نتایج جستجو برای: oprd porin protein

تعداد نتایج: 1235787  

Journal: :The Southeast Asian journal of tropical medicine and public health 2010
Penphun Naenna Pirom Noisumdaeng Pintip Pongpech Chanwit Tribuddharat

Decreased permeability to imipenem is the most frequent mechanism of imipenem resistance in Pseudomonas aeruginosa. We have determined the presence of OprD porin protein, an imipenem influx channel, in 70 carbapenem-resistant P. aeruginosa clinical isolates by Western blot analysis using rabbit anti-OprD polyclonal antibody. Ninety-eight percent (54 of 55 isolates) of imipenem-and meropenem-res...

Journal: :jundishapur journal of microbiology 0
huseyin agah terzi department of medical microbiology, training and research hospital, sakarya university, sakarya, turkey; department of medical microbiology, training and research hospital, sakarya university, sakarya, turkey. tel:+90-5364628654, fax: +90-2642759192 canan kulah department of medical microbiology, school of medicine, bulent ecevit university, zonguldak, turkey ali riza atasoy department of medical microbiology, training and research hospital, sakarya university, sakarya, turkey ihsan hakki ciftci department of medical microbiology, training and research hospital, sakarya university, sakarya, turkey

conclusions although the data support the idea that the basic mechanism of imipenem resistance could be via the loss of oprd, they do not fully explain the role of oprd and indicate that other mechanisms may play an important role. additionally, the significant decrease in the oprd levels in mdr strains suggests that oprd also plays a role in the emergence of both carbapenem and non-carbapenem ...

Journal: :Antimicrobial agents and chemotherapy 2001
S F Epp T Köhler P Plésiat M Michéa-Hamzehpour J Frey J C Pechère

We investigated the unusual susceptibility to meropenem observed for seven imipenem-resistant clinical isolates of Pseudomonas aeruginosa. These strains were genetically closely related, expressed OprD, as determined by Western blot analyses, and were resistant to imipenem (>5 microg/ml) but susceptible to meropenem (<1 microg/ml). The oprD genes from two isolates were entirely sequenced, and t...

Journal: :Antimicrobial agents and chemotherapy 2012
Manuella Catel-Ferreira Rony Nehmé Virginie Molle Jesús Aranda Emeline Bouffartigues Sylvie Chevalier Germán Bou Thierry Jouenne Emmanuelle Dé

The increasing number of carbapenem-resistant Acinetobacter baumannii isolates is a major cause for concern which restricts therapeutic options to treat severe infections caused by this emerging pathogen. To identify the molecular mechanisms involved in carbapenem resistance, we studied the contribution of an outer membrane protein homologue of the Pseudomonas aeruginosa OprD porin. Suspected t...

Journal: :Antimicrobial agents and chemotherapy 1999
M M Ochs M P McCusker M Bains R E Hancock

Pseudomonas aeruginosa OprD is a specific porin which facilitates the uptake of basic amino acids and imipenem, a carbapenem antibiotic. Resistance to imipenem due to the loss of OprD is an important mechanism for the loss of clinical effectiveness. To investigate the negative regulatory mechanisms influencing oprD expression, a gene upstream of the coregulated mexEF-oprN efflux operon, designa...

Journal: :Jundishapur journal of microbiology 2015
Huseyin Agah Terzi Canan Kulah Ali Riza Atasoy Ihsan Hakki Ciftci

BACKGROUND The Pseudomonas aeruginosa porin OprD is a substrate-specific porin that facilitates the diffusion of basic amino acids, small peptides, and carbapenems into the cell. OprD-mediated resistance occurs as a result of decreased transcriptional expression of oprD and/or loss of function mutations that disrupt protein activity. OBJECTIVES In this study, we examined the level of oprD exp...

Journal: :Journal of bacteriology 1993
H Huang R E Hancock

Earlier studies proved that Pseudomonas aeruginosa OprD is a specific porin for basic amino acids and imipenem. It was also considered to function as a nonspecific porin that allowed the size-dependent uptake of monosaccharides and facilitation of the uptake of quinolone and other antibiotics. In the present study, we utilized P. aeruginosa strains with genetically defined levels of OprD to cha...

Journal: :Antimicrobial agents and chemotherapy 2000
M M Ochs M Bains R E Hancock

Mutant proteins with eight amino acid deletions in putative surface loops 2 and 3 of the imipenem-specific porin OprD of Pseudomonas aeruginosa failed to reconstitute imipenem susceptibility in an oprD-deficient background. The loop 3 deletion prevented the ability of imipenem to inhibit KCl conductance through the OprD channel, as previously shown for a loop 2 deletion. This suggests that both...

Journal: :Journal of bacteriology 2006
Sandeep Tamber Martina M Ochs Robert E W Hancock

To circumvent the permeability barrier of its outer membrane, Pseudomonas aeruginosa has evolved a series of specific porins. These channels have binding sites for related classes of molecules that facilitate uptake under nutrient-limited conditions. Here, we report on the identification of a 19-member family of porins similar to the basic-amino-acid-specific porin OprD. The members of this fam...

Journal: :FEMS microbiology letters 1992
H Huang R J Siehnel F Bellido E Rawling R E Hancock

A Tn501 mutant of Pseudomonas aeruginosa resistant to imipenem and lacking the imipenem-specific outer membrane porin protein OprD was isolated. The mutation could be complemented to imipenem susceptibility and OprD-sufficiency by a cloned 6-kb EcoRI-PstI fragment of DNA from the region of chromosome of the wild-type strain surrounding the site of Tn501 insertion. However, this fragment did not...

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