ArticleJournal of bacteriology1998
Cloning and comparison of fliC genes and identification of glycosylation in the flagellin of Pseudomonas aeruginosa a-type strains.
Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 121 citations in OpenAlex.
- Asymmetric sheath coordination controls flagellar architecture and function in Leptospira spirochete.The EMBO journal · 2026Article
- Specialization of independently acquired flagellar FliC proteins in plant-associatedProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Specialization of independently acquired flagellar FliC proteins in plant-associatedbioRxiv : the preprint server for biology · 2026Article
- Elucidation of the Glycan Structure of the b-type Flagellin ofACS infectious diseases · 2025Article
- The O-glycan is essential for the induction of protective antibodies against lethal infection by flagella A-bearingInfection and immunity · 2024Article
- Dual function of the O-antigen WaaL ligase of Aggregatibacter actinomycetemcomitans.Molecular oral microbiology · 2023Article
- Amber-codon suppression for spatial localization and in vivo photoaffinity capture of the interactome of the Pseudomonas aeruginosa rare lipoprotein A lytic transglycosylase.Protein science : a publication of the Protein Society · 2023Article
- Bacterial Flagellar Filament: A Supramolecular Multifunctional Nanostructure.International journal of molecular sciences · 2021Review
- Exoproteomics for Better UnderstandingToxins · 2020Review
- Microfluidic-based transcriptomics reveal force-independent bacterial rheosensing.Nature microbiology · 2019Article
- Article
- Whole-Genome Sequence of Multidrug-Resistant Pseudomonas aeruginosa Strain BAMCPA07-48, Isolated from a Combat Injury Wound.Genome announcements · 2016Article
- Cloning, Expression, and Purification of Pseudomonas aeruginosa Flagellin, and Characterization of the Elicited Anti-Flagellin Antibody.Iranian Red Crescent medical journal · 2016Article
- Type IV pilus glycosylation mediates resistance of Pseudomonas aeruginosa to opsonic activities of the pulmonary surfactant protein A.Infection and immunity · 2015Article
- Bacterial flagella: twist and stick, or dodge across the kingdoms.PLoS pathogens · 2015Review
- The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014Review
- Gram-negative flagella glycosylation.International journal of molecular sciences · 2014Review
- Flagellar glycosylation in Burkholderia pseudomallei and Burkholderia thailandensis.Journal of bacteriology · 2011Article
- Protein glycosylation in bacteria: sweeter than ever.Nature reviews. Microbiology · 2010Review
- Interleukin-8 production by human airway epithelial cells in response to Pseudomonas aeruginosa clinical isolates expressing type a or type b flagellins.Clinical and vaccine immunology : CVI · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudomonas aeruginosa a-type strains produce flagellin proteins which vary in molecular weight between strains. To compare the properties of a-type flagellins, the flagellin genes of several Pseudomonas aeruginosa a-type strains, as determined by interaction with specific anti-a monoclonal antibody, were cloned and sequenced. PCR amplification of the a-type flagellin gene fragments from five strains each yielded a 1.02-kb product, indicating that the gene size is not likely to be responsible for the observed molecular weight differences among the a-type strains. The flagellin amino acid sequences of several a-type strains (170,018, 5933, 5939, and PAK) were compared, and that of 170,018 was compared with that of PAO1, a b-type strain. The former comparisons revealed that a-type strains are similar in amino acid sequence, while the latter comparison revealed differences between 170,018 and PAO1. Posttranslational modification was explored for its contribution to the observed differences in molecular weight among the a-type strains. A biotin-hydrazide glycosylation assay was performed on the flagellins of three a-type strains (170,018, 5933, and 5939) and one b-type strain (M2), revealing a positive glycosylation reaction for strains 5933 and 5939 and a negative reaction for 170,018 and M2. Deglycosylation of the flagellin proteins with trifluoromethanesulfonic acid (TFMS) confirmed the glycosylation results. A molecular weight shift was observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis for the TFMS-treated flagellins of 5933 and 5939. These results indicate that the molecular weight discrepancies observed for the a-type flagellins can be attributed, at least in part, to glycosylation of the protein. Anti-a flagellin monoclonal antibody reacted with the TFMS-treated flagellins, suggesting that the glycosyl groups are not a necessary component of the epitope for the human anti-a monoclonal antibody. Comparisons between a-type sequences and a b-type sequence (PAO1) will aid in delineation of the epitope for this monoclonal antibody.
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