دورية أكاديمية

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

التفاصيل البيبلوغرافية
العنوان: Als3‐mediated attachment of enolase on the surface of Candida albicans cells regulates their interactions with host proteins.
المؤلفون: Karkowska‐Kuleta, Justyna, Wronowska, Ewelina, Satala, Dorota, Zawrotniak, Marcin, Bras, Grazyna, Kozik, Andrzej, Nobbs, Angela H., Rapala‐Kozik, Maria
المصدر: Cellular Microbiology; Apr2021, Vol. 23 Issue 4, p1-20, 20p
مصطلحات موضوعية: CANDIDA albicans, ENOLASE, PLASMINOGEN, BLOOD proteins, MOLECULAR weights, CHEMICAL affinity, PROTEIN-protein interactions
مستخلص: The multifunctional protein enolase has repeatedly been identified on 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 examined, 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 the 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. [ABSTRACT FROM AUTHOR]
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قاعدة البيانات: Complementary Index
الوصف
تدمد:14625814
DOI:10.1111/cmi.13297