Substrate specificity of the pyrophosphohydrolase LpxH determines the asymmetry of <i>Bordetella pertussis</i> lipid A.

Arenas, Jesús; Pupo, Elder; de Jonge, Eline; Pérez-Ortega, Jesús; Schaarschmidt, Joerg; van der Ley, Peter; Tommassen, Jan

Substrate specificity of the pyrophosphohydrolase LpxH determines the asymmetry of Bordetella pertussis lipid A.

Arenas, Jesús; Pupo, Elder; de Jonge, Eline; Pérez-Ortega, Jesús; Schaarschmidt, Joerg; van der Ley, Peter; Tommassen, Jan.

Afiliação

Arenas J; Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. Electronic address: jaarenas@unizar.es.
Pupo E; Institute for Translational Vaccinology (Intravacc), Antonie van Leeuwenhoeklaan 9, 3721 MA Bilthoven, The Netherlands.
de Jonge E; Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Pérez-Ortega J; Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Schaarschmidt J; Computational Structural Biology Group, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
van der Ley P; Institute for Translational Vaccinology (Intravacc), Antonie van Leeuwenhoeklaan 9, 3721 MA Bilthoven, The Netherlands.
Tommassen J; Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.

J Biol Chem ; 294(20): 7982-7989, 2019 05 17.

Article em En | MEDLINE | ID: mdl-30926608

Assuntos

Aciltransferases/metabolismo; Proteínas de Bactérias/metabolismo; Bordetella pertussis/enzimologia; Lipídeo A/biossíntese; Aciltransferases/química; Aciltransferases/genética; Animais; Proteínas de Bactérias/química; Proteínas de Bactérias/genética; Bordetella pertussis/genética; Células HEK293; Humanos; Lipídeo A/química; Lipídeo A/genética; Camundongos; Neisseria meningitidis/enzimologia; Neisseria meningitidis/genética; Especificidade por Substrato/fisiologia

Palavras-chave

Bordetella pertussis; LpxA; LpxH; Neisseria meningitidis; Toll-like receptor 4 (TLR4); acyl chain length; endotoxin; innate immunity; lipid A; lipopolysaccharide (LPS)

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Bordetella pertussis / Aciltransferases / Lipídeo A Limite: Animals / Humans Idioma: En Ano de publicação: 2019 Tipo de documento: Article

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