Understanding Vibrio cholerae's Lipid A and Its Role in Immune Response
Author Information
Author(s): Hankins Jessica V, Madsen James A, Giles David K, Childers Brandon M, Klose Karl E, Brodbelt Jennifer S, Trent M Stephen
Primary Institution: Georgia Health Sciences University
Hypothesis
Does the secondary acyltransferase Vc0212 (LpxN) in Vibrio cholerae play a role in lipid A modification and immune recognition?
Conclusion
The study identifies Vc0212 as a novel lipid A secondary acyltransferase that enhances polymyxin B resistance and is crucial for TLR4 activation.
Supporting Evidence
- V. cholerae serogroups O1 and O139 synthesize a similar hexa-acylated lipid A species.
- The presence of a 3-hydroxyl group on the secondary acyl chain promotes antimicrobial peptide resistance.
- Loss of Vc0212 activity resulted in a significant decrease in polymyxin B resistance.
- Hexa-acylation of V. cholerae LPS is required for stimulation of TLR4.
Takeaway
Vibrio cholerae has a special part in its structure that helps it resist certain medicines and triggers the body's immune response.
Methodology
Mass spectrometry was used to analyze lipid A species from various V. cholerae strains, and complementation studies were performed to assess the role of Vc0212.
Limitations
The study primarily focuses on specific serogroups and may not represent all V. cholerae strains.
Statistical Information
P-Value
p ≤ 0.006
Statistical Significance
p ≤ 0.006
Digital Object Identifier (DOI)
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