<i>Xylella fastidiosa</i> Esterase Rather than Hydroxynitrile Lyase

Torrelo, Guzmán; Souza, Fayene Zeferino Ribeiro de; Carrilho, Emanuel; Hanefeld, Ulf

doi:10.1002/cbic.201402685

Cited by 6 publications

(8 citation statements)

References 79 publications

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“…This CDS is encoded in pXF39-Fb7 but was not present in pXF27-like plasmids, pXF39_Pr8x and pXF64_HB. pXFa0032 has been shown to present esterase activity in vitro (Torrelo et al 2015) and might confer some advantage for citrus strains.…”

Section: Pxf51-like Plasmidsmentioning

confidence: 99%

Genetic Diversity of Xylella fastidiosa Plasmids Assessed by Comparative Genomics

Pierry

Uceda-Campos

Feitosa-Junior

et al. 2020

Trop. plant pathol.

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Plasmids are a major source of horizontal gene transfer among bacteria contributing to their evolution and ecology. The known collection of plasmids carried by the plant pathogen Xylella fastidiosa increases as new strains from different origins and hosts are sampled and sequenced. Here we performed an extensive comparison of 61 publicly available sequences annotated as plasmids belonging to 38 X. fastidiosa strains isolated from different plant species and distinct geographical locations. Twenty-six strains exhibited at least one plasmid and up to four plasmids were found in a single strain. Plasmids sizes varied widely from 1.3 kbp to 64.3 kbp, ranging from 1 to 70 protein-coding sequences (CDS) encompassing 324 orthologs. Based on the presence of specific mobility proteins such as relaxases and type 4 secretion system-related genes, respectively 40 and 8 of the X. fastidiosa plasmids were classified as conjugative and mobilizable, while 13 were classified as non-mobilizable. X. fastidiosa plasmids did not carry known antibiotic resistance or virulence genes, and their stability seems to take advantage of toxin/antitoxin systems. The comparative analyses described here revealed similarity among plasmids of X. fastidiosa from different subspecies, geographical regions, and hosts, as well as with sequences found in plasmids from other bacterial species. Altogether, our results provide an in silico analysis of X. fastidiosa plasmid content and their main features, with applications in future studies of epidemiology, ecology, and evolution of this phytopathogen.

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Section: Pxf51-like Plasmidsmentioning

confidence: 99%

Genetic Diversity of Xylella fastidiosa Plasmids Assessed by Comparative Genomics

Pierry

Uceda-Campos

Feitosa-Junior

et al. 2020

Trop. plant pathol.

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“…Viral protein synthesis initiated at two distinct sites from artificial fusion genes is independent of the cap-binding eIF4F complex in the presence of IRES [ 29 ]. Furthermore, the cleavage products of eIF4GI (C-terminal portion) stimulate the translation of uncapped RNAs and those carrying IRESs [ 49 ]. The interaction of the two eIF4G proteins with IRES is an essential event for promoting IRES activity.…”

Section: Cleavage Of Host Proteins Induced By L Promentioning

confidence: 99%

Multifunctional roles of leader protein of foot-and-mouth disease viruses in suppressing host antiviral responses

Liu

Zhu

Zhang

et al. 2015

Vet Res

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Foot-and-mouth disease virus (FMDV) leader protein (Lpro) is a papain-like proteinase, which plays an important role in FMDV pathogenesis. Lpro exists as two forms, Lab and Lb, due to translation being initiated from two different start codons separated by 84 nucleotides. Lpro self-cleaves from the nascent viral polyprotein precursor as the first mature viral protein. In addition to its role as a viral proteinase, Lpro also has the ability to antagonize host antiviral effects. To promote FMDV replication, Lpro can suppress host antiviral responses by three different mechanisms: (1) cleavage of eukaryotic translation initiation factor 4 γ (eIF4G) to shut off host protein synthesis; (2) inhibition of host innate immune responses through restriction of interferon-α/β production; and (3) Lpro can also act as a deubiquitinase and catalyze deubiquitination of innate immune signaling molecules. In the light of recent functional and biochemical findings regarding Lpro, this review introduces the basic properties of Lpro and the mechanisms by which it antagonizes host antiviral responses.

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“…Tm 1459 and Tm 1459-C106L yielded rac- 2a (31 ± 0.17 and 43 ± 0.14%, respectively) after 24 h of reaction time. As the chemical background reaction is known to lead to misassignments of HNL activity, blank reactions were performed . In this case, the reaction with just the enzyme carrier but without enzyme yielded rac - 2a (23 ± 0.33%).…”

Section: Resultsmentioning

confidence: 99%

Can a Hydroxynitrile Lyase Catalyze an Oxidative Cleavage?

et al. 2023

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Granulicella tundricola hydroxynitrile lyase (GtHNL) is a manganese dependent cupin that catalyzes the enantioselective synthesis of cyanohydrins. The analysis of its active site shows high similarity with the active site of cupin Tm1459 from Thermotoga maritima, an enzyme that catalyzes the oxidative cleavage of styrene derivatives. GtHNL (GtHNL-WT) was found to catalyze the oxidative cleavage of α-methyl styrene, too. The conversion of α-methyl styrene yielded 23.6 ± 0.8% of acetophenone after 20 h. On the other hand, Tm1459 was not able to catalyze the synthesis of cyanohydrins efficiently. A low yield of rac-mandelonitrile was obtained from benzaldehyde and HCN using either Tm1459-WT or Tm1459-C106L, a variant more active in oxidative catalysis. On the basis of the molecular analysis of GtHNL and Tm1459 active sites, the variants GtHNL-H96A, GtHNL-H96F, and GtHNL-A40H/V42T/H96A/Q110H were produced and evaluated for improved catalytic activity toward oxidative cleavage of styrenes. The amino acid substitution H96A liberates an additional manganese coordination position and enlarges the GtHNL-WT active site cavity. Similarly, the amino acid substitution H96F liberates a coordination site as described for the GtHNL-H96A variant but without enlarging the active site space. All variants were able to catalyze the oxidative cleavage of styrene derivatives. The best results were observed using GtHNL-H96A as catalyst. It displayed a higher yield of acetophenone (42%) as compared to GtHNL-A40H/V42T/H96A/Q110H (12%) and GtHNL-H96F (11%) after 20 h of reaction time. No oxidation of Mn(II) to Mn(III) could be detected by electron paramagnetic resonance (EPR), whereas evidence for a radical mechanism is presented. Control reactions using 0.1 and 0.5 mM of MnCl 2 in the absence of enzyme showed no significant oxidation reaction.

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Xylella fastidiosa Esterase Rather than Hydroxynitrile Lyase

Cited by 6 publications

References 79 publications

Genetic Diversity of Xylella fastidiosa Plasmids Assessed by Comparative Genomics

Genetic Diversity of Xylella fastidiosa Plasmids Assessed by Comparative Genomics

Multifunctional roles of leader protein of foot-and-mouth disease viruses in suppressing host antiviral responses

Can a Hydroxynitrile Lyase Catalyze an Oxidative Cleavage?

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