Limits...
Molecular Diversity and Gene Evolution of the Venom Arsenal of Terebridae Predatory Marine Snails.

Gorson J, Ramrattan G, Verdes A, Wright EM, Kantor Y, Rajaram Srinivasan R, Musunuri R, Packer D, Albano G, Qiu WG, Holford M - Genome Biol Evol (2015)

Bottom Line: Phylogenetic methodology was used to identify 14 teretoxin gene superfamilies for the first time, 13 of which are unique to the Terebridae.Additionally, basic local algorithm search tool homology-based searches to venom-related genes and posttranslational modification enzymes identified a convergence of certain venom proteins, such as actinoporin, commonly found in venoms.This research provides novel insights into venom evolution and recruitment in Conoidean predatory marine snails and identifies a plethora of terebrid venom peptides that can be used to investigate fundamental questions pertaining to gene evolution.

View Article: PubMed Central - PubMed

Affiliation: Hunter College and The Graduate Center, City University of New York Invertebrate Zoology, Sackler Institute for Comparative Genomics, American Museum of Natural History, New York.

Show MeSH
Posttranslational modification enzymes found in Terebrid venom-duct transcriptomes. (A) Posttranslational modification enzymes found in Tr. anilis and Te. subulata transcriptomes, with respective amino acid length and accession number. (B) Representative BLAST alignment to tyrosyl sulfotransferase from Littorina sitkana, which is responsible for sulfation of tyrosine in conotoxins.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4494067&req=5

evv104-F7: Posttranslational modification enzymes found in Terebrid venom-duct transcriptomes. (A) Posttranslational modification enzymes found in Tr. anilis and Te. subulata transcriptomes, with respective amino acid length and accession number. (B) Representative BLAST alignment to tyrosyl sulfotransferase from Littorina sitkana, which is responsible for sulfation of tyrosine in conotoxins.

Mentions: Posttranslational modifications are prominent in conotoxins (Craig et al. 1999; Buczek et al. 2005; Wang et al. 2007; Safavi-Hemami et al. 2010); however preliminary research, based on limited molecular and proteomic data, suggested that teretoxins were not posttranslationally modified (Imperial et al. 2003; Imperial et al. 2007). In the interest of gaining an overview of posttranslational enzymes present in the terebrid venom arsenal, GO analyses were performed on Tr. anilis and Te. subulata assembled transcriptomes. Annotation of Tr. anilis and Te. subulata transcriptomes for the presence of posttranslational enzymes yielded a number of candidate proteins similar to those found in conotoxins (fig. 7 and supplementary fig. S1, Supplementary Material online). These proteins are described below.Fig. 7.—


Molecular Diversity and Gene Evolution of the Venom Arsenal of Terebridae Predatory Marine Snails.

Gorson J, Ramrattan G, Verdes A, Wright EM, Kantor Y, Rajaram Srinivasan R, Musunuri R, Packer D, Albano G, Qiu WG, Holford M - Genome Biol Evol (2015)

Posttranslational modification enzymes found in Terebrid venom-duct transcriptomes. (A) Posttranslational modification enzymes found in Tr. anilis and Te. subulata transcriptomes, with respective amino acid length and accession number. (B) Representative BLAST alignment to tyrosyl sulfotransferase from Littorina sitkana, which is responsible for sulfation of tyrosine in conotoxins.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4494067&req=5

evv104-F7: Posttranslational modification enzymes found in Terebrid venom-duct transcriptomes. (A) Posttranslational modification enzymes found in Tr. anilis and Te. subulata transcriptomes, with respective amino acid length and accession number. (B) Representative BLAST alignment to tyrosyl sulfotransferase from Littorina sitkana, which is responsible for sulfation of tyrosine in conotoxins.
Mentions: Posttranslational modifications are prominent in conotoxins (Craig et al. 1999; Buczek et al. 2005; Wang et al. 2007; Safavi-Hemami et al. 2010); however preliminary research, based on limited molecular and proteomic data, suggested that teretoxins were not posttranslationally modified (Imperial et al. 2003; Imperial et al. 2007). In the interest of gaining an overview of posttranslational enzymes present in the terebrid venom arsenal, GO analyses were performed on Tr. anilis and Te. subulata assembled transcriptomes. Annotation of Tr. anilis and Te. subulata transcriptomes for the presence of posttranslational enzymes yielded a number of candidate proteins similar to those found in conotoxins (fig. 7 and supplementary fig. S1, Supplementary Material online). These proteins are described below.Fig. 7.—

Bottom Line: Phylogenetic methodology was used to identify 14 teretoxin gene superfamilies for the first time, 13 of which are unique to the Terebridae.Additionally, basic local algorithm search tool homology-based searches to venom-related genes and posttranslational modification enzymes identified a convergence of certain venom proteins, such as actinoporin, commonly found in venoms.This research provides novel insights into venom evolution and recruitment in Conoidean predatory marine snails and identifies a plethora of terebrid venom peptides that can be used to investigate fundamental questions pertaining to gene evolution.

View Article: PubMed Central - PubMed

Affiliation: Hunter College and The Graduate Center, City University of New York Invertebrate Zoology, Sackler Institute for Comparative Genomics, American Museum of Natural History, New York.

Show MeSH