ArticleInfection and immunity2004
Proteolytic processing of the Mycoplasma hyopneumoniae cilium adhesin.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
51 citing papers in PubMed.
- Research Progress on Immune Evasion ofMicroorganisms · 2024Review
- Chimeric proteins of Mycoplasma hyopneumoniae as vaccine and preclinical model for immunological evaluation.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Comparative Proteomic Analysis of Secretory Proteins ofVeterinary sciences · 2023Article
- Hijacking of Host Plasminogen byMicrobiology spectrum · 2023Article
- Differential domains and endoproteolytic processing in dominant surface proteins of unknown function fromHeliyon · 2023Article
- TheFrontiers in microbiology · 2022Review
- Review
- Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae.Scientific reports · 2021Article
- Construction ofFrontiers in microbiology · 2021Article
- Novel Secreted Protein ofFrontiers in immunology · 2021Article
- Pathogenicity & virulence ofVirulence · 2020Review
- Mycoplasma hyopneumoniae J elicits an antioxidant response and decreases the expression of ciliary genes in infected swine epithelial cells.Scientific reports · 2020Article
- Mycoplasma bovis Membrane Protein MilA Is a Multifunctional Lipase with Novel Lipid and Glycosaminoglycan Binding Activity.Infection and immunity · 2020Article
- Genomic Variability and Post-translational Protein Processing Enhance the Immune Evasion ofFrontiers in immunology · 2020Review
- Combined Transcriptome Sequencing ofFrontiers in microbiology · 2020Article
- Genetic variation of Mycoplasma hyopneumoniae from Brazilian field samples.BMC microbiology · 2019Article
- Mycoplasma hyopneumoniae surface-associated proteases cleave bradykinin, substance P, neurokinin A and neuropeptide Y.Scientific reports · 2019Article
- Terminomics Methodologies and the Completeness of Reductive Dimethylation: A Meta-Analysis of Publicly Available Datasets.Proteomes · 2019Article
- Mycoplasma hyopneumoniae resides intracellularly within porcine epithelial cells.Scientific reports · 2018Article
- Extracellular Actin Is a Receptor forFrontiers in cellular and infection microbiology · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma hyopneumoniae is an economically significant swine pathogen that colonizes the respiratory ciliated epithelial cells. Cilium adherence is mediated by P97, a surface protein containing a repeating element (R1) that is responsible for binding. Here, we show that the cilium adhesin is proteolytically processed on the surface. Proteomic analysis of strain J proteins identified cleavage products of 22, 28, 66, and 94 kDa. N-terminal sequencing showed that the 66- and 94-kDa proteins possessed identical N termini and that the 66-kDa variant was generated by cleavage of the 28-kDa product from the C terminus. The 22-kDa product represented the N-terminal 195 amino acids of the cilium adhesin preprotein, confirming that the hydrophobic leader signal sequence is not cleaved during translocation across the membrane. Comparative studies of M. hyopneumoniae strain 232 showed that the major cleavage products of the cilium adhesin are similar, although P22 and P28 appear to be processed further in strain 232. Immunoblotting studies using antisera raised against peptide sequences within P22 and P66/P94 indicate that processing is complex, with cleavage occurring at different frequencies within multiple sites, and is strain specific. Immunogold electron microscopy showed that fragments containing the cilium-binding site remained associated with the cell surface whereas cleavage products not containing the R1 element were located elsewhere. Not all secreted proteins undergo multiple cleavage, however, as evidenced by the analysis of the P102 gene product. The ability of M. hyopneumoniae to selectively cleave its secreted proteins provides this pathogen with a remarkable capacity to alter its surface architecture.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.