Changes in flagellin glycosylation affect Campylobacter autoagglutination and virulence
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Analysis of the complete flagellin glycosylation locus of Campylobacter jejuni strain 81-176 revealed a less complex genomic organization than the corresponding region in the genome strain, C. jejuni NCTC 11168. Twenty-four of the 45 genes found between Cj1293 and Cj1337 in NCTC 11168 are missing in 81-176. Mutation of six new genes, in addition to three previously reported, resulted in a non-motile phenotype, consistent with a role in synthesis of pseudaminic acid (PseAc) or transfer of PseAc to flagellin. Mutation of Cj1316c or pseA had been shown to result in loss of the acetamidino form of pseudaminic acid (PseAm). Mutation of a second gene also resulted in loss of PseAm, as well as a minor modification that appears to be PseAm extended with N-acetyl-glutamic acid. Previously described mutants in C. jejuni 81-176 and Campylobacter coli VC167 that produced flagella lacking PseAm or PseAc failed to autoagglutinate. This suggests that interactions between modifications on adjacent flagella filaments are required for autoagglutination. Mutants (81-176) defective in autoagglutination showed a modest reduction in adherence and invasion of INT407 cells. However, there was a qualitative difference in binding patterns to INT407 cells using GFP-labelled 81-176 and mutants lacking PseAm. A mutant lacking PseAm was attenuated in the ferret diarrhoeal disease model.
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Proteinaceous autoagglutinins include pili and fimbriae, flagella, large adhesin proteins such as M proteins and MSCRAMMs, and small β-barrel proteins.
“Proteinaceous autoagglutinins include pili and fimbriae [30],[46], flagella [28],[29], large adhesin proteins such as M proteins and MSCRAMMs (for microbial surface components recognising adhesive matrix molecules) [49],[52], and small β-barrel proteins [36],[56].”
From Bacterial autoaggregation (2018) · cites this paper as [28]
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“The time required for observing sedimentation this way varies depending on the agglutinins and bacteria present, from a few minutes to several hours to overnight [15,21,28,36].”
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- Authors
- Guerry, P., Ewing, C. P., Schirm, M., Lorenzo, M., Kelly, J., Pattarini, D., Majam, G., Thibault, P., & Logan, S.
- Affiliations
- Naval Medical Research Command (US)
- Institute for Research in Immunology and Cancer (CA)
- National Research Council Canada (CA)
- Corresponding author
- Guerry, Patricia
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2006-02-23
- Volume
- 60
- Issue
- 2
- Pages
- 299-311
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- PMC
- PMC1424674
- OpenAlex
- W2134062395
- Cited by
- 265
- References
- 58
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 11 · 2023: 8 · 2022: 6 · 2021: 16 · 2020: 15 · 2019: 10 · 2018: 12 · 2017: 10 · 2016: 14 · 2015: 16 · 2014: 26 · 2013: 17 · 2012: 13
- FWCI
- 26.30
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Genomic Health
- National Medical Research Council
- National Institute of Allergy and Infectious Diseases (R01 AI 43559, R01AI043559)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Salmonella and Campylobacter epidemiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
- Keywords
- Campylobacter jejuni, flagellin glycosylation, pseudaminic acid, flagellar motility, virulence, adherence, intestinal invasion, deletion mutants
- MeSH terms
- Agglutination, Base Sequence, Cell Adhesion, DNA Mutational Analysis, Flagellin, Genes, Bacterial, Glycosylation, Intestinal Mucosa, Molecular Sequence Data, Virulence, Campylobacter jejuni, Genome, Bacterial
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