Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5508185 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2017 | 30 Pages |
Abstract
In this review we present an overview of this family of Corynebacteriales enzymes, starting with their expression, localization, structure and activity to finally discuss their putative functions in the cell. In addition, we show that Corynebacteriales possess multiple mycoloyltransferases encoding genes in their genome. The reason for this multiplicity is not known, as their function in mycolates biogenesis appear to be only partially redundant. It is thus possible that, in some species living in specific environments, some mycoloyltransferases have evolved to gain some new functions. In any case, the few characterized mycoloyltransferases are very important for the bacterial physiology and are also involved in adaptation in the host where they constitute major secreted antigens. Although not discussed in this review, all these functions make them interesting targets for the discovery of new antibiotics and promising vaccines candidates. This article is part of a Special Issue entitled "Science for Life" Guest Editor: Dr. Austen Angell, Dr. Salvatore Magazù and Dr. Federica Migliardo
Keywords
HTSTMMMAGPTDMAg85ArabinogalactanDEPMARRMSDRNDDTTESI-MSFITCINHTrehalose monomycolateantigen 85EsteraseAmino acidsisoniazidTATTrehalose dimycolatediethyl phosphatedithiothreitolhigh throughput screeningfluorescein isothiocyanateMycobacteriumMultiple antibiotic resistanceresistance-nodulation-divisionFibronectin-binding proteinPeptidoglycan
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Authors
Nathalie Dautin, Célia de Sousa-d'Auria, Florence Constantinesco-Becker, Cécile Labarre, Jacques Oberto, Ines Li de la Sierra-Gallay, Christiane Dietrich, Hanane Issa, Christine Houssin, Nicolas Bayan,