Publication
Antimicrobial peptide resistance in Neisseria meningitidis
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- Persistent URL
- Last modified
- 02/20/2025
- Type of Material
- Authors
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Yih-Ling Tzeng, Emory UniversityDavid Stephens, Emory University
- Language
- English
- Date
- 2015-11-01
- Publisher
- Elsevier
- Publication Version
- Copyright Statement
- © 2015 Elsevier B.V.
- License
- Final Published Version (URL)
- Title of Journal or Parent Work
- Volume
- 1848
- Issue
- 11
- Start Page
- 3026
- End Page
- 3031
- Grant/Funding Information
- This work was supported in part by NIH Grant 5R01 AI40247 awarded to DSS and by NIH Grant R56AI 061031 awarded to YT.
- Abstract
- Antimicrobial peptides (AMPs) play an important role as a host defense against microbial pathogens and are key components of the human innate immune response. Neisseria meningitidis frequently colonizes the human nasopharynx as a commensal but also is a worldwide cause of epidemic meningitis and rapidly fatal sepsis. In the human respiratory tract, the only known reservoir of N. meningitidis, meningococci are exposed to human endogenous AMPs. Thus, it is not surprising that meningococci have evolved effective mechanisms to confer intrinsic and high levels of resistance to the action of AMPs. This article reviews the current knowledge about AMP resistance mechanisms employed by N. meningitidis. Two major resistance mechanisms employed by meningococci are the constitutive modification of the lipid A head groups of lipooligosaccharides by phosphoethanolamine and the active efflux pump mediated excretion of AMPs. Other factors influencing AMP resistance, such as the major porin PorB, the pilin biogenesis apparatus, and capsular polysaccharides, have also been identified. Even with an inherently high intrinsic resistance, several AMP resistance determinants can be further induced upon exposure to AMPs. Many well-characterized AMP resistance mechanisms in other Gram-negative bacteria are not found in meningococci. Thus, N. meningitidis utilizes a limited but highly effective set of molecular mechanisms to mediate antimicrobial peptide resistance. This article is part of a Special Issue entitled: Bacterial Resistance to Antimicrobial Peptides.
- Author Notes
- Keywords
- GRAM-NEGATIVE BACTERIA
- Biochemistry & Molecular Biology
- MEMBRANE FRAGMENTATION
- Life Sciences & Biomedicine
- Science & Technology
- LIPOPOLYSACCHARIDE MICELLES
- HUMAN BETA-DEFENSIN-3
- Antimicrobial resistance
- BIOFILM FORMATION
- Efflux pump
- BINDING-PROTEIN-B
- POLYMYXIN-B RESISTANCE
- Biophysics
- Phosphoethanolamine modification of lipid A
- 2-COMPONENT REGULATORY SYSTEM
- Neisseria meningitidis
- Research Categories
- Biology, Microbiology
- Health Sciences, General
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Publication File - rtj16.pdf | Primary Content | 2025-02-17 | Public | Download |