Purification and characterization of a pore‐forming protein from the marine sponge <i>Tethya lyncurium</i>

Mangel, Andreas; Leitão, José; Batel, Renato; Zimmermann, Herbert; Müller, Wernér E.G.; Schröder, Heinz C.

doi:10.1111/j.1432-1033.1992.tb17448.x

Cited by 34 publications

(19 citation statements)

References 59 publications

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“…Também não foi encontrado na literatura referência de atividade hemolítica devido a lectinas em extratos de esponjas marinhas. No entanto, além da proteína tóxica suberitina, foram descritos como responsáveis pela atividade hemolítica em extratos de esponjas polímeros de alquilpiridinas e outros compostos não identifi cados (Berlinck et al, 1996;Bourget et al, 1988;Cariello;Zanetti, 1979;Mangel et al, 1992;Sepcic et al, 1997).…”

Section: Resultsunclassified

Detecção de atividade lectínica e atividade hemolítica em extratos de esponjas (Porifera) nativas da costa atlântica do Brasil

Dresch¹,

Haeser²,

Lerner³

et al. 2005

Rev. bras. farmacogn.

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RESUMO:Extratos aquosos de vinte espécies de esponjas da costa Atlântica brasileira foram testados para verifi cação da presença de atividade lectínica e atividade hemolítica. Hemaglutinação para eritrócitos humanos e de distintos animais foi evidenciada em 12 dos 20 extratos testados. Os extratos das espécies Axinella corrugata, Chondrilla nucula, Chondrosia collectrix, Cinachyrella alloclada e Guitarra sp1. foram os que apresentaram maior atividade hemaglutinante. Dos doze extratos com atividade hemaglutinante dez tiveram a atividade inibida por um ou mais açúcares e/ou glicoproteínas. A lectina do extrato de Chondrilla nucula foi resistente à desnaturação térmica quando aquecida a 100 o C por 60 minutos. Atividade hemolítica foi encontrada apenas nos extratos de Petromica citrina e Acervochalina sp. As espécies que apresentaram maior potencial para futuros estudos de suas lectinas foram Axinella corrugata, Chondrilla nucula e Chondrosia collectrix, em vista da maior atividade hemaglutinante apresentada por seus extratos, aliada à maior atividade específi ca.Unitermos: Esponjas, lectinas, atividade hemaglutinante, atividade hemolítica.ABSTRACT: "Detection of lectinic activity and hemolytic activity in extracts of native sponges (Porifera) of atlantic coast of Brazil". Aqueous extracts of twenty species of sea sponges of the Brazilian Atlantic coast were tested with the aim of searching the presence of lectinic and hemolytic activity. Hemagglutinating activity for human erythrocytes and for distinct animals were found in 12 of the 20 tested extracts. The extracts of Axinella corrugata, Chondrilla nucula, Chondrosia collectrix, Cinachyrella alloclada and Guitarra sp1. were the ones that presented highest hemagglutinating activity. Ten of the 12 hemagglutinating extracts had the activity inhibited by one or more sugars or glycoproteins. The lectin from Chondrilla nucula was resistant to thermal denaturation when heated up to 100 o C for 60 minutes. Hemolytic activity was only found in the extracts from Petromica citrina and Acervochalina sp. The species of sea sponges that showed major potential for futures studies of their lectins were Axinella corrugata, Chondrilla nucula and Chondrosia collectrix, due to the highest hemagglutinating activity presented by their extracts, allied to the highest specifi c activity.

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Section: Resultsunclassified

Detecção de atividade lectínica e atividade hemolítica em extratos de esponjas (Porifera) nativas da costa atlântica do Brasil

Dresch¹,

Haeser²,

Lerner³

et al. 2005

Rev. bras. farmacogn.

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“…Furthermore, studies with drugs have shown that agonists of TLRs can initiate the release of perforin in human CD8 ϩ cells (24). From earlier studies, it is known that also in sponges, perforin-related molecules exist; from the sponge Tethya lyncurium, a pore-forming protein had been isolated (55), and recently a first cDNA encoding a perforin-like protein was isolated (47).…”

Section: Discussionmentioning

confidence: 99%

Innate Immune Defense of the Sponge Suberites domuncula against Bacteria Involves a MyD88-dependent Signaling Pathway

Wiens

Korzhev

Krasko

et al. 2005

Journal of Biological Chemistry

171

172

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Sponges (phylum Porifera) are the phylogenetically oldest metazoa; as filter feeders, they are abundantly exposed to marine microorganisms. Here we present data indicating that the demosponge Suberites domuncula is provided with a recognition system for Gramnegative bacteria. The lipopolysaccharide (LPS)-interacting protein was identified as a receptor on the sponge cell surface, which recognizes the bacterial endotoxin LPS. The cDNA was isolated, and the protein (M r 49,937) was expressed. During binding to LPS, the protein dimerizes and interacts with MyD88, which was also identified and cloned. The sponge MyD88 (M r 28,441) is composed of two protein interaction domains, a Toll/interleukin-1 receptor domain (found in MyD88 and in Toll-like receptors) and a death domain (present in MyD88 and interleukin-1 receptor-associated kinase). Northern blot experiments and in situ hybridization studies showed that after LPS treatment, the level of the LPS-interacting protein remains unchanged, whereas MyD88 is strongly up-regulated. A perforin-like molecule (M r 74,171), the macrophage-expressed protein, was identified as an executing molecule of this pathway. This gene is highly expressed after LPS treatment, especially at the surfaces of the animals. The recombinant protein possesses biological activity and eliminates Gram-negative bacteria; it is inactive against Gram-positive bacteria. These data indicate that S. domuncula is provided with an innate immune system against Gramnegative bacteria; the ligand LPS (a pathogen-associated molecular pattern) is recognized by the pattern recognition receptor (LPS-interacting protein), which interacts with MyD88. A signal transduction is established, which results in an elevated expression of MyD88 as well as of the macrophage-expressed protein as an executing protein.

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“…Well-known members of these proteins are the poreforming cytolysins such as the alpha-toxin from S. aureus (14), streptolysin O (35), E. coli hemolysin (3), hemolysin from Tethya lyncurium (29), and Leishmania cytolysin (32). The mechanism of membrane damage by the pore-forming proteins involves the binding of the toxin to the target cell membrane and penetration followed by disruption of the membrane and alteration of membrane permeability, leading to cytolysis (37).…”

Section: Discussionmentioning

confidence: 99%

Cytotoxic Activities of Leptospira interrogans Hemolysin SphH as a Pore-Forming Protein on Mammalian Cells

Lee¹,

Kim

Park³

et al. 2002

Infect Immun

101

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. Escherichia coli lysate harboring the sphH showed high hemolytic activities on sheep erythrocytes. However, it neither showed sphingomyelinase nor phospholipase activities, in contrast to SphA which was known to have sphingomyelinase activity. Interestingly, the SphH-mediated hemolysis on erythrocytes was osmotically protected by PEG 5000, suggesting that the SphH might have caused pore formation on the erythrocyte membrane. In the present study, we have prepared the Leptospira hemolysin SphH and investigated its hemolytic and cytotoxic activities on mammalian cells. SphH was shown to be a pore-forming protein on several mammalian cells: When treated with the SphH, the sheep erythrocyte membranes formed pores, which were morphologically confirmed by transmission electron microscopy. Furthermore, the SphH-mediated cytotoxicities on mammalian cells were demonstrated by the release of LDH and by inverted microscopic examinations. Finally, the immune serum against the full-length hemolysin could effectively neutralize the SphH-mediated hemolytic and cytotoxic activities. In conclusion, these results suggest that the virulence of Leptospira SphH was due to the pore formation on mammalian cell membranes.

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Purification and characterization of a pore‐forming protein from the marine sponge Tethya lyncurium

Cited by 34 publications

References 59 publications

Detecção de atividade lectínica e atividade hemolítica em extratos de esponjas (Porifera) nativas da costa atlântica do Brasil

Detecção de atividade lectínica e atividade hemolítica em extratos de esponjas (Porifera) nativas da costa atlântica do Brasil

Innate Immune Defense of the Sponge Suberites domuncula against Bacteria Involves a MyD88-dependent Signaling Pathway

Cytotoxic Activities of Leptospira interrogans Hemolysin SphH as a Pore-Forming Protein on Mammalian Cells

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