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. Author manuscript; available in PMC: 2020 Jun 12.
Published in final edited form as: Nano Lett. 2019 Apr 30;19(6):3846–3853. doi: 10.1021/acs.nanolett.9b01010

Figure 5.

Figure 5

Mechanism of amyloid-like homophilic adhesion in Candida albicans. (Left) Force-induced unfolding of Als5 proteins leads to the exposure of hidden amyloid sequences, which trigger the lateral assembly (cis interactions) of the proteins on the cell surface. Strong homophilic adhesion (trans interactions) between adhesins on opposing cells is mediated by amyloid-like bonds. Green, orange, and blue colors represent the folded TR, T, and Ig regions. Shown in red is the amyloid sequence of the force-induced unfolded T region. Altering the amyloid sequence (upper right) or lowering the protein density (lower right) abrogates strong homophilic adhesion between adhesins, emphasizing the key role of cis and trans amyloid bonding in fungal aggregation.