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Aleksandrov, A.

Publications and source records attributed to Aleksandrov, A..

2 recordsLinked to original sources

Atonosomes, compartments involved in membrane tension decrease

To ensure survival, cells need to buffer the effects of environmental stress on their plasma membrane, yet the structural mechanisms by which this is acutely achieved remain largely unknown. Here, we propose atonosomes as a unifying identity for a class of previously observed but enigmatic, tension-responsive, plasma membrane-derived compartments that arise across contexts of acute and chronic membrane tension loss. Leveraging unprecedented high resolution cryo-FIB-ET imaging in yeast, we show that atonosomes are complex, organelle-containing structures bounded by membranes and cell wall material, spanning hundreds of nanometers, and displaying a remarkable morphological diversity. Atonosomes form within seconds in response to reduced plasma membrane tension, and their emergence appears to require no dedicated molecular machinery, arising instead as a direct consequence of membrane biophysics. Upon formation, they recruit key membrane-associated proteins, including TORC2, Slm1, and septins. Under conditions of chronic disruption of PM homeostasis, atonosomes become constitutively present. Their stability and reversibility are further modulated by the cell wall, whose polymerization state influences atonosome dynamics. Structural conservation in fungi and ichthyosporea, demonstrates that atonosomes are a conserved stress-triggered response of cell-wall enclosed organisms. Together, these findings establish atonosomes as a novel compartment that mediates cellular responses to plasma membrane tension variation, coupling membrane remodeling and lipid homeostasis to preserve cellular integrity under stress.

cell biology↗

Peptide fibrils as vaccine: a proof of concept

The potential of amyloid-like fibrils formed by peptides as vaccine candidates was investigated using a fragment of the Ebola virus glycoprotein. Peptide in fibrillar form were found to induce an immune response to the full-length protein without causing cellular toxicity or significant changes in hematological studies. The ability of the studied peptide fragment to oligomerize and form amyloid-like fibrils and intermediates suggests potential implications for the viruss mechanisms of action on cells, particularly those of the immune system. Additionally, if native GP2 epitopes are retained in the peptide fibrils, they may serve as effective immunization agents due to their autoadjuvant properties; however, it is important to consider the possibility of cross-reactivity with human proteins. These findings provide valuable insights into the potential use of amyloid-forming peptide as vaccine candidates and highlight the need for further research into their immunogenic and adjuvant properties.

biophysics↗