Oligomerization, Pathogenesis, Protein Assembly, Protein Structure, Pseudomonas Aeruginosa, Review, Signal Transduction, Animals, Drug Resistance, Microbial, Gram-Negative Bacteria, Host-Pathogen Interactions, Structure-Activity Relationship,
Affiliations:
*** IBB - CNR ***
Department of Biological Sciences, Division of Biostructures, University of Naples Federico II and Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Naples, Italy
Department of Experimental Medicine, Division of Microbiology -II University of Naples, Via De Crecchio 7, 80138, Naples, Italy
References:
Not available.
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 843-854.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.326, 5-year impact factor: 3.148
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84874850186&partnerID=40&md5=8bb221fcb760d60daed2fc2a9ceedfd4
Keywords: Bacteria, Immunobiology, Porin, Signaling Pathways, Structure, Antibiotic Agent, Bacteriorhodopsin, Cd11 Antigen, Cd14 Antigen, Cd18 Antigen, Immunoglobulin Enhancer Binding Protein, Interleukin 6, Lipopolysaccharide, Mitogen Activated Protein Kinase Kinase 1, Myeloid Differentiation Factor 88, Outer Membrane Protein F, Toll Like Receptor 1, Tumor Necrosis Factor Alpha, Antibiotic Resistance, Bacterial Infection, Bacterial Membrane, Gram Negative Bacterium, Haemophilus Influenzae, Host Pathogen Interaction, Human, Nonhuman, Oligomerization, Pathogenesis, Protein Assembly, Protein Structure, Pseudomonas Aeruginosa, Review, Signal Transduction, Animals, Drug Resistance, Microbial, Gram-Negative Bacteria, Host-Pathogen Interactions, Structure-Activity Relationship,
Affiliations:
*** IBB - CNR ***
Department of Biological Sciences, Division of Biostructures, University of Naples Federico II and Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Naples, Italy
Department of Experimental Medicine, Division of Microbiology -II University of Naples, Via De Crecchio 7, 80138, Naples, Italy
References:
Not available.
Microbe-Host Interactions: Structure and Role of Gram-Negative Bacterial Porins
Gram negative bacteria have evolved many mechanisms of attaching to and invading host epithelial and immune cells. In particular, many outer membrane proteins (OMPs) are involved in this initial interaction between the pathogen and their host. The outer membrane (OM) of Gram-negative bacteria performs the crucial role of providing an extra layer of protection to the organism without compromising the exchange of material required for sustaining life. The OM, therefore, represents a sophisticated macromolecular assembly, whose complexity has yet to be fully elucidated. This review will summarize the structural information available for porins, a class of OMP, and highlight their role in bacterial pathogenesis and their potential as therapeutic targets. The functional role of porins in microbe-host interactions during various bacterial infections has emerged only during the last few decades, and their interaction with a variety of host tissues for adhesion to and invasion of the cell and for evasion of host-defense mechanisms have placed bacterial porins at the forefront of research in bacterial pathogenesis. This review will discuss the role that porins play in activating immunological responses, in inducing signaling pathways and their influence on antibiotic resistance mechanisms that involve modifications of the properties of the OM lipid barrier.
Gram negative bacteria have evolved many mechanisms of attaching to and invading host epithelial and immune cells. In particular, many outer membrane proteins (OMPs) are involved in this initial interaction between the pathogen and their host. The outer membrane (OM) of Gram-negative bacteria performs the crucial role of providing an extra layer of protection to the organism without compromising the exchange of material required for sustaining life. The OM, therefore, represents a sophisticated macromolecular assembly, whose complexity has yet to be fully elucidated. This review will summarize the structural information available for porins, a class of OMP, and highlight their role in bacterial pathogenesis and their potential as therapeutic targets. The functional role of porins in microbe-host interactions during various bacterial infections has emerged only during the last few decades, and their interaction with a variety of host tissues for adhesion to and invasion of the cell and for evasion of host-defense mechanisms have placed bacterial porins at the forefront of research in bacterial pathogenesis. This review will discuss the role that porins play in activating immunological responses, in inducing signaling pathways and their influence on antibiotic resistance mechanisms that involve modifications of the properties of the OM lipid barrier.
Microbe-Host Interactions: Structure and Role of Gram-Negative Bacterial Porins
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Microbe-Host Interactions: Structure and Role of Gram-Negative Bacterial Porins
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Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
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Berisio R, Schluenzen F, Harms J, Bashan A, Auerbach T, Baram D, Yonath A
* Structural insight into the role of the ribosomal tunnel in cellular regulation (484 views)
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Impact Factor: 11.579
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Monti SM, Fogliano V, Logrieco A, Ferracane R, Ritieni A
Simultaneous determination of beauvericin, enniatins, and fusaproliferin by high performance liquid chromatography (573 views)
J Agric Food Chem (ISSN: 0021-8561), 2000 Sep; 48(8): 3317-3320.
Impact Factor: 1.56
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29 Records (27 excluding Abstracts).
Total impact factor: 110.223 (104.096 excluding Abstracts).
Total 5 year impact factor: 108.226 (101.88 excluding Abstracts).
Total impact factor: 110.223 (104.096 excluding Abstracts).
Total 5 year impact factor: 108.226 (101.88 excluding Abstracts).
885 views. Last view on Wednesday 18 September 2024, 0:42:48
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