Characterization and phylogenetic analysis of the chitinase gene from the Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus

Wang, Hualin; Wu, Dong; Deng, Fei; Peng, Haiyi; Chen, Xinwen; Lauzon, Hilary A. M.; Arif, Basil M.; Jehle, Johannes A.; Hú, Zhìhóng

doi:10.1016/j.virusres.2003.11.015

Cited by 20 publications

(20 citation statements)

References 43 publications

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“…Recent work suggested a monophyletic origin of bacterial and fungal GH18s [Gan et al, 2007b;Wang et al, 2004], although with lateral transfer of GH18 genes between different bacterial groups [Cottrell et al, 2000;Wang et al, 2004]. We show that bacterial and fungal GH18 genes do not form monophyletic groups and that the previously suggested relationships between bacterial and fungal GH18s are based on incomplete coverage of GH18 diversity [Dong et al, 2007;Gan et al, 2007a;Wang et al, 2004].…”

Section: Discussionmentioning

confidence: 38%

“…We show that bacterial and fungal GH18 genes do not form monophyletic groups and that the previously suggested relationships between bacterial and fungal GH18s are based on incomplete coverage of GH18 diversity [Dong et al, 2007;Gan et al, 2007a;Wang et al, 2004]. This emphasizes the importance of complete coverage of members in protein families within a single species and to analyze evolution of proteins across taxonomic borders, something which is greatly assisted by the growing numbers of completed genome sequences from all parts of the tree of life.…”

Section: Discussionmentioning

confidence: 67%

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Evolution of Family 18 Glycoside Hydrolases: Diversity, Domain Structures and Phylogenetic Relationships

Karlsson

Stenlid²

2008

Microb Physiol

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Chitin and its derivates have many industrial and medical uses. There is a demand for chitin-modifying enzymes with new or modified properties and as microorganisms are the primary degraders of chitin in the environment, they provide a source of chitin-modifying enzymes with novel properties. We have analyzed the diversity, domain structure and phylogenetic relationships between family 18 chitinases based on complete genome sequences of bacteria, archaea, viruses, fungi, plants and animals. Our study shows that family 18 chitinases are divided into three main clusters, A, B and C. Clusters A and B both contain family 18 chitinases from bacteria, fungi and plants, suggesting that the differentiation of cluster A and B chitinases preceded the appearance of the eukaryotic lineage. Subgroups within clusters can have specific domain structures, as well as specific amino acid replacements in catalytic sites, which imply functional adaptation. This work provides a comprehensive overview of the evolutionary relationships of family 18 chitinases and provides a context for further investigations on functional aspects of family 18 chitinases in ecology and biotechnology.

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Section: Discussionmentioning

confidence: 38%

Section: Discussionmentioning

confidence: 67%

Evolution of Family 18 Glycoside Hydrolases: Diversity, Domain Structures and Phylogenetic Relationships

Karlsson

Stenlid²

2008

Microb Physiol

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“…DNA sequence analysis of chiI gene with FramePlot software (Ishikawa and Hotta 1999) reveals that it has a high G+C content (64.9%) with a typically actinobacterial codon distribution; i.e., no sign of horizontal gene transfer (HGT) from Gram-negative bacteria. The extensive analysis by Karlsson and Stenlid (2009) also highlighted the fact that GH18 bacterial and fungal chitinases genes do not form monophyletic groups, in opposition to earlier suggestions (Gan et al 2007; Wang et al 2004). …”

Section: Molecular Evolution Of Chitinolytic Enzymes In Actinobacteriamentioning

confidence: 90%

Chitinolytic functions in actinobacteria: ecology, enzymes, and evolution

Lacombe-Harvey

Brzeziński

Beaulieu

2018

Appl Microbiol Biotechnol

110

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Actinobacteria, a large group of Gram-positive bacteria, secrete a wide range of extracellular enzymes involved in the degradation of organic compounds and biopolymers including the ubiquitous aminopolysaccharides chitin and chitosan. While chitinolytic enzymes are distributed in all kingdoms of life, actinobacteria are recognized as particularly good decomposers of chitinous material and several members of this taxon carry impressive sets of genes dedicated to chitin and chitosan degradation. Degradation of these polymers in actinobacteria is dependent on endo- and exo-acting hydrolases as well as lytic polysaccharide monooxygenases. Actinobacterial chitinases and chitosanases belong to nine major families of glycosyl hydrolases that share no sequence similarity. In this paper, the distribution of chitinolytic actinobacteria within different ecosystems is examined and their chitinolytic machinery is described and compared to those of other chitinolytic organisms.Electronic supplementary materialThe online version of this article (10.1007/s00253-018-9149-4) contains supplementary material, which is available to authorized users.

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“…Its DNA genome is 131 kb and contains 135 open reading frames (ORFs) that potentially encode proteins of 50 amino acids (aa) or larger (13). Several HearNPV genes, such as the polyhedrin gene (polh) (14), the ecdysteroid UDP-glucosyltransferase gene (egt) (15), the late expression factor 2 gene (lef-2) (12), the basic DNA-binding protein gene (p6.9) (61), ha122 (37), Ha94 (19), chitinase (60), fp25K (67), p10 (18), and the F-protein gene (ha133) (36), have been characterized.…”

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confidence: 99%

Proteomics Analysis of Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus Identified Two New Occlusion-Derived Virus-Associated Proteins, HA44 and HA100

Deng

Wang

Mao

et al. 2007

J Virol

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Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometry were used to analyze the structural proteins of the occlusion-derived virus (ODV) of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus (HearNPV), a group II NPV. Twenty-three structural proteins of HearNPV ODV were identified, 21 of which have been reported previously as structural proteins or ODV-associated proteins in other baculoviruses. These include polyhedrin, P78/83, P49, ODV-E18, ODV-EC27, ODV-E56, P74, LEF-3, HA66 (AC66), DNA polymerase, GP41, VP39, P33, ODV-E25, helicase, P6.9, ODV/BV-C42, VP80, ODV-EC43, ODV-E66, and PIF-1. Two proteins encoded by HearNPV ORF44 (ha44) and ORF100 (ha100) were discovered as ODV-associated proteins for the first time. ha44 encodes a protein of 378 aa with a predicted mass of 42.8 kDa. ha100 encodes a protein of 510 aa with a predicted mass of 58.1 kDa and is a homologue of the gene for poly(ADP-ribose) glycohydrolase (parg). Western blot analysis and immunoelectron microscopy confirmed that HA44 is associated with the nucleocapsid and HA100 is associated with both the nucleocapsid and the envelope of HearNPV ODV. HA44 is conserved in group II NPVs and granuloviruses but does not exist in group I NPVs, while HA100 is conserved only in group II NPVs.

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Characterization and phylogenetic analysis of the chitinase gene from the Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus

Cited by 20 publications

References 43 publications

Evolution of Family 18 Glycoside Hydrolases: Diversity, Domain Structures and Phylogenetic Relationships

Evolution of Family 18 Glycoside Hydrolases: Diversity, Domain Structures and Phylogenetic Relationships

Chitinolytic functions in actinobacteria: ecology, enzymes, and evolution

Proteomics Analysis of Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus Identified Two New Occlusion-Derived Virus-Associated Proteins, HA44 and HA100

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