Dataset Information

Severe hepatic abscess: Conservative treatment of multi-organ infection by Stenotrophomonas maltophilia. A case report.

ABSTRACT:

Introduction

Stenotrophomonas Malthophilia (SM) is generally considered a nosocomial pathogen but it has also been reported as a cause of community-acquired systemic infection. We reported a rare case of SM multi-organ infection involving the liver and the left ocular region.

Presentation of the case

A 64 years old man presented with fever for 4 days and acute blindness of the left eye. We performed an abdomen and head CT scan that identified respectively a liver lesion in central region, likely a hepatic abscess, and inflammation process involving the left eye. After 5 days of antibiotic therapy, no improvement of the clinical condition was noted. A CT guided drainage of the hepatic abscess was performed. SM was identified in the content of the drain and selected antibiotic therapy with combination of tygecycline and TMP-SMX was immediately initiated.After 15 days of the selected therapy, the hepatic abscess and the left eye infection were completely resolved but unfortunately the patient reported permanent blindness.

Discussion

Several studies identified most of the SM infections as nosocomial, however that can be excluded in this case because the patient presented signs of severe systemic infection 72 h before the hospitalization. The conservative treatment, with a combination of CT guided drainage and selected antibiotic therapy, gave good results.

Conclusion

Although SM is thought to be a nosocomial pathogen, it can be involved in severe systemic sepsis affecting different organs outside the hospital setting. Fortunately, the combination of tigecycline with TMP-SMX seems to be the best therapeutic option.

SUBMITTER: Inviati A

PROVIDER: S-EPMC6143753 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Publications

Severe hepatic abscess: Conservative treatment of multi-organ infection by Stenotrophomonas maltophilia. A case report.

Inviati A A Pellegrino D M DM Schifano D D

Annals of medicine and surgery (2012) 20180906

<h4>Introduction</h4>Stenotrophomonas Malthophilia (SM) is generally considered a nosocomial pathogen but it has also been reported as a cause of community-acquired systemic infection. We reported a rare case of SM multi-organ infection involving the liver and the left ocular region.<h4>Presentation of the case</h4>A 64 years old man presented with fever for 4 days and acute blindness of the left eye. We performed an abdomen and head CT scan that identified respectively a liver lesion in central ...[more]

PMID: 30237880

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Project description:PabB, aminodeoxychorismate synthase, is the chorismic acid binding component of the heterodimeric PabA-PabB complex that converts chorismic acid to 4-amino-4-deoxychorismate, a precursor of p-aminobenzoate and folic acid in microorganisms. The second component, a glutamine amidotransferase subunit, PabA, generates ammonia that is channeled to the PabB active site where it attacks C4 of a chorismate-derived intermediate that is covalently bound, through C2, to an active site lysine residue. The presence of a PIKGT motif was, until recently, believed to allow discrimination of PabB enzymes from the closely related enzyme anthranilate synthase, which typically contains a PIAGT active site motif and does not form a covalent enzyme-substrate intermediate with chorismate. A subclass of PabB enzymes that employ an alternative mechanism requiring 2 equiv of ammonia from glutamine and that feature a noncovalently bound 2-amino-2-deoxyisochorismate intermediate was recently identified. Here we report the 2.25 Å crystal structure of PabB from the emerging pathogen Stenotrophomonas maltophilia. It is the first reported structure of a PabB that features the PIAGT motif. Surprisingly, no dedicated pabA is evident in the genome of S. maltophilia, suggesting that another cellular amidotransferase is able to fulfill the role of PabA in this organism. Evaluation of the ammonia-dependent aminodeoxychorismate synthase activity of S. maltophilia PabB alone revealed that it is virtually inactive. However, in the presence of a heterologous PabA surrogate, typical levels of activity were observed using either glutamine or ammonia as the nitrogen source. Additionally, the structure suggests that a key segment of the polypeptide can remodel itself to interact with a nonspecialized or shared amidotransferase partner in vivo. The structure and mass spectral analysis further suggest that S. maltophilia PabB, like Escherichia coli PabB, binds tryptophan in a vestigial regulatory site. The observation that the binding site is unoccupied in the crystal structure, however, suggests the affinity may be low relative to that of E. coli PabB.

Dataset Information

Severe hepatic abscess: Conservative treatment of multi-organ infection by Stenotrophomonas maltophilia. A case report.

Introduction

Presentation of the case

Discussion

Conclusion

Publications

Severe hepatic abscess: Conservative treatment of multi-organ infection by Stenotrophomonas maltophilia. A case report.

Similar Datasets

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