porins

por·ins

(pōr'inz),
Proteins found in the outer membrane of a double membrane that allow permeability in most small molecules.
[G. poros, passageway, + -in]
References in periodicals archive ?
However, ESBLs and AmpC can confer carbapenem resistance when associated with alteration or loss of porins, a family of proteins on the outer membrane of gram-negative bacteria (2,5).
Use of OmpU porins for attachment and invasion of Crassostrea gigas immune cells by the oyster pathogen Vibrio splendidus.
Creative Biolabs has successfully expressed different types of membrane proteins such as GPCRs, ion channels, porins, viral proteins, transporters, drug receptors, etc.
influenzae, Neisseria gonnorrhoeae; ESBLs (2) (TEM-3, SHV-1 & 2, OXA-1, K1(OXY-1) CTX-M) Ecoli, K pneumoniae Decreased cell Porins (protein Imipenem--small PSE-1, membrane channels) in outer Carbenicillin-- Pseudomonas spp.
Cefoxitin-resistance can be used to screen isolates for detecting possible AmpC production, but lack of permeation of porins has also been reported as one of the resistance mechanism of cefoxitin in AmpC non-producers (15).
In order to get inside the cell, these molecules must pass through porins, which are protein channels that span the outer membrane.
Gram-negative bacteria possess proteins called porins in their outer membranes that, when altered, reduce or halt drug absorption.
Table 2A: Antibiotic Selection for Pediatric Pharyngitis Penicillin, Amoxicillin or Erythromycin (%) Baseline Period Study Period Distant Control 62 69 Local Control 74 73 Intervention 80 80 Table 2B: Antibiotic Selection for Adult Bronchitis Penicillin, Amoxicillin, Second- or Generation Cephalos- Erythromycin Macrolides porins Pre Post Pre Post Pre Post (%) (%) (%) (%) (%) (%) Distant 17 16 56 60 10 8 Control Local 31 23 48 55 8 6 Control Intervention 61 56 25 24 2 6 Sulfona- Tetra- Quinolones mides cyclines Pre Post Pre Post Pre Post (%) (%) (%) (%) (%) (%) Distant 5 6 4 1 8 4 Control Local 4 7 3 1 6 5 Control Intervention 0 0 7 7 4 3
2,3] This is accomplished by mutations of genes encoding the outer-membrane protein channels called porins.
These proteins, called porins, are usually employed by bacteria to form channels that allow nutrients to enter through the cell wall.
This reduction in virulence and fitness was due to the loss of the major porins OmpK35/36 (through which p-lactams penetrate into K.