The Als3-mediated attachment of enolase on the surface of Candida albicans cells regulates their interactions with host proteins

Justyna Karkowska-Kuleta, Ewelina Wronowska, Dorota Satala, Marcin Zawrotniak, Grazyna Bras, Andrzej Kozik, Angela H Nobbs, Maria Rapala-Kozik*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

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The multifunctional protein enolase has repeatedly been identified at the surface of numerous cell types, including a variety of pathogenic microorganisms. In Candida albicans-one of the most common fungal pathogens in humans-a surface-exposed enolase form has been previously demonstrated to play an important role in candidal pathogenicity. In our current study, the presence of enolase at the fungal cell surface under different growth conditions was summarized and a higher abundance of enolase at the surface of C. albicans hyphal forms compared to yeast-like cells was found. Affinity chromatography and chemical cross-linking indicated a member of the agglutinin-like sequence protein family-Als3-as an important potential partner required for the surface display of enolase. Analysis of Saccharomyces cerevisiae cells overexpressing Als3 with site-specific deletions showed that the Ig-like N-terminal region of Als3 (aa 166-225; aa 218-285; aa 270-305; aa 277-286) and central repeat domain (aa 434-830) are essential for the interaction of this adhesin with enolase. In addition, binding between enolase and Als3 influenced subsequent docking of host plasma proteins-high molecular mass kininogen and plasminogen-on the candidal cell surface, thus supporting the hypothesis that C. albicans can modulate plasma proteolytic cascades to affect homeostasis within the host and propagate inflammation during infection. This article is protected by copyright. All rights reserved.

Original languageEnglish
Pages (from-to)e13297
Number of pages20
JournalCellular Microbiology
Early online date25 Nov 2020
Publication statusE-pub ahead of print - 25 Nov 2020


  • enolase
  • agglutinin‐like sequence protein Als3
  • moonlighting proteins
  • Candida albicans
  • plasminogen
  • kininogen


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