Role of Alanine Racemase Mutations in Mycobacterium tuberculosis d -Cycloserine Resistance | Zendy

Yoshio Nakatani | Zendy; Helen K. OpelReading | Zendy; Matthias Merker | Zendy; Diana Machado | Zendy; Sönke Andres | Zendy; S Siva Kumar | Zendy; Danesh Moradigaravand | Zendy; Francesc Coll | Zendy; João Perdigão | Zendy; Isabel Portugal | Zendy; Thomas Schön | Zendy; Diir | Zendy; Kangjam Rekha Devi | Zendy; Thomas A. Kohl | Zendy; Patrick Beckert | Zendy; Taane G. Clark | Zendy; Gugu Maphalala | Zendy; Derrick Khumalo | Zendy; Roland Diel | Zendy; Kadri Klaos | Zendy; Htin Aung | Zendy; Gregory M. Cook | Zendy; Julian Parkhill | Zendy; Sharon J. Peacock | Zendy; Soumya Swaminathan | Zendy; Miguel Viveiros | Zendy; Stefan Niemann | Zendy; Kurt L. Krause | Zendy; Claudio U. Köser | Zendy

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Role of Alanine Racemase Mutations in Mycobacterium tuberculosis d -Cycloserine Resistance

Author(s) -

Yoshio Nakatani,

Helen K. OpelReading,

Matthias Merker,

Diana Machado,

Sönke Andres,

S Siva Kumar,

Danesh Moradigaravand,

Francesc Coll,

João Perdigão,

Isabel Portugal,

Thomas Schön,

Diir,

Kangjam Rekha Devi,

Thomas A. Kohl,

Patrick Beckert,

Taane G. Clark,

Gugu Maphalala,

Derrick Khumalo,

Roland Diel,

Kadri Klaos,

Htin Aung,

Gregory M. Cook,

Julian Parkhill,

Sharon J. Peacock,

Soumya Swaminathan,

Miguel Viveiros,

Stefan Niemann,

Kurt L. Krause,

Claudio U. Köser

Publication year - 2017

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.01575-17

Subject(s) - cycloserine , mycobacterium tuberculosis , microbiology and biotechnology , biology , mutation , drug resistance , in vitro , alanine , tuberculosis , genetics , antibiotics , gene , amino acid , medicine , pathology

A screening of more than 1,500 drug-resistant strains of Mycobacterium tuberculosis revealed evolutionary patterns characteristic of positive selection for three alanine racemase (Alr) mutations. We investigated these mutations using molecular modeling, in vitro MIC testing, as well as direct measurements of enzymatic activity, which demonstrated that these mutations likely confer resistance to d-cycloserine.

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