Autocatalytic association of proteins by covalent bond formation: a Bio Molecular Welding toolbox derived from a bacterial adhesin
Unusual intramolecular cross-links present in adhesins from Gram-positive bacteria have been used to develop a generic process amenable to biotechnology applications. Based on the crystal structure of RrgA, the Streptococcus pneumoniae pilus adhesin, we provide evidence that two engineered protein f...
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| Veröffentlicht in: | Scientific reports 2017-03, Vol.7 (1), p.43564-43564, Article 43564 |
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| creator | Bonnet, J. Cartannaz, J. Tourcier, G. Contreras-Martel, C. Kleman, J. P. Morlot, C. Vernet, T. Di Guilmi, A. M. |
| description | Unusual intramolecular cross-links present in adhesins from Gram-positive bacteria have been used to develop a generic process amenable to biotechnology applications. Based on the crystal structure of RrgA, the
Streptococcus pneumoniae
pilus adhesin, we provide evidence that two engineered protein fragments retain their ability to associate covalently with high specificity,
in vivo
and
in vitro
, once isolated from the parent protein. We determined the optimal conditions for the assembly of the complex and we solved its crystal structure at 2 Å. Furthermore, we demonstrate biotechnological applications related to antibody production, nanoassembly and cell-surface labeling based on this process we named Bio Molecular Welding. |
| doi_str_mv | 10.1038/srep43564 |
| format | Article |
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Streptococcus pneumoniae
pilus adhesin, we provide evidence that two engineered protein fragments retain their ability to associate covalently with high specificity,
in vivo
and
in vitro
, once isolated from the parent protein. We determined the optimal conditions for the assembly of the complex and we solved its crystal structure at 2 Å. Furthermore, we demonstrate biotechnological applications related to antibody production, nanoassembly and cell-surface labeling based on this process we named Bio Molecular Welding.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep43564</identifier><identifier>PMID: 28252635</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13/44 ; 14/35 ; 631/61/338 ; 631/92/612 ; 82/1 ; 82/16 ; 82/29 ; 82/58 ; 82/80 ; 82/83 ; Adhesins ; Bacteria ; Biochemistry, Molecular Biology ; Biotechnology ; Cell surface ; Crystal structure ; Gram-positive bacteria ; Humanities and Social Sciences ; Life Sciences ; multidisciplinary ; Science ; Streptococcus infections ; Structural Biology ; Welding</subject><ispartof>Scientific reports, 2017-03, Vol.7 (1), p.43564-43564, Article 43564</ispartof><rights>The Author(s) 2017</rights><rights>Copyright Nature Publishing Group Mar 2017</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>Copyright © 2017, The Author(s) 2017 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c472t-9a31110489254fad52bc349cc1aa99a3f40af702d9a7cee50dffd7f731f44d793</citedby><cites>FETCH-LOGICAL-c472t-9a31110489254fad52bc349cc1aa99a3f40af702d9a7cee50dffd7f731f44d793</cites><orcidid>0000-0002-9295-1035 ; 0000-0002-4595-9317 ; 0000-0003-1151-5766 ; 0000-0001-5648-5295 ; 0000-0003-2034-7944</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5333627/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5333627/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28252635$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01485073$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Bonnet, J.</creatorcontrib><creatorcontrib>Cartannaz, J.</creatorcontrib><creatorcontrib>Tourcier, G.</creatorcontrib><creatorcontrib>Contreras-Martel, C.</creatorcontrib><creatorcontrib>Kleman, J. P.</creatorcontrib><creatorcontrib>Morlot, C.</creatorcontrib><creatorcontrib>Vernet, T.</creatorcontrib><creatorcontrib>Di Guilmi, A. M.</creatorcontrib><title>Autocatalytic association of proteins by covalent bond formation: a Bio Molecular Welding toolbox derived from a bacterial adhesin</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Unusual intramolecular cross-links present in adhesins from Gram-positive bacteria have been used to develop a generic process amenable to biotechnology applications. Based on the crystal structure of RrgA, the
Streptococcus pneumoniae
pilus adhesin, we provide evidence that two engineered protein fragments retain their ability to associate covalently with high specificity,
in vivo
and
in vitro
, once isolated from the parent protein. We determined the optimal conditions for the assembly of the complex and we solved its crystal structure at 2 Å. Furthermore, we demonstrate biotechnological applications related to antibody production, nanoassembly and cell-surface labeling based on this process we named Bio Molecular Welding.</description><subject>13/44</subject><subject>14/35</subject><subject>631/61/338</subject><subject>631/92/612</subject><subject>82/1</subject><subject>82/16</subject><subject>82/29</subject><subject>82/58</subject><subject>82/80</subject><subject>82/83</subject><subject>Adhesins</subject><subject>Bacteria</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biotechnology</subject><subject>Cell surface</subject><subject>Crystal structure</subject><subject>Gram-positive bacteria</subject><subject>Humanities and Social Sciences</subject><subject>Life Sciences</subject><subject>multidisciplinary</subject><subject>Science</subject><subject>Streptococcus infections</subject><subject>Structural Biology</subject><subject>Welding</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>BENPR</sourceid><recordid>eNplkk1vEzEQhlcIRKvSA38AWeIClQL-XGc5IIUKKFIQFxBHa9YfiSvvOtjeiFz7y3FJCaH4Ymvm8ft6PNM0Twl-RTCbv87JbjgTLX_QnFLMxYwySh8enU-a85yvcV2Cdpx0j5sTOqeCtkycNjeLqUQNBcKueI0g56g9FB9HFB3apFisHzPqd0jHLQQ7FtTH0SAX0_Abe4MAvfMRfY7B6ilAQt9tMH5coRJj6ONPZGzyW1uvpDhUuAddagQCArO22Y9PmkcOQrbnd_tZ8-3D-6-XV7Pll4-fLhfLmeaSllkHjBCC-byjgjswgvaa8U5rAtDVpOMYnMTUdCC1tQIb54x0khHHuZEdO2ve7nU3Uz9Yo2stCYLaJD9A2qkIXv2bGf1areJWCcZYS2UVeLkXWN-7drVYqtsYJnwusGRbUtkXd2Yp_phsLmrwWdsQYLRxyorMJZOUYc4r-vweeh2nNNavUKTD1Zq0Lf5rrlPMtefu8AKC1e0gqMMgVPbZcaUH8k_bK3CxB3JNjSubjiz_U_sFLI6-fg</recordid><startdate>20170302</startdate><enddate>20170302</enddate><creator>Bonnet, J.</creator><creator>Cartannaz, J.</creator><creator>Tourcier, G.</creator><creator>Contreras-Martel, C.</creator><creator>Kleman, J. 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P.</au><au>Morlot, C.</au><au>Vernet, T.</au><au>Di Guilmi, A. M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Autocatalytic association of proteins by covalent bond formation: a Bio Molecular Welding toolbox derived from a bacterial adhesin</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2017-03-02</date><risdate>2017</risdate><volume>7</volume><issue>1</issue><spage>43564</spage><epage>43564</epage><pages>43564-43564</pages><artnum>43564</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Unusual intramolecular cross-links present in adhesins from Gram-positive bacteria have been used to develop a generic process amenable to biotechnology applications. Based on the crystal structure of RrgA, the
Streptococcus pneumoniae
pilus adhesin, we provide evidence that two engineered protein fragments retain their ability to associate covalently with high specificity,
in vivo
and
in vitro
, once isolated from the parent protein. We determined the optimal conditions for the assembly of the complex and we solved its crystal structure at 2 Å. Furthermore, we demonstrate biotechnological applications related to antibody production, nanoassembly and cell-surface labeling based on this process we named Bio Molecular Welding.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>28252635</pmid><doi>10.1038/srep43564</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-9295-1035</orcidid><orcidid>https://orcid.org/0000-0002-4595-9317</orcidid><orcidid>https://orcid.org/0000-0003-1151-5766</orcidid><orcidid>https://orcid.org/0000-0001-5648-5295</orcidid><orcidid>https://orcid.org/0000-0003-2034-7944</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 13/44 14/35 631/61/338 631/92/612 82/1 82/16 82/29 82/58 82/80 82/83 Adhesins Bacteria Biochemistry, Molecular Biology Biotechnology Cell surface Crystal structure Gram-positive bacteria Humanities and Social Sciences Life Sciences multidisciplinary Science Streptococcus infections Structural Biology Welding |
| title | Autocatalytic association of proteins by covalent bond formation: a Bio Molecular Welding toolbox derived from a bacterial adhesin |
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