Sialic acid-containing glycans play a role in the activity of snake venom proteases
Structural variability is a feature of snake venom proteins, and glycosylation is a post-translational modification that contributes to the diversification of venom proteomes. Studies by our group have shown that Bothrops venoms are distinctly defined by their glycoprotein content, and that most hyb...
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| Veröffentlicht in: | Biochimie 2023-01, Vol.204, p.140-153 |
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| creator | Brás-Costa, Carolina Alencar Chaves, Alison Felipe Trevisan-Silva, Dilza Menezes, Milene C. Rocha, Marisa M.T. Cajado-Carvalho, Daniela Andrade-Silva, Débora Serrano, Solange M.T. |
| description | Structural variability is a feature of snake venom proteins, and glycosylation is a post-translational modification that contributes to the diversification of venom proteomes. Studies by our group have shown that Bothrops venoms are distinctly defined by their glycoprotein content, and that most hybrid/complex N-glycans identified in these venoms contain sialic acid. Considering that metalloproteases and serine proteases are abundant components of Bothrops venoms and essential in the envenomation process, and that these enzymes contain several glycosylation sites, the role of sialic acid in venom proteolytic activity was evaluated. Here we show that removal of sialic acid by treatment of nine Bothrops venoms with neuraminidase (i) altered the pattern of gelatinolysis in zymography of most venoms and reduced the gelatinolytic activity of all venoms, (ii) decreased the proteolytic activity of some venoms on fibrinogen and the clotting activity of human plasma of all venoms, and (iii) altered the proteolysis profile of plasma proteins by B. jararaca venom, suggesting that sialic acid may play a role in the interaction of proteases with their protein substrates. In contrast, the profile of venom amidolytic activity on Bz-Arg-pNA did not change after removal of sialic acid, indicating that this monosaccharide is not essential in N-glycans of serine proteases acting on small substrates. In summary, these results expand the knowledge about the variability of the subproteomes of Bothrops venom proteases, and for the first time point to the importance of carbohydrate chains containing sialic acid in the enzymatic activities of venom proteases relevant in human envenomation.
•Most hybrid/complex N-glycans identified in Bothrops venoms contain sialic acid.•Enzymatic removal of sialic acid decreased proteolytic activity of nine Bothrops venoms on different substrates.•Sialic acid-containing glycans play a role in the activity of snake venom proteases. |
| doi_str_mv | 10.1016/j.biochi.2022.09.011 |
| format | Article |
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•Most hybrid/complex N-glycans identified in Bothrops venoms contain sialic acid.•Enzymatic removal of sialic acid decreased proteolytic activity of nine Bothrops venoms on different substrates.•Sialic acid-containing glycans play a role in the activity of snake venom proteases.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/j.biochi.2022.09.011</identifier><identifier>PMID: 36210615</identifier><language>eng</language><publisher>France: Elsevier B.V</publisher><subject>Animals ; Bothrops ; Bothrops - metabolism ; Crotalid Venoms - chemistry ; Glycoprotein ; Glycoproteins - metabolism ; Humans ; Mass spectrometry ; N-Acetylneuraminic Acid - metabolism ; Polysaccharides - metabolism ; Protease ; Serine Endopeptidases - metabolism ; Serine Proteases - metabolism ; Sialic acid ; Snake venom ; Snake Venoms</subject><ispartof>Biochimie, 2023-01, Vol.204, p.140-153</ispartof><rights>2022 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM)</rights><rights>Copyright © 2022 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c362t-187c2b10350c1e69e6d451c7fd94d9b71241c00972262000b093df38886d20843</citedby><cites>FETCH-LOGICAL-c362t-187c2b10350c1e69e6d451c7fd94d9b71241c00972262000b093df38886d20843</cites><orcidid>0000-0001-8994-1904</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.biochi.2022.09.011$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36210615$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brás-Costa, Carolina</creatorcontrib><creatorcontrib>Alencar Chaves, Alison Felipe</creatorcontrib><creatorcontrib>Trevisan-Silva, Dilza</creatorcontrib><creatorcontrib>Menezes, Milene C.</creatorcontrib><creatorcontrib>Rocha, Marisa M.T.</creatorcontrib><creatorcontrib>Cajado-Carvalho, Daniela</creatorcontrib><creatorcontrib>Andrade-Silva, Débora</creatorcontrib><creatorcontrib>Serrano, Solange M.T.</creatorcontrib><title>Sialic acid-containing glycans play a role in the activity of snake venom proteases</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>Structural variability is a feature of snake venom proteins, and glycosylation is a post-translational modification that contributes to the diversification of venom proteomes. Studies by our group have shown that Bothrops venoms are distinctly defined by their glycoprotein content, and that most hybrid/complex N-glycans identified in these venoms contain sialic acid. Considering that metalloproteases and serine proteases are abundant components of Bothrops venoms and essential in the envenomation process, and that these enzymes contain several glycosylation sites, the role of sialic acid in venom proteolytic activity was evaluated. Here we show that removal of sialic acid by treatment of nine Bothrops venoms with neuraminidase (i) altered the pattern of gelatinolysis in zymography of most venoms and reduced the gelatinolytic activity of all venoms, (ii) decreased the proteolytic activity of some venoms on fibrinogen and the clotting activity of human plasma of all venoms, and (iii) altered the proteolysis profile of plasma proteins by B. jararaca venom, suggesting that sialic acid may play a role in the interaction of proteases with their protein substrates. In contrast, the profile of venom amidolytic activity on Bz-Arg-pNA did not change after removal of sialic acid, indicating that this monosaccharide is not essential in N-glycans of serine proteases acting on small substrates. In summary, these results expand the knowledge about the variability of the subproteomes of Bothrops venom proteases, and for the first time point to the importance of carbohydrate chains containing sialic acid in the enzymatic activities of venom proteases relevant in human envenomation.
•Most hybrid/complex N-glycans identified in Bothrops venoms contain sialic acid.•Enzymatic removal of sialic acid decreased proteolytic activity of nine Bothrops venoms on different substrates.•Sialic acid-containing glycans play a role in the activity of snake venom proteases.</description><subject>Animals</subject><subject>Bothrops</subject><subject>Bothrops - metabolism</subject><subject>Crotalid Venoms - chemistry</subject><subject>Glycoprotein</subject><subject>Glycoproteins - metabolism</subject><subject>Humans</subject><subject>Mass spectrometry</subject><subject>N-Acetylneuraminic Acid - metabolism</subject><subject>Polysaccharides - metabolism</subject><subject>Protease</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Serine Proteases - metabolism</subject><subject>Sialic acid</subject><subject>Snake venom</subject><subject>Snake Venoms</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LxDAQhoMoun78A5EcvbROkjZtLoKIXyB4UM8hTaaatZusTXdh_72RVY-e5vK88848hJwyKBkweTEvOx_tuy85cF6CKoGxHTJjUrSFZK3YJTMQAIWCtjoghynNAaAGrvbJgZCcgWT1jDw_ezN4S431rrAxTMYHH97o27CxJiS6HMyGGjrGAakPdHrHjE5-7acNjT1NwXwgXWOIC7oc44QmYTome70ZEp78zCPyenvzcn1fPD7dPVxfPRY2908FaxvLOwaiBstQKpSuqplteqcqp7qG8YpZANVwLnm-vQMlXC_atpWO56fEETnf7s3NnytMk174ZHEYTMC4Spo3XFRt0_A6o9UWtWNMacReL0e_MONGM9DfOvVcb3Xqb50alM46c-zsp2HVLdD9hX79ZeByC2D-c-1x1Ml6DBadH9FO2kX_f8MXIi-GPg</recordid><startdate>202301</startdate><enddate>202301</enddate><creator>Brás-Costa, Carolina</creator><creator>Alencar Chaves, Alison Felipe</creator><creator>Trevisan-Silva, Dilza</creator><creator>Menezes, Milene C.</creator><creator>Rocha, Marisa M.T.</creator><creator>Cajado-Carvalho, Daniela</creator><creator>Andrade-Silva, Débora</creator><creator>Serrano, Solange M.T.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-8994-1904</orcidid></search><sort><creationdate>202301</creationdate><title>Sialic acid-containing glycans play a role in the activity of snake venom proteases</title><author>Brás-Costa, Carolina ; Alencar Chaves, Alison Felipe ; Trevisan-Silva, Dilza ; Menezes, Milene C. ; Rocha, Marisa M.T. ; Cajado-Carvalho, Daniela ; Andrade-Silva, Débora ; Serrano, Solange M.T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c362t-187c2b10350c1e69e6d451c7fd94d9b71241c00972262000b093df38886d20843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Animals</topic><topic>Bothrops</topic><topic>Bothrops - metabolism</topic><topic>Crotalid Venoms - chemistry</topic><topic>Glycoprotein</topic><topic>Glycoproteins - metabolism</topic><topic>Humans</topic><topic>Mass spectrometry</topic><topic>N-Acetylneuraminic Acid - metabolism</topic><topic>Polysaccharides - metabolism</topic><topic>Protease</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Serine Proteases - metabolism</topic><topic>Sialic acid</topic><topic>Snake venom</topic><topic>Snake Venoms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brás-Costa, Carolina</creatorcontrib><creatorcontrib>Alencar Chaves, Alison Felipe</creatorcontrib><creatorcontrib>Trevisan-Silva, Dilza</creatorcontrib><creatorcontrib>Menezes, Milene C.</creatorcontrib><creatorcontrib>Rocha, Marisa M.T.</creatorcontrib><creatorcontrib>Cajado-Carvalho, Daniela</creatorcontrib><creatorcontrib>Andrade-Silva, Débora</creatorcontrib><creatorcontrib>Serrano, Solange M.T.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brás-Costa, Carolina</au><au>Alencar Chaves, Alison Felipe</au><au>Trevisan-Silva, Dilza</au><au>Menezes, Milene C.</au><au>Rocha, Marisa M.T.</au><au>Cajado-Carvalho, Daniela</au><au>Andrade-Silva, Débora</au><au>Serrano, Solange M.T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sialic acid-containing glycans play a role in the activity of snake venom proteases</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>2023-01</date><risdate>2023</risdate><volume>204</volume><spage>140</spage><epage>153</epage><pages>140-153</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>Structural variability is a feature of snake venom proteins, and glycosylation is a post-translational modification that contributes to the diversification of venom proteomes. Studies by our group have shown that Bothrops venoms are distinctly defined by their glycoprotein content, and that most hybrid/complex N-glycans identified in these venoms contain sialic acid. Considering that metalloproteases and serine proteases are abundant components of Bothrops venoms and essential in the envenomation process, and that these enzymes contain several glycosylation sites, the role of sialic acid in venom proteolytic activity was evaluated. Here we show that removal of sialic acid by treatment of nine Bothrops venoms with neuraminidase (i) altered the pattern of gelatinolysis in zymography of most venoms and reduced the gelatinolytic activity of all venoms, (ii) decreased the proteolytic activity of some venoms on fibrinogen and the clotting activity of human plasma of all venoms, and (iii) altered the proteolysis profile of plasma proteins by B. jararaca venom, suggesting that sialic acid may play a role in the interaction of proteases with their protein substrates. In contrast, the profile of venom amidolytic activity on Bz-Arg-pNA did not change after removal of sialic acid, indicating that this monosaccharide is not essential in N-glycans of serine proteases acting on small substrates. In summary, these results expand the knowledge about the variability of the subproteomes of Bothrops venom proteases, and for the first time point to the importance of carbohydrate chains containing sialic acid in the enzymatic activities of venom proteases relevant in human envenomation.
•Most hybrid/complex N-glycans identified in Bothrops venoms contain sialic acid.•Enzymatic removal of sialic acid decreased proteolytic activity of nine Bothrops venoms on different substrates.•Sialic acid-containing glycans play a role in the activity of snake venom proteases.</abstract><cop>France</cop><pub>Elsevier B.V</pub><pmid>36210615</pmid><doi>10.1016/j.biochi.2022.09.011</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0001-8994-1904</orcidid></addata></record> |
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| ispartof | Biochimie, 2023-01, Vol.204, p.140-153 |
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| subjects | Animals Bothrops Bothrops - metabolism Crotalid Venoms - chemistry Glycoprotein Glycoproteins - metabolism Humans Mass spectrometry N-Acetylneuraminic Acid - metabolism Polysaccharides - metabolism Protease Serine Endopeptidases - metabolism Serine Proteases - metabolism Sialic acid Snake venom Snake Venoms |
| title | Sialic acid-containing glycans play a role in the activity of snake venom proteases |
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