Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1

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 ar...

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Autores principales:	Seyed Mohammad Ghafoori, Alyssa M. Robles, Angelika M. Arada, Paniz Shirmast, David M. Dranow, Stephen J. Mayclin, Donald D. Lorimer, Peter J. Myler, Thomas E. Edwards, Misty L. Kuhn, Jade K. Forwood
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2d0fc8d578e94f488773d631f30cf36a
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spelling	oai:doaj.org-article:2d0fc8d578e94f488773d631f30cf36a2021-12-02T14:49:33ZStructural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP110.1038/s41598-021-88672-z2045-2322https://doaj.org/article/2d0fc8d578e94f488773d631f30cf36a2021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-88672-zhttps://doaj.org/toc/2045-2322Abstract 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.Seyed Mohammad GhafooriAlyssa M. RoblesAngelika M. AradaPaniz ShirmastDavid M. DranowStephen J. MayclinDonald D. LorimerPeter J. MylerThomas E. EdwardsMisty L. KuhnJade K. ForwoodNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Seyed Mohammad Ghafoori Alyssa M. Robles Angelika M. Arada Paniz Shirmast David M. Dranow Stephen J. Mayclin Donald D. Lorimer Peter J. Myler Thomas E. Edwards Misty L. Kuhn Jade K. Forwood Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1
description	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.
format	article
author	Seyed Mohammad Ghafoori Alyssa M. Robles Angelika M. Arada Paniz Shirmast David M. Dranow Stephen J. Mayclin Donald D. Lorimer Peter J. Myler Thomas E. Edwards Misty L. Kuhn Jade K. Forwood
author_facet	Seyed Mohammad Ghafoori Alyssa M. Robles Angelika M. Arada Paniz Shirmast David M. Dranow Stephen J. Mayclin Donald D. Lorimer Peter J. Myler Thomas E. Edwards Misty L. Kuhn Jade K. Forwood
author_sort	Seyed Mohammad Ghafoori
title	Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1
title_short	Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1
title_full	Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1
title_fullStr	Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1
title_full_unstemmed	Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1
title_sort	structural characterization of a type b chloramphenicol acetyltransferase from the emerging pathogen elizabethkingia anophelis nuhp1
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/2d0fc8d578e94f488773d631f30cf36a
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Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1

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