Movatterモバイル変換


[0]ホーム

URL:


Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
Thehttps:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

NIH NLM Logo
Log inShow account info
Access keysNCBI HomepageMyNCBI HomepageMain ContentMain Navigation
pubmed logo
Advanced Clipboard
User Guide

Full text links

Atypon full text link Atypon Free PMC article
Full text links

Actions

Share

.2012 Apr 7;279(1732):1351-8.
doi: 10.1098/rspb.2011.1731. Epub 2011 Nov 2.

Neurotoxin localization to ectodermal gland cells uncovers an alternative mechanism of venom delivery in sea anemones

Affiliations

Neurotoxin localization to ectodermal gland cells uncovers an alternative mechanism of venom delivery in sea anemones

Yehu Moran et al. Proc Biol Sci..

Abstract

Jellyfish, hydras, corals and sea anemones (phylum Cnidaria) are known for their venomous stinging cells, nematocytes, used for prey and defence. Here we show, however, that the potent Type I neurotoxin of the sea anemone Nematostella vectensis, Nv1, is confined to ectodermal gland cells rather than nematocytes. We demonstrate massive Nv1 secretion upon encounter with a crustacean prey. Concomitant discharge of nematocysts probably pierces the prey, expediting toxin penetration. Toxin efficiency in sea water is further demonstrated by the rapid paralysis of fish or crustacean larvae upon application of recombinant Nv1 into their medium. Analysis of other anemone species reveals that in Anthopleura elegantissima, Type I neurotoxins also appear in gland cells, whereas in the common species Anemonia viridis, Type I toxins are localized to both nematocytes and ectodermal gland cells. The nematocyte-based and gland cell-based envenomation mechanisms may reflect substantial differences in the ecology and feeding habits of sea anemone species. Overall, the immunolocalization of neurotoxins to gland cells changes the common view in the literature that sea anemone neurotoxins are produced and delivered only by stinging nematocytes, and raises the possibility that this toxin-secretion mechanism is an ancestral evolutionary state of the venom delivery machinery in sea anemones.

PubMed Disclaimer

Figures

Figure 1.
Figure 1.
Nv1 expression in various life stages ofN. vectensis. Nv1 antibody and an Alexa Fluor-conjugated secondary antibody were used to localize Nv1 in whole-mounts of threeN. vectensis developmental stages: 5 day-old planula, 9 day-old primary polyp and an adult. Scale bars: 100, 50 and 200 µm.
Figure 2.
Figure 2.
Nv1 is accumulated in gland cells ofN. vectensis and is released to the water during preying. Nv1 antibody and an Alexa Fluor-conjugated secondary antibody were used to localize Nv1 (appear in red). Nuclei were stained with 4′,6-diamidino-2-phenylindole dihydrochloride (DAPI) (blue). (a) Nv1 is localized to thick gland cells inside the tentacle and to clumped structures at the tentacle surface (indicated by arrowheads). (b) Double immunostaining of Nv1 (red) and chondroitin (green; a proteoglycan involved in nematocyst tubule formation) shows that these molecules are also localized to different cells. Cells with Nv1-positive vesicles are designated by arrowheads. (c) Double immunostaining of Nv1 (red) and Nv-Ncol 3 (green; a minicollagen component of the nematocyst capsule) clearly shows that these peptides are localized to different cells. (d) An Nv1-containing gland cell inN. vectensis tentacle macerate. The vesicular structures suggest toxin accumulation in vesicles. (e,f) Nomarski and fluorescent images localize Nv1 to the surface of interaction betweenN. vectensis tentacles (shown as Nv) andArtemia salina (shown as As) during feeding. Scale bars: (a) 100 µm; (b) 25 µm; (c) 10 µm; (d) 20 µm and (e,f) 50 µm.
Figure 3.
Figure 3.
Anemonia viridis Type I neurotoxins are localized to both gland cells and nematocytes. Nv1 antibody and an Alexa Fluor 568-conjugated secondary antibody were used to localize Nv1 homologues inA. viridis (appear in red). Nuclei were stained with DAPI (blue). (a) In whole-mount tentacles, anti-Nv1 staining is observed in thick gland cells. (b) After treatment with acetic acid, numerous thread-like structures are stained in whole-mount tentacles. (c) Maceration ofA. viridis tentacles reveals the structure of the gland cells (indicated by an arrowhead) and suggests that the neurotoxin is packed in vesicles (a non-merged image is provided as an inset). (d) Maceration reveals that the thread-like stained structures are tubules ofA. viridis nematocysts (shown as Tu). Unlike the tubule, the capsule and the barbed shaft (indicated as Ca and Sh, respectively) are not stained. (e) The Nv1 immunostaining in charged nematocytes indicates that the tubule is coiled, and that the neurotoxin is probably packed on or inside the tubule prior to discharge (a non-merged image is provided as inset). (f) Cryosectioning of the tentacle enables anti-Nv1 immunostaining of a charged nematocyte (indicated by an arrowhead) without maceration. Scale bars: (a,b,d,f) 20 µm; (c) 50 µm and (e) 10 µm.
Figure 4.
Figure 4.
Anthopleura elegantissima Type I neurotoxins are localized to gland cells. (a) Phylogeny ofA. elegantissima,A. viridis andN. vectensis based on previous analysis [32]. (b) Nv1 antibody staining ofA. elegantissima tentacles localizes the toxin to granule-rich gland cells and suggests that the neurotoxin is packed in vesicles (a non-merged image is provided as an inset). Scale bar, 10 µm. (c) Mass spectrometry analysis of extracts fromA. elegantissima tentacle soft tissue reveals mass to charge ratios (m/z) identical (approx. 8 ppm) to those of the APE 2-1 Type I neurotoxin (expectedm/z of 1219.56 Da whenz = 4).
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Ruppert E. E., Barnes R. D. 1994. The cnidarians. In Invertebrate zoology, pp. 103–154, 6th edn. Philadelphia, PA: Saunders College Publishing
    1. Tibballs J. 2006. Australian venomous jellyfish, envenomation syndromes, toxins and therapy. Toxicon 48, 830–85910.1016/j.toxicon.2006.07.020 (doi:10.1016/j.toxicon.2006.07.020) - DOI - DOI - PubMed
    1. Kass-Simon G., Scappaticci A. A., Jr 2002. The behavioral and developmental physiology of nematocysts. Can. J. Zool. 80, 1772–179410.1139/z02-135 (doi:10.1139/z02-135) - DOI - DOI
    1. Özbek S., Balasubramanian P. G., Holstein T. W. 2009. Cnidocyst structure and the biomechanics of discharge. Toxicon 54, 1038–104510.1016/j.toxicon.2009.03.006 (doi:10.1016/j.toxicon.2009.03.006) - DOI - DOI - PubMed
    1. Nüchter T., Benoit M., Engel U., Ozbek S., Holstein T. W. 2006. Nanosecond-scale kinetics of nemtocyst discharge. Curr. Biol. 16, R316–R31810.1016/j.cub.2006.03.089 (doi:10.1016/j.cub.2006.03.089) - DOI - DOI - PubMed

Publication types

MeSH terms

Substances

Related information

Grants and funding

LinkOut - more resources

Full text links
Atypon full text link Atypon Free PMC article
Cite
Send To

NCBI Literature Resources

MeSHPMCBookshelfDisclaimer

The PubMed wordmark and PubMed logo are registered trademarks of the U.S. Department of Health and Human Services (HHS). Unauthorized use of these marks is strictly prohibited.


[8]ページ先頭

©2009-2025 Movatter.jp