Antibiotic resistance of Mycoplasma Synoviae strains isolated in China from 2016 to 2019

Abstract Background In the past decade, Mycoplasma synoviae (M. synoviae) infection has become widely prevalent in China, has caused serious economic losses and has become one of the most important diseases in the chicken industry. Medication is a general approach for the control of M. synoviae infection, but antibiotics are sometimes ineffective in clinical practice. To investigate the sensitivity of M. synoviae to antimicrobials commonly used in the treatment of M. synoviae infection, the antibiotic susceptibility of 32 M. synoviae strains isolated from China from 2016 to 2019 were determined using the minimum inhibitory concentration (MIC) method. Results All isolates had low MIC values for the combination of lincomycin and spectinomycin, pleuromutilin, and macrolides. However, the M. synoviae isolates displayed variance in MICs for doxycycline hydrochloride with a range of 0.25 to 8 μg/mL, and oxytetracycline hydrochloride with a range of 0.5 to 8 μg/mL. Three and one M. synoviae isolates showed intermediate MIC values to doxycycline hydrochloride and oxytetracycline hydrochloride, respectively. High MIC values for enrofloxacin were detected in all isolates with MICs ranging from 4 to 32 μg/mL. Furthermore, comparison of the parC QRDR identified a mutation at nucleotide position 254 (C254T) resulting in a Thr 85 Ile amino acid change in all M. synoviae isolates and the reference strain ATCC 25204 being resistant to enrofloxacin. Moreover, mutations at Glu 804 Gly and Thr 686 Ala of gyrA QRDR were identified in all M. synoviae isolates and ATCC 25204. The mutation in the QRDR of the parE gene resulted in amino acid changes at positions 197 (Pro to Ser) in 27/32 M. synoviae isolates. Conclusion Three nonsynonymous mutations in gyrA and parE were first identified to be related to enrofloxacin resistance. Our results showed that M. synoviae resistance to enrofloxacin is widespread.

Download Full-text

Complete and Draft Genome Sequences of Amino Acid-Producing Corynebacterium glutamicum Strains ATCC 21799 and ATCC 31831 and Their Genomic Islands

Microbiology Resource Announcements ◽

10.1128/mra.00430-20 ◽

2020 ◽

Vol 9 (32) ◽

Author(s):

Hideo Kawaguchi ◽

Takashi Sazuka ◽

Akihiko Kondo

Keyword(s):

Amino Acid ◽

Corynebacterium Glutamicum ◽

Reference Strain ◽

Draft Genome ◽

Genomic Islands ◽

Strain Atcc ◽

Genome Sequences ◽

Coding Sequences ◽

Content Type

ABSTRACT We determined the complete and draft genome sequences of two strains of Corynebacterium glutamicum and revealed their genomic islands (GEIs). The two strains, ATCC 21799 and ATCC 31831, were found to have 3,079 and 3,109 coding sequences, respectively, with 13 GEIs each not present in the reference strain, ATCC 13032.

Download Full-text

Mutations in the gyrA and parC genes in fluoroquinolone-resistant clinical isolates of Pseudomonas aeruginosa.

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.41.10.2289 ◽

1997 ◽

Vol 41 (10) ◽

pp. 2289-2291 ◽

Cited By ~ 51

Author(s):

M Nakano ◽

T Deguchi ◽

T Kawamura ◽

M Yasuda ◽

M Kimura ◽

...

Keyword(s):

Pseudomonas Aeruginosa ◽

Amino Acid ◽

Amino Acid Change ◽

Susceptible Strain ◽

Clinical Isolates ◽

Single Amino Acid ◽

Strain Atcc ◽

Single Amino Acid Change ◽

Double Amino Acid

We determined partial sequences of the gyrA and parC genes of the fluoroquinolone-susceptible strain ATCC 27853 and 22 clinical isolates of Pseudomonas aeruginosa. While a single amino acid change in GyrA with or without a change in ParC was found in 14 isolates with decreased susceptibility to fluoroquinolones, 3 higher-level fluoroquinolone-resistant isolates had a double amino acid change in GyrA and a single amino acid change in ParC.

Download Full-text

Paris I Dysfibrinogenemia: A Point Mutation in Intron 8 Results in Insertion of a 15 Amino Acid Sequence in the Fibrinogen γ-Chain

Thrombosis and Haemostasis ◽

10.1055/s-0038-1651583 ◽

1993 ◽

Vol 69 (03) ◽

pp. 217-220 ◽

Cited By ~ 12

Author(s):

Jonathan B Rosenberg ◽

Peter J Newman ◽

Michael W Mosesson ◽

Marie-Claude Guillin ◽

David L Amrani

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Point Mutation ◽

Genomic Dna ◽

Comparative Sequence Analysis ◽

Chain Gene ◽

Molecular Defect ◽

Nucleotide Position ◽

Normal Individuals ◽

Polymerase Chain

SummaryParis I dysfibrinogenemia results in the production of a fibrinogen molecule containing a functionally abnormal γ-chain. We determined the basis of the molecular defect using polymerase chain reaction (PCR) to amplify the γ-chain region of the Paris I subject’s genomic DNA. Comparative sequence analysis of cloned PCR segments of normal and Paris I genomic DNA revealed only an A→G point mutation occurring at nucleotide position 6588 within intron 8 of the Paris I γ-chain gene. We examined six normal individuals and found only normal sequence in this region, indicating that this change is not likely to represent a normal polymorphism. This nucleotide change leads to a 45 bp fragment being inserted between exons 8 and 9 in the mature γparis I chain mRNA, and encodes a 15 amino acid insert after γ350 [M-C-G-E-A-L-P-M-L-K-D-P-C-Y]. Alternative splicing of this region from intron 8 into the mature Paris I γ-chain mRNA also results after translation into a substitution of S for G at position γ351. Biochemical studies of 14C-iodoacetamide incorporation into disulfide-reduced Paris I and normal fibrinogen corroborated the molecular biologic predictions that two additional cysteine residues exist within the γpariS I chain. We conclude that the insertion of this amino acid sequence leads to a conformationallyaltered, and dysfunctional γ-chain in Paris I fibrinogen.

Download Full-text

Faculty Opinions recommendation of A single amino acid change (Asp 53 --> Ala53) converts Survivin from anti-apoptotic to pro-apoptotic.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1018104.207609 ◽

2004 ◽

Author(s):

William Earnshaw

Keyword(s):

Amino Acid ◽

Amino Acid Change ◽

Single Amino Acid ◽

Single Amino Acid Change

Download Full-text

Single amino acid changes in the mumps virus haemagglutinin–neuraminidase and polymerase proteins are associated with neuroattenuation

Journal of General Virology ◽

10.1099/vir.0.009449-0 ◽

2009 ◽

Vol 90 (7) ◽

pp. 1741-1747 ◽

Cited By ~ 11

Author(s):

Tahir H. Malik ◽

Candie Wolbert ◽

Laura Nerret ◽

Christian Sauder ◽

Steven Rubin

Keyword(s):

Amino Acid ◽

Clinical Isolate ◽

Amino Acid Change ◽

Mumps Virus ◽

Site Directed Mutagenesis ◽

Single Amino Acid ◽

Supporting Evidence ◽

L Protein ◽

Single Amino Acid Change

It has previously been shown that three amino acid changes, one each in the fusion (F; Ala/Thr-91→Thr), haemagglutinin–neuraminidase (HN; Ser-466→Asn) and polymerase (L; Ile-736→Val) proteins, are associated with attenuation of a neurovirulent clinical isolate of mumps virus (88-1961) following serial passage in vitro. Here, using full-length cDNA plasmid clones and site-directed mutagenesis, it was shown that the single amino acid change in the HN protein and to a lesser extent, the change in the L protein, resulted in neuroattenuation, as assessed in rats. The combination of both amino acid changes caused neuroattenuation of the virus to levels previously reported for the clinical isolate following attenuation in vitro. The amino acid change in the F protein, despite having a dramatic effect on protein function in vitro, was previously shown to not be involved in the observed neuroattenuation, highlighting the importance of conducting confirmatory in vivo studies. This report provides additional supporting evidence for the role of the HN protein as a virulence factor and, as far as is known, is the first report to associate an amino acid change in the L protein with mumps virus neuroattenuation.

Download Full-text

An Amino Acid Change in the DNA-Binding Region of Sry, found in Mus Musculus Domesticus and Other Species, does not Explain CS7BL/6J-yDOM Sex-Reversal

Biochemical and Biophysical Research Communications ◽

10.1016/s0006-291x(05)90001-6 ◽

1992 ◽

Vol 185 (1) ◽

pp. 310-316 ◽

Cited By ~ 7

Author(s):

Penelope E. Graves ◽

Robert P. Erickson

Keyword(s):

Amino Acid ◽

Dna Binding ◽

Mus Musculus ◽

Amino Acid Change ◽

Sex Reversal ◽

Mus Musculus Domesticus ◽

Binding Region

Download Full-text

Novel Seleno- and Thio-Urea Containing Dihydropyrrol-2-One Analogues as Antibacterial Agents

Antibiotics ◽

10.3390/antibiotics10030321 ◽

2021 ◽

Vol 10 (3) ◽

pp. 321

Author(s):

Shekh Sabir ◽

Tsz Tin Yu ◽

Rajesh Kuppusamy ◽

Basmah Almohaywi ◽

George Iskander ◽

...

Keyword(s):

Antibacterial Activity ◽

Antibiotic Resistance ◽

Quorum Sensing ◽

Antibacterial Agents ◽

Inhibitory Concentration ◽

Resistant Bacteria ◽

Drug Resistant ◽

Positive Bacterium ◽

Quorum Sensing Inhibition ◽

Drug Resistant Bacteria

The quorum sensing (QS) system in multi-drug-resistant bacteria such as P. aeruginosa is primarily responsible for the development of antibiotic resistance and is considered an attractive target for antimicrobial drug discovery. In this study, we synthesised a series of novel selenourea and thiourea-containing dihydropyrrol-2-one (DHP) analogues as LasR antagonists. The selenium DHP derivatives displayed significantly better quorum-sensing inhibition (QSI) activities than the corresponding sulphur analogues. The most potent analogue 3e efficiently inhibited the las QS system by 81% at 125 µM and 53% at 31 µM. Additionally, all the compounds were screened for their minimum inhibitory concentration (MIC) against the Gram-positive bacterium S. aureus, and interestingly, only the selenium analogues showed antibacterial activity, with 3c and 3e being the most potent with a MIC of 15.6 µM.

Download Full-text

Temporal Variations in Patterns of Clostridioides difficile Strain Diversity and Antibiotic Resistance in Thailand

Antibiotics ◽

10.3390/antibiotics10060714 ◽

2021 ◽

Vol 10 (6) ◽

pp. 714

Author(s):

Supapit Wongkuna ◽

Tavan Janvilisri ◽

Matthew Phanchana ◽

Phurt Harnvoravongchai ◽

Amornrat Aroonnual ◽

...

Keyword(s):

Antibiotic Resistance ◽

Antimicrobial Susceptibility ◽

Reference Strain ◽

Toxin Production ◽

Temporal Variations ◽

Toxin Gene ◽

Data Sets ◽

Clostridioides Difficile ◽

Life Threatening ◽

Susceptibility Profiles

Clostridioides difficile has been recognized as a life-threatening pathogen that causes enteric diseases, including antibiotic-associated diarrhea and pseudomembranous colitis. The severity of C. difficile infection (CDI) correlates with toxin production and antibiotic resistance of C. difficile. In Thailand, the data addressing ribotypes, toxigenic, and antimicrobial susceptibility profiles of this pathogen are scarce and some of these data sets are limited. In this study, two groups of C. difficile isolates in Thailand, including 50 isolates collected from 2006 to 2009 (THA group) and 26 isolates collected from 2010 to 2012 (THB group), were compared for toxin genes and ribotyping profiles. The production of toxins A and B were determined on the basis of toxin gene profiles. In addition, minimum inhibitory concentration of eight antibiotics were examined for all 76 C. difficile isolates. The isolates of the THA group were categorized into 27 A−B+CDT− (54%) and 23 A-B-CDT- (46%), while the THB isolates were classified into five toxigenic profiles, including six A+B+CDT+ (23%), two A+B+CDT− (8%), five A−B+CDT+ (19%), seven A−B+CDT− (27%), and six A−B−CDT− (23%). By visually comparing them to the references, only five ribotypes were identified among THA isolates, while 15 ribotypes were identified within THB isolates. Ribotype 017 was the most common in both groups. Interestingly, 18 unknown ribotyping patterns were identified. Among eight tcdA-positive isolates, three isolates showed significantly greater levels of toxin A than the reference strain. The levels of toxin B in 3 of 47 tcdB-positive isolates were significantly higher than that of the reference strain. Based on the antimicrobial susceptibility test, metronidazole showed potent efficiency against most isolates in both groups. However, high MIC values of cefoxitin (MICs 256 μg/mL) and chloramphenicol (MICs ≥ 64 μg/mL) were observed with most of the isolates. The other five antibiotics exhibited diverse MIC values among two groups of isolates. This work provides evidence of temporal changes in both C. difficile strains and patterns of antimicrobial resistance in Thailand.

Download Full-text