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Example sentences for: maltophilia
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This work describes our efforts on metallo-β-lactamase L1 from S. maltophilia.
, Burkholderia cepacia , and some strains of Stenotrophomonas maltophilia are usually resistant to colistin [ 8 9 10 11 12 13 14 15 16 17 18 ] . Cross-resistance with other antibiotics has not been reported [ 10 13 ] , and acquired resistance is rare [ 11 17 ] . Although lower susceptibility rates for P. aeruginosa have been reported in patients with cystic fibrosis undergoing chronic prophylactic treatment with inhaled colistin [ 18 ] , 81% of strains of P. aeruginosa from such patients are still susceptible to colistin [ 14 ] .
However, because errors are observed mainly for S. maltophilia and much less often for Acinetobacter spp.
To combat these enzymes, β-lactamase inhibitors such as clavulanic acid, sulbactam, and tazobactam have been given in combination with a β-lactam containing antibiotic to treat bacterial infections [ 52 ] . One class of β-lactamases that are particularly unaffected by the known β-lactamase inhibitors and have been shown to hydrolyze almost all known β-lactam containing antibiotics including late generation carbapenems at high rates are the metallo-β-lactamases [ 14 15 16 17 18 19 ] . Although there are no reports of metallo-β-lactamases isolated from major pathogens [ 51 53 ] , these enzymes are produced by pathogens such as B. fragilis, S. maltophilia, and P. aeruginosa.
S. maltophilia is an important pathogen in nosocomial infections of immunocompromised patients suffering from cancer, cystic fibrosis, drug addition, AIDS and in patients with organ transplants and on dialysis [ 30 31 32 ] . This organism is inherently resistant to most antibiotics due to its low outer membrane permeability [ 33 ] and to β-lactam containing antibiotics due to the production of a chromosomally expressed group 2e β-lactamase (L2) and a group 3c β-lactamase (L1) [ 34 35 ] . L1 has been cloned, over-expressed, and partially characterized by kinetic and crystallographic studies [ 36 37 ] . The enzyme exists as a homotetramer of ca. 118 kDa in solution and in the crystalline state.
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