Antimicrobial Factors in Earthworms

Department of Cell BiologyKatedra buněčné biologiePřírodovědecká fakultaFaculty of Scienc

Antimicrobial Factors in Earthworms

Department of Cell BiologyKatedra buněčné biologiePřírodovědecká fakultaFaculty of Scienc

CRM and its Importance for Business Competitiveness

This paper deals with the Customer Relationship Management (CRM) system with emphasis on the importance for the competitiveness of a business. The aim of the present article is to seek whether a business pursues customer value on a regular basis regardless of its size. Monitoring customer value can thus be one of the criteria that measure the success of implementing an overall customer relationship management concept in a particular business. CRM system is also used in agribusiness

Effect of experimental microbial challenge on the expression of defense molecules in Eisenia foetida earthworm

Earthworms are able to protect themselves against invading pathogens due to efficient innate defense mechanisms. Currently, two types of antimicrobial factors including lysozyme-like molecule and factors with hemolytic activity, as well as a pattern recognition protein named coelomic cytolytic factor (CCF) have been identified in Eisenia foetida earthworms. However, the modulations of these defense molecules during in vivo immune response have not been addressed. In this study, we investigated the effect of experimental challenge with live Gram-negative and Gram-positive bacteria and with β-1,3-glucan on the expression of CCF and the hemolytic factor fetidin. In parallel, we followed levels of hemolytic activity and lysozyme-like activity in the coelomic fluid of challenged earthworms. We show that the biosynthesis of CCF, but not fetidin, is up-regulated upon microbial stimulation. Parenteral administration of bacteria or microbial polysaccharides in earthworms results, in the coelomic fluid, in augmented level of CCF, increased lysozyme-like activity and decreased hemolytic activity. The decreased hemolytic activity of the coelomic fluid reflects the increase of the whole protein content in the absence of synthesis of hemolytic proteins. © 2004 Elsevier Ltd. All rights reserved.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

The Digital Economy in the Context of Digital Transformation and Their Impact on the Electronification of Accounting Processes in the Slovak Republic

As a result of the explosive growth of scientific knowledge and the rapid development of ICT, the world economy is undergoing crucial global changes, which are the most significant since the industrial revolution. Digitization represents the most important element of the fourth industrial revolution, enabling the connection of technology and people. The digital economy is related to the rapid onset and penetration of information and communication technologies into all areas of human activity, which also requires new perspectives on the factors affecting the development and success of the economy. We digitize information and data, digitize the processes and systems that make up the functioning of the company, and digitally transform the company and its strategy. The main task of article is to determine the digital economy in the context of digital transformation and their impact on the electronification of accounting processes in the Slovak Republic. The article defines the progress and level of development of Europe's digital competitiveness in individual EU member states using the Digital Economy and Society Index (DESI). The position of Slovakia and the EU is compared for the period from 2018 to 2022. Slovakia needs to create conditions for the gradual digital transformation of all sectors of the economy. Digitization is also coming to the accounting. The article also describes how the approved amendment to the Act on Accounting as of January 1, 2022 creates space for streamlining the processing and archiving of accounting records. The current change in the amendment to the Act on Accounting thus offers completely new opportunities for working with corporate accounting in relation to internal processes in the company, but also in relation to financial administration or tax authorities. All entities, this also applies to agricultural entities keeping the double entry accounting, are obliged to follow the Act No. 431/2002 Coll. on Accounting as amended

Involvement of the iron regulatory protein from Eisenia andrei earthworms in the regulation of cellular iron homeostasis.

Iron homeostasis in cells is regulated by iron regulatory proteins (IRPs) that exist in different organisms. IRPs are cytosolic proteins that bind to iron-responsive elements (IREs) of the 5'- or 3'-untranslated regions (UTR) of mRNAs that encode many proteins involved in iron metabolism. In this study, we have cloned and described a new regulatory protein belonging to the family of IRPs from the earthworm Eisenia andrei (EaIRP). The earthworm IRE site in 5'-UTR of ferritin mRNA most likely folds into a secondary structure that differs from the conventional IRE structures of ferritin due to the absence of a typically unpaired cytosine that participates in protein binding. Prepared recombinant EaIRP and proteins from mammalian liver extracts are able to bind both mammalian and Eisenia IRE structures of ferritin mRNA, although the affinity of the rEaIRP/Eisenia IRE structure is rather low. This result suggests the possible contribution of a conventional IRE structure. When IRP is supplemented with a Fe-S cluster, it can function as a cytosolic aconitase. Cellular cytosolic and mitochondrial fractions, as well as recombinant EaIRP, exhibit aconitase activity that can be abolished by the action of oxygen radicals. The highest expression of EaIRP was detected in parts of the digestive tract. We can assume that earthworms may possess an IRE/IRP regulatory network as a potential mechanism for maintaining cellular iron homeostasis, although the aconitase function of EaIRP is most likely more relevant

Comparative study of the CCF-like pattern recognition protein in different Lumbricid species

Coelomic fluid of the Lumbricid Eisenia fetida contains a 42-kDa pattern recognition protein named coelomic cytolytic factor (CCF) that binds microbial cell wall components and triggers the activation of the prophenoloxidase cascade, an important invertebrate defense pathway. Here we report on the sequence characterization of CCF-like molecules of other Lumbricids: Aporrectodea caliginosa, Aporrectodea icterica, Aporrectodea longa, Aporrectodea rosea, Dendrobaena veneta, Lumbricus rubellus and Lumbricus terrestris, and show that CCF from E. fetida has a broader saccharide-binding specificity, being the only one recognizing N,N′-diacetylchitobiose. We suggest that the broad recognition repertoire of E. fetida CCF reflects a particular microbial environment this species lives in. © 2005 Elsevier Ltd. All rights reserved.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Coomassie staining of SDS-PAGE of <i>E. coli</i> lysate proteins transformed with pRSET B-<i>EaIRP</i> and purified rEaIRP.

<p>Lanes: M – MW markers, a - transformed <i>E. coli</i> BL21, b - transformed <i>E. coli</i> BL21 induced with 1 mM IPTG, c – purified rEaIRP, d- purified rEaIRP reduced with 1 mM 2-mercaptoethanol.</p

The expression of <i>Ea</i>IRP in different tissues.

<p>The expression of <i>EaIRP</i> in coelomocytes and different tissues was normalized to two different housekeeping genes: RPL13, RPL17. <i>EaIRP</i> was constitutively expressed in coelomocytes and in all tested tissues (EP – epidermis, CS – coelomocytes, SV – seminal vesicles, PH – pharynx, ES – esophagus, CR – crop, GZ – gizzard, INT – intestine). The expression was related to the expression in the epidermis, where the expression of <i>Ea</i>IRP was the lowest. The highest level of <i>EaIRP</i> expression was found in the part of the digestive tract that included the crop, gizzard and intestine. One-way ANOVA with Dunnett’s post-test was performed, using GraphPad Prism software to evaluate the significance of the data. Differences were considered significant when P<0.05, 0.001.</p

Amino acid sequence alignments of for various IRPs.

<p>The alignment of the predicted amino acid sequence of <i>E. andrei</i> IRP with <i>H. sapiens</i> IRP-1, <i>D. rerio</i> IRP-1, <i>A. thaliana</i> aconitase, <i>P. falciparum</i> IRP-like protein, <i>D. melanogaster</i> IRP-1A, <i>P. leniusculus</i> IRP-1-like protein and <i>C. elegans</i> aconitase-1 using the ClustalW multiple sequence alignment program. Putative conserved domains and binding sites were detected by NCBI-CDD. Two conserved domains of IRP are in gray: (Arg84-Val568: Aconitase catalytic domain, Asn672-Ile839: Aconitase swivel domain). The aconitase catalytic domain includes a ligand binding site that binds to the Fe-S cluster required for the activity. The aconitase swivel domain includes a substrate binding site with residues participating in the active site of the catalytic domain. Asterisks show homology in amino acids in all aligned proteins. Black arrows (▾) indicate three cysteine residues binding the Fe-S cluster. Further ligand binding sites are indicated by white arrows (Δ). Putative amino acid residues involved in RNA binding are underlined (based on NCBI-CDD prediction or from the comparison with human IRP1). The square (▪) shows the position of a serine that can be phosphorylated.</p