A multi-domain snail metallothionein increases cadmium resistance and fitness in Caenorhabditis elegans
Metallothioneins (MTs) are a family of mostly low-molecular weight, cysteine-rich proteins capable of specific metal-ion binding that are involved in metal detoxification and homeostasis, as well as in stress response. In contrast to most other animal species which possess two-domain (bidominial) MT...
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Published in: | Scientific reports Vol. 14; no. 1; pp. 25589 - 14 |
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Main Authors: | , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
London
Nature Publishing Group UK
26-10-2024
Nature Publishing Group Nature Portfolio |
Subjects: | |
Online Access: | Get full text |
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Summary: | Metallothioneins (MTs) are a family of mostly low-molecular weight, cysteine-rich proteins capable of specific metal-ion binding that are involved in metal detoxification and homeostasis, as well as in stress response. In contrast to most other animal species which possess two-domain (bidominial) MTs, some gastropod species have evolved Cd
2+
-selective multidomain MTs (md-MTs) consisting of several concatenated β3 domains and a single C-terminal β1 domain. Each domain contains three-metal ion clusters and binds three metal ions. The terrestrial snail
Alinda biplicata
possesses, among other MT isoforms, an md-MT with nine β3 domains and a C-terminal β1 domain (termed 10md-MT), capable of binding up to 30 Cd
2+
ions per protein molecule. In the present study, the
Alinda biplicata 10md-MT
gene and a truncated version consisting of one β3 domain and a single C-terminal β1 domain (
2d-MT
) were introduced into a
Caenorhabditis elegans
knock-out strain lacking a native MT gene (
mtl-1
). The two snail MT constructs consistently increased Cd
2+
resistance, and partially improved morphological, life history and physiological fitness traits in the nematode model host
Caenorhabditis elegans
. This highlights how the engineering of transgenic
Caenorhabditis elegans
strains expressing snail MTs provides an enhancement of the innate metal detoxification mechanism and in doing so provides a platform for enhanced mechanistic toxicology. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 2045-2322 2045-2322 |
DOI: | 10.1038/s41598-024-76268-2 |