Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Internalization of tenecin 3 by a fungal cellular process is essential for its fungicidal effect on candida albicans

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Kim, Dae Hee
  • Lee, D. G.
  • Kim, K. L.
  • Lee, Y.

publication date

  • August 2001

journal

  • European Journal of Biochemistry  Journal

abstract

  • Tenecin 3 is a glycine-rich, antifungal protein of 78 residues isolated from the insect Tenebrio molitor larva. As an initial step towards understanding the antifungal mechanism of tenecin 3, we examined how this protein interacts with the pathogenic fungus Candida albicans to exert its antifungal action. Tenecin 3 did not induce the release of a fluorescent dye trapped in the artificial membrane vesicles and it did not perturb the membrane potential of C. albicans by the initial interaction. Fluorescence confocal microscopy and flow cytometric analysis revealed that tenecin 3 is rapidly internalized into the cytoplasmic space in energy-dependent and temperature-dependent manners. This internalization is also dependent on the ionic environment and cellular metabolic states. These results suggest that the internalization of tenecin 3 into the cytoplasm of C. albicans is mediated by a fungal cellular process. The internalized tenecin 3 is dispersed in the cytoplasm, and the loss of cell viability occurs after this internalization.

subject areas

  • Amino Acid Sequence
  • Antifungal Agents
  • Candida albicans
  • Insect Proteins
  • Membrane Potentials
  • Molecular Sequence Data
  • Recombinant Proteins
scroll to property group menus

Research

keywords

  • antifungal protein
  • fungus
  • insect
  • internalization
  • tenecin 3
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0014-2956

Digital Object Identifier (DOI)

  • 10.1046/j.1432-1327.2001.02364.x

PubMed ID

  • 11502205
scroll to property group menus

Additional Document Info

start page

  • 4449

end page

  • 4458

volume

  • 268

issue

  • 16

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support