ArticleScientific reports2021
Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Environmental resistome of culturable gram-negative bacilli from the Yaque del Norte River: baseline genomic evidence for one health surveillance.Frontiers in microbiology · 2026Article
- Structural basis for antibiotic resistance by chloramphenicol acetyltransferase type A in Staphylococcus aureus.Scientific reports · 2025Article
- Multidrug-ResistantInfection and drug resistance · 2025Article
- Genomic profiling ofFrontiers in microbiology · 2025Article
- Determinants of Antibiotic Resistance and Virulence Factors in the Genome ofAntibiotics (Basel, Switzerland) · 2024Article
- Whole-genome sequence and resistance determinants of four Elizabethkingia anophelis clinical isolates collected in Hanoi, Vietnam.Scientific reports · 2024Article
- Draft Genome Sequences of Nine Stenotrophomonas maltophilia Isolates from a Freshwater Catchment Area in Hong Kong.Microbiology resource announcements · 2022Article
- Epidemiology and Characteristics ofMicroorganisms · 2022Review
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Authors and funding
11 authors.
Funding
Abstract
Elizabethkingia anophelis is an emerging multidrug resistant pathogen that has caused several global outbreaks. E. anophelis belongs to the large family of Flavobacteriaceae, which contains many bacteria that are plant, bird, fish, and human pathogens. Several antibiotic resistance genes are found within the E. anophelis genome, including a chloramphenicol acetyltransferase (CAT). CATs play important roles in antibiotic resistance and can be transferred in genetic mobile elements. They catalyse the acetylation of the antibiotic chloramphenicol, thereby reducing its effectiveness as a viable drug for therapy. Here, we determined the high-resolution crystal structure of a CAT protein from the E. anophelis NUHP1 strain that caused a Singaporean outbreak. Its structure does not resemble that of the classical Type A CATs but rather exhibits significant similarity to other previously characterized Type B (CatB) proteins from Pseudomonas aeruginosa, Vibrio cholerae and Vibrio vulnificus, which adopt a hexapeptide repeat fold. Moreover, the CAT protein from E. anophelis displayed high sequence similarity to other clinically validated chloramphenicol resistance genes, indicating it may also play a role in resistance to this antibiotic. Our work expands the very limited structural and functional coverage of proteins from Flavobacteriaceae pathogens which are becoming increasingly more problematic.
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