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Feriruminatoris

ABSTRACT: Complete genome sequence of 6 Mycoplasma feriruminatoris strains, fast-growing mycoplasma species isolated in Switzerland

PROVIDER: PRJEB35485 | ENA |

REPOSITORIES: ENA

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Dataset's files

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			Action	DRS
	ERR3938361_subreads.fastq.gz	Fastqsanger.gz
	ERR3938362_1.fastq.gz	Fastqsanger.gz
	ERR3938362_2.fastq.gz	Fastqsanger.gz
	ERR3938363_subreads.fastq.gz	Fastqsanger.gz
	ERR3938364_subreads.fastq.gz	Fastqsanger.gz

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Project description:The Mycoplasma Immunoglobulin Binding/Protease (MIB-MIP) system is a candidate virulence factor present in multiple pathogenic species of the Mollicutes, including the fast-growing species Mycoplasma feriruminatoris. The MIB-MIP system cleaves the heavy chain of host immunoglobulins, hence affecting antigen-antibody interactions and potentially facilitating immune evasion. In this work, using -omics technologies and 5’RACE, we show that the four copies of the M. feriruminatoris MIB-MIP system have different expression levels and are transcribed as operons controlled by four different promoters. Individual MIB-MIP gene pairs of M. feriruminatoris and other Mollicutes were introduced in an engineered M. feriruminatoris strain devoid of MIB-MIP genes and were tested for their functionality using newly developed oriC-based plasmids. The two proteins are functionally expressed at the surface of M. feriruminatoris, which confirms the possibility to display large membrane-associated proteins in this bacterium. However, functional expression of heterologous MIB-MIP systems introduced in this engineered strain from phylogenetically distant porcine Mollicutes like Mesomycoplasma hyorhinis or Mesomycoplasma hyopneumoniae could not be achieved. Finally, since M. feriruminatoris is a candidate for biomedical applications such as drug delivery, we confirmed its safety in vivo in domestic goats, which are the closest livestock relatives to its native host the Alpine ibex.

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