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LL-37

Cathelicidin, hCAP-18, FALL-39, CAP-18

Quick Stats
Studies 2230
Trials 95
Score 1
2014 pubmed

Bordetella pertussis lipid A glucosamine modification confers resistance to cationic antimicrobial peptides and increases resistance to outer membrane perturbation.

Shah. Nita R NR; Hancock. Robert E W RE; Fernandez. Rachel C RC

Key Findings

  • Bordetella pertussis modifies its lipid A with glucosamine.
  • The glucosamine modification makes the bacteria more resistant to LL‑37 and other cationic antimicrobial peptides.
  • This modification also protects the bacterial outer membrane from disruption.

Practical Outcomes

  • For biohackers, the finding mainly highlights a bacterial resistance mechanism rather than offering a new way to use LL‑37 for health. It suggests that LL‑37’s antimicrobial power can be limited against certain pathogens, but it doesn’t change dosing or application strategies for human use.

Summary

The study shows that the whooping cough bug can add a sugar (glucosamine) to a part of its outer coating, which makes it harder for natural antimicrobial proteins like LL‑37 to kill it. This tweak also helps the bacteria keep its outer membrane stable.

Abstract

Bordetella pertussis, the causative agent of whooping cough, has many strategies for evading the human immune system. Lipopolysaccharide (LPS) is an important Gram-negative bacterial surface structure that activates the immune system via Toll-like receptor 4 and enables susceptibility to cationic antimicrobial peptides (CAMPs). We show modification of the lipid A region of LPS with glucosamine increased resistance to numerous CAMPs, including LL-37. Furthermore, we demonstrate that this glucosamine modification increased resistance to outer membrane perturbation.

Study Information

Provider

pubmed

Year

2014

Date

2014-05-27T00:00:00.000Z

DOI

10.1128/aac.02590-14