Antimicrobial properties of allicin from garlic

Microbes Infect. 1999 Feb;1(2):125-9. doi: 10.1016/s1286-4579(99)80003-3.

Abstract

Allicin, one of the active principles of freshly crushed garlic homogenates, has a variety of antimicrobial activities. Allicin in its pure form was found to exhibit i) antibacterial activity against a wide range of Gram-negative and Gram-positive bacteria, including multidrug-resistant enterotoxicogenic strains of Escherichia coli; ii) antifungal activity, particularly against Candida albicans; iii) antiparasitic activity, including some major human intestinal protozoan parasites such as Entamoeba histolytica and Giardia lamblia; and iv) antiviral activity. The main antimicrobial effect of allicin is due to its chemical reaction with thiol groups of various enzymes, e.g. alcohol dehydrogenase, thioredoxin reductase, and RNA polymerase, which can affect essential metabolism of cysteine proteinase activity involved in the virulence of E. histolytica.

Publication types

  • Review

MeSH terms

  • Alcohol Dehydrogenase / antagonists & inhibitors
  • Animals
  • Anti-Bacterial Agents
  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / metabolism
  • Anti-Infective Agents / pharmacology*
  • Antifungal Agents / pharmacology
  • Antiparasitic Agents / pharmacology
  • Antiviral Agents / pharmacology
  • Candida albicans / drug effects
  • DNA-Directed RNA Polymerases / antagonists & inhibitors
  • Drug Resistance, Microbial
  • Entamoeba histolytica / drug effects
  • Escherichia coli / drug effects
  • Garlic / chemistry*
  • Giardia lamblia / drug effects
  • Plants, Medicinal*
  • Sulfinic Acids / chemistry
  • Sulfinic Acids / metabolism
  • Sulfinic Acids / pharmacology*
  • Thioredoxin-Disulfide Reductase / antagonists & inhibitors

Substances

  • Anti-Bacterial Agents
  • Anti-Infective Agents
  • Antifungal Agents
  • Antiparasitic Agents
  • Antiviral Agents
  • Sulfinic Acids
  • allicin
  • Alcohol Dehydrogenase
  • Thioredoxin-Disulfide Reductase
  • DNA-Directed RNA Polymerases