Conserved leucine-rich repeat proteins in the adhesive projectile slime of velvet worms

Z Zhaolong Hu (Centre for Sustainable Materials, School of Materials Science and Engineering, Nanyang Technological University) A Alexander Baer (Department of Chemistry, McGill University) L Lars Hering (Department of Zoology, Institute of Biology, University of Kassel) I Ivo de Sena Oliveira (Department of Zoology, Institute of Biology, University of Kassel) A Alexandre Poulhazan (Department of Chemistry, McGill University) D Darren C. Browne (Department of Biological and Chemical Sciences, University of the West Indies) X Xue Guo Q Quentin Moana Perrin (Centre for Sustainable Materials, School of Materials Science and Engineering, Nanyang Technological University) R Radoslaw M. Sobota (Functional Proteomics Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research) S Shawn Hoon (Molecular Engineering Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research) G Georg Mayer (Department of Zoology, Institute of Biology, University of Kassel) S Srinivasaraghavan Kannan (Bioinformatics Institute, Agency for Science, Technology, and Research) C Chandra S. Verma (Bioinformatics Institute, Agency for Science, Technology, and Research) M Matthew J. Harrington (Department of Chemistry, McGill University) A Ali Miserez (Center for Sustainable Materials (SusMat), School of Materials Science and Engineering)

Abstract

The slime of velvet worms (Onychophora) is a protein-based bioadhesive that undergoes rapid, yet reversible transition from a fluid into stiff fibers used for prey capture and defense, but the mechanism by which this phase transition functions is largely unknown. Here, integrating transcriptomic and proteomic approaches with AI-guided structure predictions, we discover a group of evolutionarily conserved leucine-rich repeat (LRR) proteins in velvet worm slime that readily adopt a receptor-like, protein-binding “horseshoe” structure. Our structural predictions suggest dimerization of LRR proteins and support their interactions with conserved β-sheet-rich domains of high-molecular-weight proteins, the primary building blocks of velvet worm slime fibers. This suggests that LRR proteins might be involved in reversible, receptor-based supramolecular interactions in these biofibers, providing potential avenues for fabricating fully recyclable (bio)polymeric materials.

Article Details

Volume / Issue Vol. 122, Issue 12
Published March 25, 2025
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (15)

Z

Zhaolong Hu

Centre for Sustainable Materials, School of Materials Science and Engineering, Nanyang Technological University

A

Alexander Baer

Department of Chemistry, McGill University

L

Lars Hering

Department of Zoology, Institute of Biology, University of Kassel

I

Ivo de Sena Oliveira

Department of Zoology, Institute of Biology, University of Kassel

A

Alexandre Poulhazan

Department of Chemistry, McGill University

D

Darren C. Browne

Department of Biological and Chemical Sciences, University of the West Indies

X

Xue Guo

Q

Quentin Moana Perrin

Centre for Sustainable Materials, School of Materials Science and Engineering, Nanyang Technological University

R

Radoslaw M. Sobota

Functional Proteomics Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research

S

Shawn Hoon

Molecular Engineering Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology, and Research

G

Georg Mayer

Department of Zoology, Institute of Biology, University of Kassel

S

Srinivasaraghavan Kannan

Bioinformatics Institute, Agency for Science, Technology, and Research

C

Chandra S. Verma

Bioinformatics Institute, Agency for Science, Technology, and Research

M

Matthew J. Harrington

Department of Chemistry, McGill University

A

Ali Miserez

Center for Sustainable Materials (SusMat), School of Materials Science and Engineering