Clostridial Neurotoxins: Structure, Function and Implications to Other Bacterial Toxins
Gram-positive bacteria are ancient organisms. Many bacteria, including Gram-positive bacteria, produce toxins to manipulate the host, leading to various diseases. While the targets of Gram-positive bacterial toxins are diverse, many of those toxins use a similar mechanism to invade host cells and ex...
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oai:doaj.org-article:3950ad8acce844afb763d7c12c31833b2021-11-25T18:24:15ZClostridial Neurotoxins: Structure, Function and Implications to Other Bacterial Toxins10.3390/microorganisms91122062076-2607https://doaj.org/article/3950ad8acce844afb763d7c12c31833b2021-10-01T00:00:00Zhttps://www.mdpi.com/2076-2607/9/11/2206https://doaj.org/toc/2076-2607Gram-positive bacteria are ancient organisms. Many bacteria, including Gram-positive bacteria, produce toxins to manipulate the host, leading to various diseases. While the targets of Gram-positive bacterial toxins are diverse, many of those toxins use a similar mechanism to invade host cells and exert their functions. Clostridial neurotoxins produced by <i>Clostridial tetani</i> and <i>Clostridial botulinum</i> provide a classical example to illustrate the structure–function relationship of bacterial toxins. Here, we critically review the recent progress of the structure–function relationship of clostridial neurotoxins, including the diversity of the clostridial neurotoxins, the mode of actions, and the flexible structures required for the activation of toxins. The mechanism clostridial neurotoxins use for triggering their activity is shared with many other Gram-positive bacterial toxins, especially molten globule-type structures. This review also summarizes the implications of the molten globule-type flexible structures to other Gram-positive bacterial toxins. Understanding these highly dynamic flexible structures in solution and their role in the function of bacterial toxins not only fills in the missing link of the high-resolution structures from X-ray crystallography but also provides vital information for better designing antidotes against those toxins.Shuowei CaiRaj KumarBal Ram SinghMDPI AGarticleGram-positive bacterial toxinsclostridial neurotoxinbotulinum neurotoxintetanus neurotoxinmolten globulediphtheria toxinBiology (General)QH301-705.5ENMicroorganisms, Vol 9, Iss 2206, p 2206 (2021) |
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DOAJ |
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Gram-positive bacterial toxins clostridial neurotoxin botulinum neurotoxin tetanus neurotoxin molten globule diphtheria toxin Biology (General) QH301-705.5 |
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Gram-positive bacterial toxins clostridial neurotoxin botulinum neurotoxin tetanus neurotoxin molten globule diphtheria toxin Biology (General) QH301-705.5 Shuowei Cai Raj Kumar Bal Ram Singh Clostridial Neurotoxins: Structure, Function and Implications to Other Bacterial Toxins |
description |
Gram-positive bacteria are ancient organisms. Many bacteria, including Gram-positive bacteria, produce toxins to manipulate the host, leading to various diseases. While the targets of Gram-positive bacterial toxins are diverse, many of those toxins use a similar mechanism to invade host cells and exert their functions. Clostridial neurotoxins produced by <i>Clostridial tetani</i> and <i>Clostridial botulinum</i> provide a classical example to illustrate the structure–function relationship of bacterial toxins. Here, we critically review the recent progress of the structure–function relationship of clostridial neurotoxins, including the diversity of the clostridial neurotoxins, the mode of actions, and the flexible structures required for the activation of toxins. The mechanism clostridial neurotoxins use for triggering their activity is shared with many other Gram-positive bacterial toxins, especially molten globule-type structures. This review also summarizes the implications of the molten globule-type flexible structures to other Gram-positive bacterial toxins. Understanding these highly dynamic flexible structures in solution and their role in the function of bacterial toxins not only fills in the missing link of the high-resolution structures from X-ray crystallography but also provides vital information for better designing antidotes against those toxins. |
format |
article |
author |
Shuowei Cai Raj Kumar Bal Ram Singh |
author_facet |
Shuowei Cai Raj Kumar Bal Ram Singh |
author_sort |
Shuowei Cai |
title |
Clostridial Neurotoxins: Structure, Function and Implications to Other Bacterial Toxins |
title_short |
Clostridial Neurotoxins: Structure, Function and Implications to Other Bacterial Toxins |
title_full |
Clostridial Neurotoxins: Structure, Function and Implications to Other Bacterial Toxins |
title_fullStr |
Clostridial Neurotoxins: Structure, Function and Implications to Other Bacterial Toxins |
title_full_unstemmed |
Clostridial Neurotoxins: Structure, Function and Implications to Other Bacterial Toxins |
title_sort |
clostridial neurotoxins: structure, function and implications to other bacterial toxins |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doaj.org/article/3950ad8acce844afb763d7c12c31833b |
work_keys_str_mv |
AT shuoweicai clostridialneurotoxinsstructurefunctionandimplicationstootherbacterialtoxins AT rajkumar clostridialneurotoxinsstructurefunctionandimplicationstootherbacterialtoxins AT balramsingh clostridialneurotoxinsstructurefunctionandimplicationstootherbacterialtoxins |
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1718411187786350592 |