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  Plumieribetin, a fish lectin homologous to mannose-binding B-type lectins, inhibits the collagen-binding α1β1 integrin

de Santana Evangelista, K., Andrich, F., Figueiredo de Rezende, F., Niland, S., Cordeiro, M. N., Horlacher, T., et al. (2009). Plumieribetin, a fish lectin homologous to mannose-binding B-type lectins, inhibits the collagen-binding α1β1 integrin. Journal of Biological Chemistry, 284(50), 34747-34759. doi:10.1074/jbc.M109.002873.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-DD86-A Version Permalink: http://hdl.handle.net/21.11116/0000-0006-DD87-9
Genre: Journal Article

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 Creators:
de Santana Evangelista, Karla, Author
Andrich, Filipe, Author
Figueiredo de Rezende, Flávia, Author
Niland, Stephan, Author
Cordeiro, Marta N., Author
Horlacher, Tim, Author
Castelli, Riccardo, Author
Schmidt-Hederich, Alletta, Author
Seeberger, Peter H.1, Author              
Sanchez, Eladio F., Author
Richardson, Michael, Author
Gomes de Figueiredo, Suely, Author
Eble, Johannes A., Author
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1External Organizations, ou_persistent22              

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 Abstract: Recently, a few fish proteins have been described with a high homology to B-type lectins of monocotyledonous plants. Because of their mannose binding activity, they have been ascribed a role in innate immunity. By screening various fish venoms for their integrin inhibitory activity, we isolated a homologous protein from the fin stings and skin mucus of the scorpionfish (Scorpaena plumieri). This protein inhibits α1β1 integrin binding to basement membrane collagen IV. By protein chemical and spectroscopic means, we demonstrated that this fish protein, called plumieribetin, is a homotetramer and contains a high content of anti-parallel β strands, similar to the mannose-binding monocot B-lectins. It lacks both N-linked glycoconjugates and common O-glycan motifs. Despite its B-lectin-like structure, plumieribetin binds to α1β1 integrin irrespective of N-glycosylation, suggesting a direct protein-protein interaction. This interaction is independent of divalent cations. On the cellular level, plumieribetin failed to completely detach hepatocarcinoma HepG2 cells and primary arterial smooth muscle cells from the collagen IV fragment CB3. However, plumieribetin weakened the cell-collagen contacts, reduced cell spreading, and altered the actin cytoskeleton, after the compensating α2β1 integrin was blocked. The integrin inhibiting effect of plumieribetin adds a new function to the B-lectin family, which is known for pathogen defense.

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 Dates: 2009
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: DOI: 10.1074/jbc.M109.002873
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Title: Journal of Biological Chemistry
  Other : J. Biol. Chem.
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 284 (50) Sequence Number: - Start / End Page: 34747 - 34759 Identifier: ISSN: 0021-9258