Dataset Information

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases.

ABSTRACT: Bacterial collagenolytic proteases are important because of their essential role in global collagen degradation and because of their virulence in some human bacterial infections. Bacterial collagenolytic proteases include some metalloproteases of the M9 family from Clostridium or Vibrio strains, some serine proteases distributed in the S1, S8, and S53 families, and members of the U32 family. In recent years, there has been remarkable progress in discovering new bacterial collagenolytic proteases and in investigating the collagen-degrading mechanisms of bacterial collagenolytic proteases. This review provides comprehensive insight into bacterial collagenolytic proteases, especially focusing on the structures and collagen-degrading mechanisms of representative bacterial collagenolytic proteases in each family. The roles of bacterial collagenolytic proteases in human diseases and global nitrogen cycling, together with the biotechnological and medical applications for these proteases, are also briefly discussed.

SUBMITTER: Zhang YZ

PROVIDER: S-EPMC4542243 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature

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Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases.

Zhang Yu-Zhong YZ Ran Li-Yuan LY Li Chun-Yang CY Chen Xiu-Lan XL

Applied and environmental microbiology 20150706 18

Bacterial collagenolytic proteases are important because of their essential role in global collagen degradation and because of their virulence in some human bacterial infections. Bacterial collagenolytic proteases include some metalloproteases of the M9 family from Clostridium or Vibrio strains, some serine proteases distributed in the S1, S8, and S53 families, and members of the U32 family. In recent years, there has been remarkable progress in discovering new bacterial collagenolytic proteases ...[more]

PMID: 26150451

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Project description:Introduction and aimThe presence of host collagenases in the degradation of the protein matrix at later stages of carious dentin lesions development, as well as the potential involvement of bacterial collagenases, have been suggested but lack conclusive evidence. This study aims to conduct a systematic review to comprehensively assess the profile of host and bacterial-derived collagenolytic proteases in both root and coronal dentin carious lesions.MethodsThe search was performed in eight databases and the grey literature. Studies evaluating ex vivo dentin, extracted teeth, or biofilms from natural caries lesions were included. The methodological quality of studies was assessed using the Joanna Briggs Institute tool. Synthesis of the results and the certainty of evidence were performed following the Synthesis without Meta-analysis (SWiM) checklist and GRADE approach for narrative synthesis, respectively.ResultsFrom 935 recovered articles, 18 were included. Although the evidence was very uncertain, it was possible to suggest that 1) MMP-2, MMP-9, MMP-13, and CT-B may be increased in carious dentin when compared to sound dentin; 2) there is no difference in MMP-2 presence, while MMP-13 may be increased in root when compared to coronal carious dentin; 3) there is no difference of MMP-2 and MMP-9 expression/activity before and after cavity sealing; 4) MMP-8 may be increased in the dentin before cavity sealing compared to dentin after cavity sealing; 5) there is no difference of MMP-20 in irradiated vs. non-irradiated carious dentin. MMP-20 probably reduces in carious outer dentin when compared to carious inner dentin (moderate certainty). Genes encoding bacterial collagenolytic proteases and protein-degrading bacteria were detected in coronal and root carious lesions.ConclusionTrends in the direction of the effect were observed for some collagenolytic proteases in carious dentin, which may represent a potential target for the development of new treatments. (Protocol register-PROSPERO: CRD42020213141).

Project description:Numerous varieties of life forms have filled the earth throughout evolution. Evolution consists of two processes: self-replication and interaction with the physical environment and other living things around it. Initiated by von Neumann et al. studies on self-replication in cellular automata have attracted much attention, which aim to explore the logical mechanism underlying the replication of living things. In nature, competition is a common and spontaneous resource to drive self-replications, whereas most cellular-automaton-based models merely focus on some self-protection mechanisms that may deprive the rights of other artificial life (loops) to live. Especially, Huang et al. designed a self-adaptive, self-replicating model using a greedy selection mechanism, which can increase the ability of loops to survive through an occasionally abandoning part of their own structural information, for the sake of adapting to the restricted environment. Though this passive adaptation can improve diversity, it is always limited by the loop's original structure and is unable to evolve or mutate new genes in a way that is consistent with the adaptive evolution of natural life. Furthermore, it is essential to implement more complex self-adaptive evolutionary mechanisms not at the cost of increasing the complexity of cellular automata. To this end, this article proposes new self-adaptive mechanisms, which can change the information of structural genes and actively adapt to the environment when the arm of a self-replicating loop encounters obstacles, thereby increasing the chance of replication. Meanwhile, our mechanisms can also actively add a proper orientation to the current construction arm for the sake of breaking through the deadlock situation. Our new mechanisms enable active self-adaptations in comparison with the passive mechanism in the work of Huang et al. which is achieved by including a few rules without increasing the number of cell states as compared to the latter. Experiments demonstrate that this active self-adaptability can bring more diversity than the previous mechanism, whereby it may facilitate the emergence of various levels in self-replicating structures.

Dataset Information

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases.

Publications

Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases.

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