Chryseobacterium meningosepticum Sepsis Complicated with Retroperitoneal Hematoma and Pleural Effusion in a Diabetic Patient

Lee, Shou-Wu; Tsai, Che-An; Lee, Bor‐Jen

doi:10.1016/s1726-4901(08)70151-5

Cited by 21 publications

(13 citation statements)

References 9 publications

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“…In addition, Ser221 is replaced by a Met residue, suggesting a more divergent metal binding site or a B2-B3 hybrid enzyme. GOB-type enzymes include 18 allelic variants, all of them expressed by E. meningoseptica, a pathogen responsible for neonatal meningitis and opportunistic infections in immunocompromised patients (26)(27)(28). So far, two GOB variants have been characterized biochemically, GOB-1 and GOB-18 (29)(30)(31)(32), which differ by three residues located far from the active site (29).…”

mentioning

confidence: 99%

Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site

Morán-Barrio

Lisa

Larrieux

et al. 2016

Antimicrob Agents Chemother

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f Metallo-beta-lactamases (MBLs) are broad-spectrum, Zn(II)-dependent lactamases able to confer resistance to virtually every ␤-lactam antibiotic currently available. The large diversity of active-site structures and metal content among MBLs from different sources has limited the design of a pan-MBL inhibitor. GOB-18 is a divergent MBL from subclass B3 that is expressed by the opportunistic Gram-negative pathogen Elizabethkingia meningoseptica. This MBL is atypical, since several residues conserved in B3 enzymes (such as a metal ligand His) are substituted in GOB enzymes. Here, we report the crystal structure of the periplasmic di-Zn(II) form of GOB-18. This enzyme displays a unique active-site structure, with residue Gln116 coordinating the Zn1 ion through its terminal amide moiety, replacing a ubiquitous His residue. This situation contrasts with that of B2 MBLs, where an equivalent His116Asn substitution leads to a di-Zn(II) inactive species. Instead, both the mono-and di-Zn(II) forms of GOB-18 are active against penicillins, cephalosporins, and carbapenems. In silico docking and molecular dynamics simulations indicate that residue Met221 is not involved in substrate binding, in contrast to Ser221, which otherwise is conserved in most B3 enzymes. These distinctive features are conserved in recently reported GOB orthologues in environmental bacteria. These findings provide valuable information for inhibitor design and also posit that GOB enzymes have alternative functions.T he expression of ␤-lactamases is the main mechanism of bacterial resistance against ␤-lactam antibiotics. These enzymes catalyze the hydrolysis of the amide bond in the ␤-lactam ring characteristic of this family of drugs (1-5). MBLs are metal-dependent hydrolases which generally use Zn(II) as a Lewis acid to activate a water molecule for the nucleophilic attack. These enzymes are refractive to clinically employed lactamase inhibitors (1) and have a particular relevance in the clinical setting as they can hydrolyze a broad spectrum of ␤-lactam substrates, being able to inactivate carbapenems, the "last-resort" antibiotics in antibacterial therapy (6).MBLs have been classified into subclasses B1, B2, and B3 based on sequence identity (7). Crystal structures of MBLs from the three subclasses have revealed that these enzymes present a common ␣␤/␤␣ sandwich fold, with the active site located within a groove at the interface between these two halves (1-6). The Zn(II)-binding residues vary among different subclasses, giving rise to diverse metal site architectures and metal contents required for activity (1-6). B1 and B3 MBLs are broad-spectrum enzymes that hydrolyze penicillins, cephalosporins, and carbapenems with a wide variety of in vitro catalytic efficiencies, displaying a broad range of resistance profiles in vivo (1)(2)(3)(4)(5)8). The di-Zn(II) form of B1 MBLs has been shown to be the active form in the bacterial periplasm, despite contradictory data obtained from in vitro studies (8-10). These enzymes display a conserved metal binding m...

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confidence: 99%

Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site

Morán-Barrio

Lisa

Larrieux

et al. 2016

Antimicrob Agents Chemother

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“…Echeverri et al reported a case of bacteremia in a patient with history of acute lymphoblastic leukemia, initially treated with moxifloxacin, then combined with vancomycin and sulfamethoxazole [10]. E. meningoseptica bacteremia has also been described in patients requiring chronic hemodialysis therapy [11][12][13][14][15][16]. A study from Taiwan on the analysis of adult patients with E. meningoseptica bacteremia showed that 86% of the patients had nosocomial infections and 60% had acquired the infection in the ICUs [17].…”

Section: Discussionmentioning

confidence: 99%

Elizabethkingia meningoseptica Bacteremia in an Immuno-competent Patient

Rao¹,

Dandamudi²,

Koppula³

2017

JCR

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Background: Elizabethkingia meningoseptica infections are not common but are clinically important because the organism is naturally resistant to multiple antibiotics. A prompt diagnosis is important so as to give appropriate antibiotic treatment. Case Report: We report a case of central line associated Elizabethkingia meningoseptica infection in a patient who was admitted with recurrent oligodendroglioma and underwent right frontal craniotomy and surgical decompression of tumor. Conclusion: Elizabethkingia meningoseptica infection should always be considered in the etiological diagnosis of septicemia who do not respond to empirical therapy as this results in an inappropriate choice of antimicrobial therapy, which may lead to increased morbidity and mortality of patients infected by this pathogen.

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“…[13–5] There are a few reported cases of Chryseobacterium meningosepticum causing infection in dialysis patients. [6–9] We report here a 37-year-old with diabetic nephropathy on hemodialysis who developed bacteremia with this bacterium. Literature search showed this is the first reported case in dialysis patient from India.…”

Section: Introductionmentioning

confidence: 99%

Chryseobacterium meningosepticum bacteremia in diabetic nephropathy patient on hemodialysis

et al. 2010

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The Chryseobacterium species are inhabitants of soil and water. In the hospital environment, they exist in water systems and wet surfaces. We report here a case of Chryseobacterium meningosepticum bacteremia in a diabetic nephropathy patient on hemodialysis. He was successfully treated with Vancomycin and ceftazidime for three weeks with good clinical outcome. This is the first case reported in dialysis patients from India.

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Chryseobacterium meningosepticum Sepsis Complicated with Retroperitoneal Hematoma and Pleural Effusion in a Diabetic Patient

Cited by 21 publications

References 9 publications

Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site

Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site

Elizabethkingia meningoseptica Bacteremia in an Immuno-competent Patient

Chryseobacterium meningosepticum bacteremia in diabetic nephropathy patient on hemodialysis

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