Structure of the catalytic domain of the colistin resistance enzyme MCR-1

Stojanoski, Vlatko; Sankaran, Banumathi; Prasad, B. V.  Venkataram; Poirel, Laurent; Nordmann, Patrice; Palzkill, Timothy

doi:10.1186/s12915-016-0303-0

Title: Structure of the catalytic domain of the colistin resistance enzyme MCR-1

Journal Article · 20 September 2016 · BMC Biology

DOI: https://doi.org/10.1186/s12915-016-0303-0 · OSTI ID:1377497

Stojanoski, Vlatko ^[1]; Sankaran, Banumathi ^[2]; Prasad, B. V. Venkataram ^[3]; Poirel, Laurent ^[4]; Nordmann, Patrice ^[5];

^[1]

Baylor College of Medicine, Houston, TX (United States). Verna and Marrs McLean Dept. of Biochemistry and Molecular Biology; Baylor College of Medicine, Houston, TX (United States). Dept. of Pharmacology
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Berkeley Center for Structural Biology, Molecular Biophysics and Integrated Bioimaging
Baylor College of Medicine, Houston, TX (United States). Verna and Marrs McLean Dept. of Biochemistry and Molecular Biology
Univ. of Fribourg (Switzerland). Lab. of Signal and Image Processing (INSERM), Infection, Antimicrobials, Modelling, Evolution (IAME), Dept. of Medicine, Medical and Molecular Microbiology Emerging Antibiotic Resistance Unit
Univ. of Fribourg (Switzerland). Lab. of Signal and Image Processing (INSERM), Infection, Antimicrobials, Modelling, Evolution (IAME), Dept. of Medicine, Medical and Molecular Microbiology Emerging Antibiotic Resistance Unit; Univ. of Lausanne (Switzerland). Univ. Hospital Center

Due to the paucity of novel antibiotics, colistin has become a last resort antibiotic for treating multidrug resistant bacteria. Colistin acts by binding the lipid A component of lipopolysaccharides and subsequently disrupting the bacterial membrane. The recently identified plasmid-encoded MCR-1 enzyme is the first transmissible colistin resistance determinant and is a cause for concern for the spread of this resistance trait. MCR-1 is a phosphoethanolamine transferase that catalyzes the addition of phosphoethanolamine to lipid A to decrease colistin affinity. The structure of the catalytic domain of MCR-1 at 1.32 Å reveals the active site is similar to that of related phosphoethanolamine transferases. The putative nucleophile for catalysis, threonine 285, is phosphorylated in cMCR-1 and a zinc is present at a conserved site in addition to three zincs more peripherally located in the active site. As noted for catalytic domains of other phosphoethanolamine transferases, binding sites for the lipid A and phosphatidylethanolamine substrates are not apparent in the cMCR-1 structure, suggesting that they are present in the membrane domain.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); National Institutes of Health (NIH); Robert Welch Foundation

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1377497

Journal Information:: BMC Biology, Journal Name: BMC Biology Journal Issue: 1 Vol. 14; ISSN 1741-7007

Publisher:: BioMed CentralCopyright Statement

Country of Publication:: United States

Language:: English

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Crystal Structure of the Catalytic Domain of MCR-1 (cMCR-1) in Complex with d-Xylose Liu, Zhao-Xin; Han, Zhenggang; Yu, Xiao-Li Crystals, Vol. 8, Issue 4 https://doi.org/10.3390/cryst8040172	journal	April 2018
Development of New Tools to Detect Colistin-Resistance among Enterobacteriaceae Strains Bardet, Lucie; Rolain, Jean-Marc Canadian Journal of Infectious Diseases and Medical Microbiology, Vol. 2018 https://doi.org/10.1155/2018/3095249	journal	December 2018
Mechanistic insights into transferable polymyxin resistance among gut bacteria Xu, Yongchang; Lin, Jingxia; Cui, Tao Journal of Biological Chemistry, Vol. 293, Issue 12 https://doi.org/10.1074/jbc.ra117.000924	journal	February 2018
Structure and function of lipid A–modifying enzymes Anandan, Anandhi; Vrielink, Alice Annals of the New York Academy of Sciences, Vol. 1459, Issue 1 https://doi.org/10.1111/nyas.14244	journal	September 2019
Definition of a Family of Nonmobile Colistin Resistance (NMCR‐1) Determinants Suggests Aquatic Reservoirs for MCR‐4 Zhang, Huimin; Wei, Wenhui; Huang, Man Advanced Science https://doi.org/10.1002/advs.201900038	journal	April 2019
Expanding landscapes of the diversified mcr-1-bearing plasmid reservoirs Wang, Qingjing; Sun, Jian; Li, Jun Microbiome, Vol. 5, Issue 1 https://doi.org/10.1186/s40168-017-0288-0	journal	July 2017
Synthesis of silver nanoparticle-decorated hydroxyapatite (HA@Ag) poriferous nanocomposites and the study of their antibacterial activities Ni, Zhihui; Gu, Xiuxian; He, Yali RSC Advances, Vol. 8, Issue 73 https://doi.org/10.1039/c8ra08148d	journal	January 2018
Definition of a Family of Nonmobile Colistin Resistance (NMCR‐1) Determinants Suggests Aquatic Reservoirs for MCR‐4 Zhang, Huimin; Wei, Wenhui; Huang, Man Advanced Science, Vol. 7, Issue 17 https://doi.org/10.1002/advs.202002530	journal	September 2020
Molecular characteristics of mcr-1-carrying plasmids and new mcr-1 variant recovered from polyclonal clinical Escherichia coli from Argentina and Canada Tijet, Nathalie; Faccone, Diego; Rapoport, Melina PLOS ONE, Vol. 12, Issue 7 https://doi.org/10.1371/journal.pone.0180347	journal	July 2017
Characterization of Two Novel Lipopolysaccharide Phosphoethanolamine Transferases in Pasteurella multocida and Their Role in Resistance to Cathelicidin-2 Harper, Marina; Wright, Amy; St. Michael, Frank Infection and Immunity, Vol. 85, Issue 11 https://doi.org/10.1128/iai.00557-17	journal	September 2017
Development and Multicentric Validation of a Lateral Flow Immunoassay for Rapid Detection of MCR-1-Producing Enterobacteriaceae Volland, Hervé; Dortet, Laurent; Bernabeu, Sandrine Journal of Clinical Microbiology, Vol. 57, Issue 5 https://doi.org/10.1128/jcm.01454-18	journal	March 2019
Synthesis of DNA-guided silver nanoparticles on a graphene oxide surface: enhancing the antibacterial effect and the wound healing activity Tong, Chunyi; Zou, Wei; Ning, Weimin RSC Advances, Vol. 8, Issue 49 https://doi.org/10.1039/c8ra04933e	journal	January 2018
Comprehensive proteomic and metabolomic profiling of mcr-1-mediated colistin resistance in Escherichia coli Li, Hui; Wang, Yingyu; Meng, Qingshi International Journal of Antimicrobial Agents, Vol. 53, Issue 6 https://doi.org/10.1016/j.ijantimicag.2019.02.014	journal	June 2019
Molecular characteristics of mcr-1-carrying plasmids and new mcr-1 variant recovered from polyclonal clinical Escherichia coli from Argentina and Canada Tijet, Nathalie; Faccone, Diego; Rapoport, Melina PLOS ONE, Vol. 12, Issue 7 https://doi.org/10.1371/journal.pone.0180347	journal	July 2017
Structural and functional insights into MCR-2 mediated colistin resistance Wang, Xudong; Lu, Qiong; Qi, Jianxun Science China Life Sciences, Vol. 61, Issue 11 https://doi.org/10.1007/s11427-018-9363-4	journal	September 2018
Development of novel antibodies for detection of mobile colistin-resistant bacteria contaminated in meats He, Xiaohua; Mavrici, Daniela; Patfield, Stephanie Scientific Reports, Vol. 8, Issue 1 https://doi.org/10.1038/s41598-018-34764-2	journal	November 2018
Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding Anandan, Anandhi; Evans, Genevieve L.; Condic-Jurkic, Karmen Proceedings of the National Academy of Sciences, Vol. 114, Issue 9 https://doi.org/10.1073/pnas.1612927114	journal	February 2017
Mcr colistin resistance gene: a systematic review of current diagnostics and detection methods Osei Sekyere, John MicrobiologyOpen, Vol. 8, Issue 4 https://doi.org/10.1002/mbo3.682	journal	July 2018
Expanding landscapes of the diversified mcr-1-bearing plasmid reservoirs Bachar, Hassan,; Xing-Ping, Li,; Jun, Li, The University of North Carolina at Chapel Hill University Libraries https://doi.org/10.17615/y6nk-5947	text	January 2017
Defining ICR-Mo, an intrinsic colistin resistance determinant from Moraxella osloensis Wei, Wenhui; Srinivas, Swaminath; Lin, Jingxia PLOS Genetics, Vol. 14, Issue 5 https://doi.org/10.1371/journal.pgen.1007389	journal	May 2018
Definition of a Family of Nonmobile Colistin Resistance (NMCR‐1) Determinants Suggests Aquatic Reservoirs for MCR‐4 Zhang, Huimin; Wei, Wenhui; Huang, Man Advanced Science https://doi.org/10.1002/advs.201900038	journal	April 2019

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Additional file 1: Figure S1. of Structure of the catalytic domain of the colistin resistance enzyme MCR-1 Stojanoski, Vlatko; Sankaran, Banumathi; Prasad, B. https://doi.org/10.6084/m9.figshare.c.3642518_d1.v1 The current record is supplemented by this dataset	dataset	September 2016
Structure of the catalytic domain of the colistin resistance enzyme MCR-1 Stojanoski, Vlatko; Sankaran, Banumathi; Prasad, B. https://doi.org/10.6084/m9.figshare.c.3642518 The current record is supplemented by this dataset	dataset	September 2016
Additional file 1: Figure S1. of Structure of the catalytic domain of the colistin resistance enzyme MCR-1 Stojanoski, Vlatko; Sankaran, Banumathi; Prasad, B. https://doi.org/10.6084/m9.figshare.c.3642518_d1 The current record is supplemented by this dataset	dataset	September 2016
Structure of the catalytic domain of the colistin resistance enzyme MCR-1 Stojanoski, Vlatko; Sankaran, Banumathi; Prasad, B. https://doi.org/10.6084/m9.figshare.c.3642518.v1 The current record is supplemented by this dataset	dataset	September 2016