Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases.
Chelt, a cholera-like toxin from Vibrio cholerae, and Certhrax, an anthrax-like toxin from Bacillus cereus, are among six new bacterial protein toxins we identified and characterized using in silico and cell-based techniques. We also uncovered medically relevant toxins from Mycobacterium avium and E...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2010-01-01
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| Series: | PLoS Computational Biology |
| Online Access: | http://europepmc.org/articles/PMC3000352?pdf=render |
| _version_ | 1828445284263264256 |
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| author | Robert J Fieldhouse Zachari Turgeon Dawn White A Rod Merrill |
| author_facet | Robert J Fieldhouse Zachari Turgeon Dawn White A Rod Merrill |
| author_sort | Robert J Fieldhouse |
| collection | DOAJ |
| description | Chelt, a cholera-like toxin from Vibrio cholerae, and Certhrax, an anthrax-like toxin from Bacillus cereus, are among six new bacterial protein toxins we identified and characterized using in silico and cell-based techniques. We also uncovered medically relevant toxins from Mycobacterium avium and Enterococcus faecalis. We found agriculturally relevant toxins in Photorhabdus luminescens and Vibrio splendidus. These toxins belong to the ADP-ribosyltransferase family that has conserved structure despite low sequence identity. Therefore, our search for new toxins combined fold recognition with rules for filtering sequences--including a primary sequence pattern--to reduce reliance on sequence identity and identify toxins using structure. We used computers to build models and analyzed each new toxin to understand features including: structure, secretion, cell entry, activation, NAD+ substrate binding, intracellular target binding and the reaction mechanism. We confirmed activity using a yeast growth test. In this era where an expanding protein structure library complements abundant protein sequence data--and we need high-throughput validation--our approach provides insight into the newest toxin ADP-ribosyltransferases. |
| first_indexed | 2024-12-10T21:56:07Z |
| format | Article |
| id | doaj.art-fd166c4f9590407bb984f99440ecba36 |
| institution | Directory Open Access Journal |
| issn | 1553-734X 1553-7358 |
| language | English |
| last_indexed | 2024-12-10T21:56:07Z |
| publishDate | 2010-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Computational Biology |
| spelling | doaj.art-fd166c4f9590407bb984f99440ecba362022-12-22T01:32:03ZengPublic Library of Science (PLoS)PLoS Computational Biology1553-734X1553-73582010-01-01612e100102910.1371/journal.pcbi.1001029Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases.Robert J FieldhouseZachari TurgeonDawn WhiteA Rod MerrillChelt, a cholera-like toxin from Vibrio cholerae, and Certhrax, an anthrax-like toxin from Bacillus cereus, are among six new bacterial protein toxins we identified and characterized using in silico and cell-based techniques. We also uncovered medically relevant toxins from Mycobacterium avium and Enterococcus faecalis. We found agriculturally relevant toxins in Photorhabdus luminescens and Vibrio splendidus. These toxins belong to the ADP-ribosyltransferase family that has conserved structure despite low sequence identity. Therefore, our search for new toxins combined fold recognition with rules for filtering sequences--including a primary sequence pattern--to reduce reliance on sequence identity and identify toxins using structure. We used computers to build models and analyzed each new toxin to understand features including: structure, secretion, cell entry, activation, NAD+ substrate binding, intracellular target binding and the reaction mechanism. We confirmed activity using a yeast growth test. In this era where an expanding protein structure library complements abundant protein sequence data--and we need high-throughput validation--our approach provides insight into the newest toxin ADP-ribosyltransferases.http://europepmc.org/articles/PMC3000352?pdf=render |
| spellingShingle | Robert J Fieldhouse Zachari Turgeon Dawn White A Rod Merrill Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases. PLoS Computational Biology |
| title | Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases. |
| title_full | Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases. |
| title_fullStr | Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases. |
| title_full_unstemmed | Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases. |
| title_short | Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases. |
| title_sort | cholera and anthrax like toxins are among several new adp ribosyltransferases |
| url | http://europepmc.org/articles/PMC3000352?pdf=render |
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