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Genome Sequences of Acholeplasma laidlawii Strains with Increased Resistance to Tetracycline and Melittin.

ABSTRACT: Acholeplasma laidlawii is a well-suited model for studying the molecular basis for adapting mollicutes to environmental conditions. Here, we present the whole-genome sequences of two strains of A. laidlawii with increased resistance to tetracycline and melittin.

SUBMITTER: Baranova NB

PROVIDER: S-EPMC5764945 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

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Genome Sequences of Acholeplasma laidlawii Strains with Increased Resistance to Tetracycline and Melittin.

Baranova Natalia B NB Malygina Tatyana Y TY Medvedeva Elena S ES Boulygina Eugenia A EA Siniagina Maria N MN Dramchini Mohamed Amine MA Prottoy Reshad Akbor RA Mouzykantov Alexey A AA Davydova Marina N MN Chernova Olga A OA Chernov Vladislav M VM

Genome announcements 20180111 2

Acholeplasma laidlawii is a well-suited model for studying the molecular basis for adapting mollicutes to environmental conditions. Here, we present the whole-genome sequences of two strains of A. laidlawii with increased resistance to tetracycline and melittin. ...[more]

PMID: 29326221

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Genome Sequences of Acholeplasma laidlawii Strains Differing in Sensitivity to Ciprofloxacin.

Project description:Acholeplasma laidlawii is a well-suited model for study of the molecular basis of the adaptation of mollicutes to environmental conditions. Here we present the whole-genome sequences of four strains of A. laidlawii with differential sensitivity to ciprofloxacin.

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Data on proteomic profiling of extracellular vesicles of Acholeplasma laidlawii strains with increased resistance to antibiotics of different classes - ciprofloxacin and tetracycline.

Project description:To elucidate the regularities of adaptation of the representatives of class Mollicutes to antimicrobials and to identify the promising targets for eradication of mycoplasma infections and contaminations the comparative analysis of the molecular basis of bacterial resistance to antibiotics of different classes is needed. Previously, we presented the data on the whole-genome sequences of Acholeplasma laidlawii strains with different susceptibility to ciprofloxacin (GenBank: LXYB00000000.1), tetracycline (GenBank: NELO00000000.2) and melittin (GenBank: NELN00000000.2) as well as the data on cell and extracellular vesicle proteomes of melittin-resistant A. laidlawii strain [1]. The lists of extracellular vesicle proteins secreted by A. laidlawii strains with the increased resistance to ciprofloxacin (PG8R10) and tetracycline (PG8RTet) are presented here. The vesicle proteome profiles were obtained by 1D SDS-PAGE and liquid chromatography-mass spectrometry.

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Complete genome and proteome of Acholeplasma laidlawii.

Project description:We present the complete genome sequence and proteogenomic map for Acholeplasma laidlawii PG-8A (class Mollicutes, order Acholeplasmatales, family Acholeplasmataceae). The genome of A. laidlawii is represented by a single 1,496,992-bp circular chromosome with an average G+C content of 31 mol%. This is the longest genome among the Mollicutes with a known nucleotide sequence. It contains genes of polymerase type I, SOS response, and signal transduction systems, as well as RNA regulatory elements, riboswitches, and T boxes. This demonstrates a significant capability for the regulation of gene expression and mutagenic response to stress. Acholeplasma laidlawii and phytoplasmas are the only Mollicutes known to use the universal genetic code, in which UGA is a stop codon. Within the Mollicutes group, only the sterol-nonrequiring Acholeplasma has the capacity to synthesize saturated fatty acids de novo. Proteomic data were used in the primary annotation of the genome, validating expression of many predicted proteins. We also detected posttranslational modifications of A. laidlawii proteins: phosphorylation and acylation. Seventy-four candidate phosphorylated proteins were found: 16 candidates are proteins unique to A. laidlawii, and 11 of them are surface-anchored or integral membrane proteins, which implies the presence of active signaling pathways. Among 20 acylated proteins, 14 contained palmitic chains, and six contained stearic chains. No residue of linoleic or oleic acid was observed. Acylated proteins were components of mainly sugar and inorganic ion transport systems and were surface-anchored proteins with unknown functions.

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Data on proteomic profiling of cells and extracellular vesicles of the melittin-resistant Acholeplasma laidlawii strain.

Project description:Acholeplasma laidlawii (class Mollicutes), a major contaminant of cell cultures, quickly adapts to various classes of antimicrobials, including antimicrobial peptides. The extracellular vesicles of this bacterium can play a significant role in the development of drug-resistance Chernov et al., 2018. We compared the cellular and vesicular proteomes of A. laidlawii strains with differing susceptibility to melittin (an antimicrobial peptide from bee venom), the genomes of which we have previously sequenced. We extracted soluble proteins from cells and extracellular vesicles of the A. laidlawii PG8RMel strain showing an increased resistance to melittin, and compared them with the cellular proteome and a previously obtained vesicular proteome of the original (reference) A. laidlawii PG8B strain Chernov et al., 2014. The cellular proteome profile of the A. laidlawii strains differing in susceptibility to melittin was determined by using two-dimensional gel electrophoresis and MALDI-TOF/TOF MS. Here we present the cellular proteins that were differentially expressed. The vesicular proteome profile was determined by using one-dimensional electrophoresis and chromatography-mass spectrometry. A list of the extracellular vesicles proteins of the melittin-resistant A. laidlawii strain is presented here.

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Draft Genome Sequence of Acholeplasma laidlawii, a Common Contaminant of Cell Cultures.

Project description:Mollicutes are important cell culture contaminants which may eventually affect the results of biological assays or affect their interpretation. Acholeplasma laidlawii is one of the most frequent contaminants of cell cultures. Here, we report the complete genome sequence of A. laidlawii strain MDBK/IPV, recovered from Madin-Darby bovine kidney (MDBK) cells.

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Extracellular membrane vesicles and phytopathogenicity of Acholeplasma laidlawii PG8.

Project description:For the first time, the phytopathogenicity of extracellular vesicles of Acholeplasma laidlawii PG8 (a ubiquitous mycoplasma that is one of the five common species of cell culture contaminants and is a causative agent for phytomycoplasmoses) in Oryza sativa L. plants was studied. Data on the ability of extracellular vesicles of Acholeplasma laidlawii PG8 to penetrate from the nutrient medium into overground parts of Oryza sativa L. through the root system and to cause alterations in ultrastructural organization of the plants were presented. As a result of the analysis of ultrathin leaf sections of plants grown in medium with A. laidlawii PG8 vesicles, we detected significant changes in tissue ultrastructure characteristic to oxidative stress in plants as well as their cultivation along with bacterial cells. The presence of nucleotide sequences of some mycoplasma genes within extracellular vesicles of Acholeplasma laidlawii PG8 allowed a possibility to use PCR (with the following sequencing) to perform differential detection of cells and bacterial vesicles in samples under study. The obtained data may suggest the ability of extracellular vesicles of the mycoplasma to display in plants the features of infection from the viewpoint of virulence criteria--invasivity, infectivity--and toxigenicity--and to favor to bacterial phytopathogenicity.

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Resistance to 16-Membered Macrolides, Tiamulin and Lincomycin in a Swine Isolate of Acholeplasma laidlawii.

Project description:Acholeplasma (A.) laidlawii is an opportunistic pathogen with the ability to disseminate resistance determinants to antibiotics; however, its resistance to macrolides has been less studied. The aim of the present study was to characterize the mechanisms responsible for the resistance to macrolides, tiamulin and lincomycin found in a strain of A. laidlawii isolated from a pig with pneumonia. MICs of erythromycin, 15- and 16-membered macrolides, tiamulin and lincomycin were determined by microdilution method with and without reserpine, an inhibitor of ABC efflux pumps and regions of the genome were sequenced. Reserpine only decreased lincomycin MIC but it did not change the MICs of macrolides and tiamulin. The analysis of the DNA sequence of 23S rRNA showed nucleotide substitutions at eight different positions, although none of them were at positions previously related to macrolide resistance. Five mutations were found in the L22 protein, one of them at the stop codon. In addition, two mutations were found in the amino acid sequence of L4. The combination of multiple mutations in the ribosomal proteins L22 and L4 together with substitutions in 23S rRNA DNA sequence was associated with the resistance to macrolides, the pleuromutilin and lincomycin in the studied A. laidlawii strain.

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Acholeplasma laidlawii

Project description:Acholeplasma laidlawii overview

| PRJNA36069 | ENA

The acylation state of surface lipoproteins of mollicute Acholeplasma laidlawii.

Project description:Acylation of the N-terminal Cys residue is an essential, ubiquitous, and uniquely bacterial posttranslational modification that allows anchoring of proteins to the lipid membrane. In gram-negative bacteria, acylation proceeds through three sequential steps requiring lipoprotein diacylglyceryltransferase, lipoprotein signal peptidase, and finally lipoprotein N-acyltransferase. The apparent lack of genes coding for recognizable homologs of lipoprotein N-acyltransferase in gram-positive bacteria and Mollicutes suggests that the final step of the protein acylation process may be absent in these organisms. In this work, we monitored the acylation state of eight major lipoproteins of the mollicute Acholeplasma laidlawii using a combination of standard two-dimensional gel electrophoresis protein separation, blotting to nitrocellulose membranes, and MALDI-MS identification of modified N-terminal tryptic peptides. We show that for each A. laidlawii lipoprotein studied a third fatty acid in an amide linkage on the N-terminal Cys residue is present, whereas diacylated species were not detected. The result thus proves that A. laidlawii encodes a lipoprotein N-acyltransferase activity. We hypothesize that N-acyltransferases encoded by genes non-homologous to N-acyltransferases of gram-negative bacteria are also present in other mollicutes and gram-positive bacteria.

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Data on the genome and proteome profiles of ciprofloxacin-resistant Acholeplasma laidlawii strains selected under different conditions in vitro.

Project description:Acholeplasma laidlawii is widespread hypermutable bacteria (class Mollicutes) capable of infecting humans, animals, plants, which is the main contaminant of cell cultures and vaccine preparations. The mechanisms of the development of antimicrobial resistance of this bacterium are associated with the secretion of extracellular vesicles, which can mediate the lateral transfer of antibiotic resistance determinants. We compared the genome profiles of ciprofloxacin-resistant A.laidlawii strains PG8r1 (MIC 10 µg/ml) and PG8r3 (MIC 10 µg/ml) selected under different in vitro conditions - when ciprofloxacin-sensitive (MIC 0.5 µg/ml) A.laidlawii PG8B strain was cultured at increasing concentrations of ciprofloxacin in a broth medium alone, and with vesicles derived from the ciprofloxacin-resistant (MIC 20 µg/ml) A.laidlawii PG8R10c-2 strain, respectively. Genome profiles of PG8c-3 (obtained from a single colony of the strain PG8B) and PG8R10c-2 were analyzed too. Patterns of the quinolone target genes (gyrA, gyrB, parE, parC) containing in extracellular vesicles of PG8c-3, PG8R10c-2, PG8r1 and PG8r3 were determined. Genome sequencing was performed on the NextSeq Illumina platform. Search and annotation of single nucleotide polymorphisms were performed using Samtools and SnpEff, respectively. We also compared cellular proteomes of PG8c-3, PG8r1 and PG8r3. The cellular proteome profiles of the A. laidlawii strains were determined by two-dimensional gel electrophoresis and MALDI-TOF/TOF MS. This work presents data on single nucleotide polymorphisms (SNPs) found in the genomes of the ciprofloxacin-resistant strains selected under different in vitro conditions and proteins that were differentially expressed in the cells of ciprofloxacin-resistant strains selected under different conditions in vitro.

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