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Deletion of MSMEG_1350 in Mycobacterium smegmatis causes loss of epoxy-mycolic acids, fitness alteration at low temperature and resistance to a set of mycobacteriophages.
Di Capua, Cecilia B; Belardinelli, Juan M; Buchieri, María V; Bortolotti, Ana; Franceschelli, Jorgelina J; Morbidoni, Héctor R.
Afiliação
  • Di Capua CB; Laboratorio de Microbiología Molecular, Cátedra de Microbiología, Facultad de Ciencias Médicas, Universidad Nacional de Rosario, Rosario, Argentina.
  • Belardinelli JM; Laboratorio de Microbiología Molecular, Cátedra de Microbiología, Facultad de Ciencias Médicas, Universidad Nacional de Rosario, Rosario, Argentina.
  • Buchieri MV; ‡â€‹Present address: Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523, USA.
  • Bortolotti A; Laboratorio de Microbiología Molecular, Cátedra de Microbiología, Facultad de Ciencias Médicas, Universidad Nacional de Rosario, Rosario, Argentina.
  • Franceschelli JJ; Laboratorio de Microbiología Molecular, Cátedra de Microbiología, Facultad de Ciencias Médicas, Universidad Nacional de Rosario, Rosario, Argentina.
  • Morbidoni HR; Laboratorio de Microbiología Molecular, Cátedra de Microbiología, Facultad de Ciencias Médicas, Universidad Nacional de Rosario, Rosario, Argentina.
Microbiology (Reading) ; 164(12): 1567-1582, 2018 12.
Article em En | MEDLINE | ID: mdl-30311878
Mycobacterium smegmatis is intrinsically resistant to thiacetazone, an anti-tubercular thiourea; however we report here that it causes a mild inhibition in growth in liquid medium. Since mycolic acid biosynthesis was affected, we cloned and expressed Mycobacterium smegmatis mycolic acid methyltransferases, postulated as targets for thiacetazone in other mycobacterial species. During this analysis we identified MSMEG_1350 as the methyltransferase involved in epoxy mycolic acid synthesis since its deletion led to their total loss. Phenotypic characterization of the mutant strain showed colony morphology alterations at all temperatures, reduced growth and a slightly increased susceptibility to SDS, lipophilic and large hydrophilic drugs at 20 °C with little effect at 37 °C. No changes were detected between parental and mutant strains in biofilm formation, sliding motility or sedimentation rate. Intriguingly, we found that several mycobacteriophages severely decreased their ability to form plaques in the mutant strain. Taken together our results prove that, in spite of being a minor component of the mycolic acid pool, epoxy-mycolates are required for a proper assembly and functioning of the cell envelope. Further studies are warranted to decipher the role of epoxy-mycolates in the M. smegmatis cell envelope.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Mycobacterium smegmatis / Metiltransferases / Micobacteriófagos / Ácidos Micólicos Tipo de estudo: Etiology_studies Idioma: En Revista: Microbiology (Reading) Assunto da revista: MICROBIOLOGIA Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Argentina País de publicação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Mycobacterium smegmatis / Metiltransferases / Micobacteriófagos / Ácidos Micólicos Tipo de estudo: Etiology_studies Idioma: En Revista: Microbiology (Reading) Assunto da revista: MICROBIOLOGIA Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Argentina País de publicação: Reino Unido