LAUSR.org creates dashboard-style pages of related content for over 1.5 million academic articles. Sign Up to like articles & get recommendations!

A novel broad spectrum venom metalloproteinase autoinhibitor in the rattlesnake Crotalus atrox evolved via a shift in paralog function

Photo from wikipedia

Significance This study investigates how rattlesnakes protect themselves from their own evolving venom. Venom toxins can be dangerous if they enter the snake’s tissues or circulatory system during feeding or… Click to show full abstract

Significance This study investigates how rattlesnakes protect themselves from their own evolving venom. Venom toxins can be dangerous if they enter the snake’s tissues or circulatory system during feeding or digestion, and many venomous species have evolved autoresistance to their own toxins. Here, we identify a broad-spectrum serum inhibitor of rattlesnake metalloproteinases, a group of toxins that causes tissue destruction and hemorrhage. We show that this inhibitor is a different member of a protein family known to inhibit metalloproteinases in Asian and South American relatives of rattlesnakes. We suggest that changes in the number and diversity of rattlesnake metalloproteinases selected for the emergence of this broad-spectrum inhibitor, which may be potentially useful in snakebite treatment.

Keywords: novel broad; venom; spectrum venom; venom metalloproteinase; broad spectrum

Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Year Published: 2022

Link to full text (if available)


Share on Social Media:                               Sign Up to like & get
recommendations!

Related content

More Information              News              Social Media              Video              Recommended



                Click one of the above tabs to view related content.