Molecular-level architecture of Chlamydomonas reinhardtii’s glycoprotein-rich cell wall

Alexandre Poulhazan, Alexandre A. Arnold, Frederic Mentink-Vigier, Artur Muszyński, Parastoo Azadi, Adnan Halim, Sergey Y. Vakhrushev, Hiren Jitendra Joshi, Tuo Wang (), Dror E. Warschawski () and Isabelle Marcotte ()
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Alexandre Poulhazan: Université du Québec à Montréal
Alexandre A. Arnold: Université du Québec à Montréal
Frederic Mentink-Vigier: Florida State University
Artur Muszyński: University of Georgia
Parastoo Azadi: University of Georgia
Adnan Halim: University of Copenhagen
Sergey Y. Vakhrushev: University of Copenhagen
Hiren Jitendra Joshi: University of Copenhagen
Tuo Wang: Michigan State University
Dror E. Warschawski: Sorbonne Université, École Normale Supérieure, PSL University
Isabelle Marcotte: Université du Québec à Montréal

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: Abstract Microalgae are a renewable and promising biomass for large-scale biofuel, food and nutrient production. However, their efficient exploitation depends on our knowledge of the cell wall composition and organization as it can limit access to high-value molecules. Here we provide an atomic-level model of the non-crystalline and water-insoluble glycoprotein-rich cell wall of Chlamydomonas reinhardtii. Using in situ solid-state and sensitivity-enhanced nuclear magnetic resonance, we reveal unprecedented details on the protein and carbohydrate composition and their nanoscale heterogeneity, as well as the presence of spatially segregated protein- and glycan-rich regions with different dynamics and hydration levels. We show that mannose-rich lower-molecular-weight proteins likely contribute to the cell wall cohesion by binding to high-molecular weight protein components, and that water provides plasticity to the cell-wall architecture. The structural insight exemplifies strategies used by nature to form cell walls devoid of cellulose or other glycan polymers.

Date: 2024
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-45246-7

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DOI: 10.1038/s41467-024-45246-7

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