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1.
Am J Case Rep ; 21: e921172, 2020 Mar 01.
Article in English | MEDLINE | ID: mdl-32114590

ABSTRACT

BACKGROUND Chryseobacterium gleum (C. gleum) is a rare but concerning device-associated infection that can cause urinary tract infections and pneumonia. It produces a biofilm and has intrinsic resistance to a wide array of broad-spectrum agents. Risk factors include neonate or immunocompromised states, intensive care unit admission for more than 21 days, broad-spectrum antibiotic exposure, indwelling devices, and mechanical ventilation. CASE REPORT A 61-year-old cachectic man presented in the United States with community-acquired pneumonia and immediately decompensated, requiring ventilator support. Despite starting broad-spectrum antibiotics, the patient developed fever, leukocytosis, and additional desaturation episodes. The patient's respiratory culture grew numerous C. gleum and few Stenotrophomonas (Xanthomonas) maltophilia. He also had a positive urine streptococcal pneumonia antigen. Broad-spectrum agents were discontinued after prolonged treatment due to a continued worsening clinical picture, and the patient was started on trimethoprim-sulfamethoxazole to cover C. gleum. The patient showed rapid clinical improvement on trimethoprim-sulfamethoxazole, with resolution of symptoms on post-discharge follow-up. CONCLUSIONS To the best of our knowledge, this is the first case report of a documented case of a patient with C. gleum respiratory infection successfully treated solely with trimethoprim-sulfamethoxazole. The expedient identification of C. gleum is essential for proper treatment. The literature has consistently shown isolated respiratory C. gleum strains to be largely susceptible to fluoroquinolones, piperacillin-tazobactam, or trimethoprim-sulfamethoxazole.


Subject(s)
Chryseobacterium/isolation & purification , Community-Acquired Infections/drug therapy , Flavobacteriaceae Infections/drug therapy , Pneumonia, Bacterial/drug therapy , Sulfadoxine/therapeutic use , Trimethoprim/therapeutic use , Anti-Infective Agents/therapeutic use , Chryseobacterium/drug effects , Drug Combinations , Humans , Male , Middle Aged
2.
Nucleic Acids Res ; 40(16): 8021-32, 2012 Sep.
Article in English | MEDLINE | ID: mdl-22661574

ABSTRACT

Hfq is an important RNA-binding protein that helps bacteria adapt to stress. Its primary function is to promote pairing between trans-acting small non-coding RNAs (sRNAs) and their target mRNAs. Identification of essential Hfq-binding motifs in up-stream regions of rpoS and fhlA led us to ask the question whether these elements are a common occurrence among other Hfq-dependent mRNAs as well. Here, we confirm the presence of a similar (ARN)(x) motif in glmS RNA, a gene controlled by two sRNAs (GlmZ and GlmY) in an Hfq-dependent manner. GlmZ represents a canonical sRNA:mRNA pairing system, whereas GlmY is non-canonical, interfacing with the RNA processing protein YhbJ. We show that glmS interacts with both Hfq-binding surfaces in the absence of sRNAs. Even though two (ARN)(x) motifs are present, using a glmS:gfp fusion system, we determined that only one specific (ARN)(x) element is essential for regulation. Furthermore, we show that residues 66-72 in the C-terminal extension of Escherichia coli Hfq are essential for activation of GlmS expression by GlmY, but not with GlmZ. This result shows that the C-terminal extension of Hfq may be required for some forms of non-canonical sRNA regulation involving ancillary components such as additional RNAs or proteins.


Subject(s)
Escherichia coli Proteins/chemistry , Escherichia coli Proteins/metabolism , Gene Expression Regulation, Bacterial , Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)/genetics , Host Factor 1 Protein/chemistry , Host Factor 1 Protein/metabolism , RNA, Messenger/chemistry , RNA, Small Untranslated/metabolism , Bacterial Proteins/metabolism , Binding Sites , Clostridioides difficile , Clostridium perfringens , Escherichia coli/genetics , Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)/metabolism , Nucleic Acid Conformation , Nucleotide Motifs , Protein Biosynthesis , Up-Regulation
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