Figure 1. Ability of fluconazole to improve survival of G

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Figure 1. Ability of fluconazole to improve survival of G Figure 1. Ability of fluconazole to improve survival of G. mellonella infected with C. orthopsilosis isolates. (a) ... Figure 1. Ability of fluconazole to improve survival of G. mellonella infected with C. orthopsilosis isolates. (a) Survival curves of the G. mellonella infected with the different strains. (b) Fungal load in G. mellonella larvae infected with various C. orthopsilosis strains. Error bars correspond to standard deviation. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy. All rights reserved. For permissions, please email: journals.permissions@oup.com.This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model) J Antimicrob Chemother, dkz204, https://doi.org/10.1093/jac/dkz204 The content of this slide may be subject to copyright: please see the slide notes for details.

Figure 2. Molecular docking of fluconazole into the CoErg11p 3D model Figure 2. Molecular docking of fluconazole into the CoErg11p 3D model. All mutated amino acids identified in the C. ... Figure 2. Molecular docking of fluconazole into the CoErg11p 3D model. All mutated amino acids identified in the C. orthopsilosis clinical isolates (Gln211, Leu376, Ser420, Ala421, Gly458 and Val485) and four known to be in direct interaction with the haem (Tyr132, Arg381, His462 and Cys464) are indicated. Gly458 and Leu376 (surrounded in grey), located close to the active site, are represented by CPK models (grey, carbon atoms; white, hydrogen atoms; red, oxygen atoms). Fluconazole is represented by a stick model (deep orange, carbon atoms; blue, nitrogen atoms; red, oxygen atoms; green, fluorine atoms); haem is represented by a ball and stick model (khaki, carbon atoms; light orange, iron atom; red, oxygen atoms). The active site pocket is highlighted in cyan (MOLCAD surface). The H-bonds with the haem propionates are indicated as yellow dotted lines and the iron-coordinated Cys464 is seen at the top. This figure appears in colour in the online version of JAC and in black and white in the printed version of JAC. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy. All rights reserved. For permissions, please email: journals.permissions@oup.com.This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model) J Antimicrob Chemother, dkz204, https://doi.org/10.1093/jac/dkz204 The content of this slide may be subject to copyright: please see the slide notes for details.

Figure 3. CRISPR-Cas9 strategy to edit the CoERG11 gene Figure 3. CRISPR-Cas9 strategy to edit the CoERG11 gene. (a) Schematic representation of the CRISPR-Cas9 system. Once ... Figure 3. CRISPR-Cas9 strategy to edit the CoERG11 gene. (a) Schematic representation of the CRISPR-Cas9 system. Once transformed, the plasmid vector expresses the desired sgRNA, which assembles with Cas9 to form a nucleoprotein complex and triggers the double-strand DNA cleavage. DNA repair is obtained by HDR with the RT harbouring the desired mutations. After plasmid curing, transformants are screened by PCR, sequenced for checking the presence of the expected mutations and tested for fluconazole susceptibility according to the CLSI M27-A3 method. (b) Plasmid curing for the two transformants (1, 2) displaying the L376I substitution. After three passages on YPD agar at 30°C, cells are no longer resistant to nourseothricin (bottom panel, no growth on YPD + nourseothricin agar) as a consequence of the rapid loss of the plasmid containing all the CRISPR-Cas9 components, thus proving that it did not integrate into the genome. (c) Schematic representation of the strategy used to introduce the G1372A mutation (G458S). The CoERG11 gene is highlighted in orange. The target base to edit (G1372) in the WT CoERG11 sequence (top panel) is indicated by an arrow and the guide (depicted in green) is followed by the corresponding PAM (TGG, in bold). The Cas9 DNA cleavage site (3 bp upstream from the PAM) is indicated by scissors. The two silent mutations introduced in the RT (in grey) are indicated in red, with the desired G1372A being also highlighted in yellow (middle panel). The edited sequence, obtained by HDR with the RT, displays the desired G1372A (G458S) and the two CRISPR-blocking mutations (bottom panel). NTC, nourseothricin. This figure appears in colour in the online version of JAC and in black and white in the printed version of JAC. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy. All rights reserved. For permissions, please email: journals.permissions@oup.com.This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model) J Antimicrob Chemother, dkz204, https://doi.org/10.1093/jac/dkz204 The content of this slide may be subject to copyright: please see the slide notes for details.