Mycoplasma hyopharyngis Isolation From Swine

Friis, N. F.; Ahrens, Peter; Hagedorn-Olsen, Tine; Nielsen, EO; Kokotovic, Branko

doi:10.1186/1751-0147-44-103

Cited by 9 publications

(7 citation statements)

References 6 publications

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“…The specificity of this last assay was tested with a collection of 34 strains of bacterial species other than M. hyorhinis (Table 1). M. hyorhinis, M. hyosynoviae, M. hyopharyngis, M. flocculare, and M. hyopneumoniae were cultivated as previously described (27,28). Streptococcus sp.…”

Section: Methodsmentioning

confidence: 99%

Multilocus Sequence Typing of Mycoplasma hyorhinis Strains Identified by a Real-Time TaqMan PCR Assay

et al. 2014

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bA real-time TaqMan PCR assay based on the gene encoding the protein p37 was developed to detect Mycoplasma hyorhinis. Its specificity was validated with 29 epidemiologically unrelated M. hyorhinis strains (28 field strains and one reference strain) and other mycoplasma species or with other microorganisms commonly found in pigs. The estimated detection limit of this qPCR assay was 125 microorganism equivalents/l. The same 29 epidemiologically unrelated M. hyorhinis strains and four previously fully sequenced strains were typed by two portable typing methods, the sequencing of the p37 gene and a multilocus sequence typing (MLST) scheme. The first method revealed 18 distinct nucleotide sequences and insufficient discriminatory power (0.934). The MLST scheme was developed with the sequenced genomes of the M. hyorhinis strains HUB-1, GDL-1, MCLD, and SK76 and based on the genes dnaA, rpoB, gyrB, gltX, adk, and gmk. In total, 2,304 bp of sequence was analyzed for each strain. MLST was capable of subdividing the 33 strains into 29 distinct sequence types. The discriminatory power of the method was >0.95, which is the threshold value for interpreting typing results with confidence (D ‫؍‬ 0.989). Population analysis showed that recombination in M. hyorhinis occurs and that strains are diverse but with a certain clonality (one unique clonal complex was identified). The new qPCR assay and the robust MLST scheme are available for the acquisition of new knowledge on M. hyorhinis epidemiology. A web-accessible database has been set up for the M. hyorhinis MLST scheme at http://pubmlst.org/mhyorhinis/.

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Section: Methodsmentioning

confidence: 99%

Multilocus Sequence Typing of Mycoplasma hyorhinis Strains Identified by a Real-Time TaqMan PCR Assay

et al. 2014

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“…In this connection it must be mentioned that Bstergdrd Kristensen et al (1 1) found that none of the 11 diffuse nontoxic goitres came within the hyperthyroid range in the T, suppression test. In other words, this 'is at variance with Friis' series (3). A comparison of the 20 yo limit with the 18 % and 15 Yo limits shows that in this respect the 20 yo limit is most advantageous (table 11).…”

Section: Similar Considerations Concerning the 4-hour Measurements Showmentioning

confidence: 74%

The Thiocyanate Suppression Test in Thyroid Disorders

Friis

Norregard

1965

Journal of Internal Medicine

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“…2.1. Monoclonal antibody generation M. hyopneumoniae strain J was grown as described previously (Friis, 1975). The cells were harvested at 20 000g upon reaching the exponential phase at pH 6.8 and were resuspended in 0.25 M NaCl.…”

Section: Methodsmentioning

confidence: 99%

Structure of P46, an immunodominant surface protein fromMycoplasma hyopneumoniae: interaction with a monoclonal antibody

Guasch

Montané²,

Moros³

et al. 2020

Acta Crystallogr D Struct Biol

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Mycoplasma hyopneumoniae is a prokaryotic pathogen that colonizes the respiratory ciliated epithelial cells in swine. Infected animals suffer respiratory lesions, causing major economic losses in the porcine industry. Characterization of the immunodominant membrane-associated proteins from M. hyopneumoniae may be instrumental in the development of new therapeutic approaches. Here, the crystal structure of P46, one of the main surface-antigen proteins, from M. hyopneumoniae is presented and shows N-and C-terminal / domains connected by a hinge. The structures solved in this work include a ligand-free open form of P46 (3.1 Å resolution) and two ligand-bound structures of P46 with maltose (2.5 Å resolution) and xylose (3.5 Å resolution) in open and closed conformations, respectively. The ligand-binding site is buried in the cleft between the domains at the hinge region. The two domains of P46 can rotate with respect to each other, giving open or closed alternative conformations. In agreement with this structural information, sequence analyses show similarities to substrate-binding members of the ABC transporter superfamily, with P46 facing the extracellular side as a functional subunit. In the structure with xylose, P46 was also bound to a high-affinity (K d = 29 nM) Fab fragment from a monoclonal antibody, allowing the characterization of a structural epitope in P46 that exclusively involves residues from the C-terminal domain. The Fab structure in the complex with P46 shows only small conformational rearrangements in the six complementarity-determining regions (CDRs) with respect to the unbound Fab (the structure of which is also determined in this work at 1.95 Å resolution). The structural information that is now available should contribute to a better understanding of sugar nutrient intake by M. hyopneumoniae. This information will also allow the design of protocols and strategies for the generation of new vaccines against this important swine pathogen. research papers Acta Cryst. (2020). D76, 418-427 Guasch et al. P46 from Mycoplasma hyopneumoniae 419

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Mycoplasma hyopharyngis Isolation From Swine

Cited by 9 publications

References 6 publications

Multilocus Sequence Typing of Mycoplasma hyorhinis Strains Identified by a Real-Time TaqMan PCR Assay

Multilocus Sequence Typing of Mycoplasma hyorhinis Strains Identified by a Real-Time TaqMan PCR Assay

The Thiocyanate Suppression Test in Thyroid Disorders

Structure of P46, an immunodominant surface protein fromMycoplasma hyopneumoniae: interaction with a monoclonal antibody

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