Brooke L. Whitelaw, Ira R. Cooke, Julian Finn, Kyall Zenger, J.M. Strugnell

Blue ringed octopus make use of a deadly neurotoxin, TTX (tetrodotoxin) which is also found a wide variety of other animals. In order to do this they must be able to tolerate the toxin themselves, as well as acquire it from the environment or produce it. This paper reviews what we know about the evolution of ttx acquisition in blue ringed octopuses.

Featured image is by Flickr user Rickard Ling (CC 2.0)

Nikeisha J. Caruana , Jan M. Strugnell, Pierre Faou, Julian Finn, and Ira R. Cooke

Nikeisha compared the slime from two bobtail squids and found that their proteomic composition was very similar. She also found several highly abundant, short secreted proteins in the slime, for which a function is unknown.

Published in the Journal of Proteome Research

Featured image is of Sepioloidea lineolata. Photograph by Richard Ling <wikipedia@rling.com> [CC BY-SA 3.0], via Wikimedia Commons

Legana C. H. W. Fingerhut, Jan M. Strugnell, Pierre Faou, Álvaro Roura Labiaga, Jia Zhang, and Ira R. Cooke

A wide variety of octopus and cuttlefish species use venom to disable and kill their prey.   Although this has been known for over a hundred years the molecules responsible for this toxicity remain relatively unknown.  In this paper we found that a particular family of proteins (serine proteases) are extremely diverse and abundant in the venom glands of octopus.  Although serine proteases are common in all animals (and not always toxins) we found that they are extraordinarily diverse in octopus and cuttlefish, and that this diversity is almost entirely due to molecules that are found in the venom glands.

Most of the work for this paper was done by Legana as part of her honours year. Well done Legana on your first paper.

Featured image is of Felicinda the octopus who was the mother of octopuses featured in this study. Photograph by Álvaro Roura

 Published in the Journal of Proteome Research