ArticleJournal of bacteriology2004
Mycoplasma hyopneumoniae p65 surface lipoprotein is a lipolytic enzyme with a preference for shorter-chain fatty acids.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
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- A novel fusion protein candidate for the serodiagnosis of Mycoplasma agalactiae infection.BMC veterinary research · 2022Article
- Pathogenicity and virulence ofVirulence · 2022Review
- Development of a Multi-Epitope Vaccine forInternational journal of molecular sciences · 2022Article
- TheFrontiers in microbiology · 2022Review
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- Combined Transcriptome Sequencing ofFrontiers in microbiology · 2020Article
- Serum metabolite markers of early Mycoplasma hyopneumoniae infection in pigs.Veterinary research · 2019Article
- Quantitative Proteomic Analyses of a Pathogenic Strain and Its Highly Passaged Attenuated Strain ofBioMed research international · 2019Article
- Development of a blocking ELISA for detection of Mycoplasma hyopneumoniae infection based on a monoclonal antibody against protein P65.The Journal of veterinary medical science · 2016Article
- A novel esterase from a marine mud metagenomic library for biocatalytic synthesis of short-chain flavor esters.Microbial cell factories · 2016Article
- Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae.Open biology · 2016Article
- Development of a recombinant protein-based enzyme-linked immunosorbent assay for diagnosis of Mycoplasma bovis infection in cattle.Clinical and vaccine immunology : CVI · 2014Article
- Article
- The Mycoplasma gallisepticum virulence factor lipoprotein MslA is a novel polynucleotide binding protein.Infection and immunity · 2013Article
- Comparative genomic analyses of Mycoplasma hyopneumoniae pathogenic 168 strain and its high-passaged attenuated strain.BMC genomics · 2013Article
- A novel esterase gene cloned from a metagenomic library from neritic sediments of the South China Sea.Microbial cell factories · 2011Article
- Mycoplasma hyopneumoniae mhp379 is a Ca2+-dependent, sugar-nonspecific exonuclease exposed on the cell surface.Journal of bacteriology · 2007Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma hyopneumoniae is the most significant bacterial pathogen of the respiratory tract of swine. p65 is an immunodominant surface lipoprotein of M. hyopneumoniae that is specifically recognized during disease. Analysis of the translated amino acid sequence of the gene encoding p65 revealed similarity to the GDSL family of lipolytic enzymes. To examine the lipolytic activity of p65, the gene was cloned and expressed in Escherichia coli after truncation of the prokaryotic lipoprotein signal sequence and mutagenesis of the mycoplasma TGA tryptophan codons. After treatment with thrombin, the recombinant glutathione S-transferase (GST)-p65 protein yielded a 66-kDa fusion protein cleavage product corresponding in size to the mature p65 protein. The esterase activity of recombinant GST-p65 was indicated by the formation of a cleared zone on tributyrin agar plates and the hydrolysis of p-nitrophenyl esters of caproate (pNPC) and p-nitrophenyl esters of palmitate (pNPP). Lipase activity was indicated by the hydrolysis of the artificial triglyceride 1,2-O-dilauryl-rac-glycero-3-glutaric acid resorufin ester. Using pNPC and pNPP as substrates, recombinant GST-p65 had optimal activity between pHs 9.2 and 10.2 and at a temperature higher than 39 degrees C. Calcium ions did not increase the activity of recombinant GST-p65. Rabbit anti-p65 antibodies inhibited the activity of recombinant GST-p65 and also inhibited the growth of M. hyopneumoniae in vitro. Examination of the kinetic parameters of recombinant GST-p65 for the hydrolysis of pNPC and pNPP indicated a preference for the shorter fatty acid chain of pNPC. The physiological and/or pathogenic role of mycoplasma lipolytic enzymes has not been determined, but they are likely to play an important role in mycoplasmas' nutritional requirements for long-chain fatty acids and may reduce the function of lung surfactants in mycoplasma-induced respiratory diseases. This is the first report of the lipolytic activity of a lipid-modified surface immunogen of a mycoplasma.
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