TY - JOUR

T1 - Structural characterization and visualization of oligomeric states of the Rhagium mordax antifreeze protein

AU - Oleinik, Galina A.

AU - Kanarskaya, Maria A.

AU - Majorina, Maria A.

AU - Lomzov, Alexander A.

AU - Melnik, Bogdan S.

AU - Koval, Vladimir V.

AU - Baranova, Svetlana V.

N1 - Oleinik, G.A., Kanarskaya, M.A., Majorina, M.A. et al. Structural characterization and visualization of oligomeric states of the Rhagium mordax antifreeze protein. Sci Rep 16, 33995 (2026). https://doi.org/10.1038/s41598-026-64071-0 This work was supported by the Russian state-funded project for ICBFM SB RAS (FWGN-2025-0020). The genetic engineering part of the work was carried out with the support of Russian Science Foundation (25-14-00260).

PY - 2026/7/26

Y1 - 2026/7/26

N2 - Some organisms produce antifreeze proteins (AFPs) that help them survive freezing by binding to ice crystals. The molecular basis of this process is not yet fully elucidated. We suggest that the activity of these natural proteins is equivalent to the area of the ice-binding surface. The study focuses on a protein from R. mordax (RmAFP). It has one threonine motif required for ice binding. Our findings propose that oligomerization of RmAFP increases the abundance of this motif and we show present of oligomeric structures in solution by mass spectrometry. We proposed potential structures for oligomers, which have a flat surface area necessary for ice binding. We have also demonstrated the presence of oligomeric forms of protein using atomic force microscopy. In addition, a model of oligomer RmAFP binding to ice surfaces has been offered. The findings of this study suggest that a molecule comprising multiple RmAFP domains in an oligomeric complex may possess augmented ice-binding capacity, which could potentially enhance the survival of the beetle Rhagium mordax in harsh winter conditions.

AB - Some organisms produce antifreeze proteins (AFPs) that help them survive freezing by binding to ice crystals. The molecular basis of this process is not yet fully elucidated. We suggest that the activity of these natural proteins is equivalent to the area of the ice-binding surface. The study focuses on a protein from R. mordax (RmAFP). It has one threonine motif required for ice binding. Our findings propose that oligomerization of RmAFP increases the abundance of this motif and we show present of oligomeric structures in solution by mass spectrometry. We proposed potential structures for oligomers, which have a flat surface area necessary for ice binding. We have also demonstrated the presence of oligomeric forms of protein using atomic force microscopy. In addition, a model of oligomer RmAFP binding to ice surfaces has been offered. The findings of this study suggest that a molecule comprising multiple RmAFP domains in an oligomeric complex may possess augmented ice-binding capacity, which could potentially enhance the survival of the beetle Rhagium mordax in harsh winter conditions.

KW - Ice-binding proteins (IBPs

KW - Antifreeze protein (AFP)

KW - Oligomeric state

KW - MALDI mass spectrometry

KW - Atomic force microscopy

KW - Molecular dynamics

UR - https://www.mendeley.com/catalogue/c4f64bba-47fa-3324-8f5e-328313041e3d/

UR - https://www.scopus.com/pages/publications/105054603210

U2 - 10.1038/s41598-026-64071-0

DO - 10.1038/s41598-026-64071-0

M3 - Article

VL - 16

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 33995

ER -