Unusual traits shape the architecture of the Ig ancestor molecule DOI Creative Commons
Alejandro Urdiciain,

Thomas Madej,

Jiyao Wang

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: July 23, 2024

Abstract Understanding the ancestral Ig domain’s molecular structure and tracing evolution of Ig-like proteins are fundamental components missing from our comprehension their evolutionary trajectory function. We have elucidated structures two most phylum, Porifera , revealing previously unidentified Ig-domain features that highlight concomitant presence a novel “Early Variable” (EV)-set in tandem with C1-set domain. The latter, to knowledge, has never been reported before non-vertebrates. IgV IgC1 sets combination into functional receptors part adaptive immune system higher vertebrates, which allows for highly specific responses. These observations ancient phylum could indicate primitive forms immunity or foundational strategy conserved through evolution. By unveiling important clues configuration domains, these findings challenge expand understanding how evolved within its current landscape.

Language: Английский

Unusual traits shape the architecture of the Ig ancestor molecule DOI Creative Commons
Alejandro Urdiciain,

Thomas Madej,

Jiyao Wang

et al.

Communications Biology, Journal Year: 2025, Volume and Issue: 8(1)

Published: March 20, 2025

Understanding the ancestral Ig domain's molecular structure and tracing evolution of Ig-like proteins are fundamental components missing from our comprehension their evolutionary trajectory function. We have determined high-resolution structures two most phylum, Porifera. The reveal N-terminal domains with an unconventional configuration features that set them apart canonical domains. These findings prompted us to call this novel domain as "Early Variable" (EV)-set. Remarkably, EV-sets linked C1-set To best knowledge, has not been previously reported in non-vertebrates. IgV IgC1 tandems combination into functional receptors part adaptive immune system higher vertebrates, which allows for highly specific responses. By unveiling important clues domains, these challenge expand understanding how immunity evolved within its current landscape. A immunoglobulin identified non-vertebrate species is presented. An early variable tandem a C-terminal provides new insights origins proteins.

Language: Английский

Citations

0
Unusual traits shape the architecture of the Ig ancestor molecule DOI Creative Commons
Alejandro Urdiciain,

Thomas Madej,

Jiyao Wang

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: July 23, 2024

Abstract Understanding the ancestral Ig domain’s molecular structure and tracing evolution of Ig-like proteins are fundamental components missing from our comprehension their evolutionary trajectory function. We have elucidated structures two most phylum, Porifera , revealing previously unidentified Ig-domain features that highlight concomitant presence a novel “Early Variable” (EV)-set in tandem with C1-set domain. The latter, to knowledge, has never been reported before non-vertebrates. IgV IgC1 sets combination into functional receptors part adaptive immune system higher vertebrates, which allows for highly specific responses. These observations ancient phylum could indicate primitive forms immunity or foundational strategy conserved through evolution. By unveiling important clues configuration domains, these findings challenge expand understanding how evolved within its current landscape.

Language: Английский

Citations

2