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Evolutionary and functional analysis of fructose bisphosphate aldolase of plant parasitic nematodes.

ABSTRACT: The essential and ubiquitous enzyme fructose bisphosphate aldolase (FBPA) has been a good target for controlling the various types of infections caused by pathogens and parasites. The parasitic infections of nematodes are the major concern of scientific community, leading to biochemical characterization of this enzyme. In this work we have developed a small dataset of all types of FBPA sequences collected from publically available databases (EMBL, NCBI and Uni-Port). The Phylogenetic study shows that evolutionary relationships among sequences of FBPA are clustered into three main groups. FBPA sequences of Globodera rostochiensis (FBPA_GR) and Heterodera glycines (FBPA_HG) are placed in group II, sharing the similar evolutionary relationship. The catalytic mechanism of these enzymes depends upon which class of aldolase, it belongs. The class of enzyme has been confirmed on the basis of sequences and structural similarity with template structure of class I FBPA. To confirm catalytic mechanism of above said model structures, the known substrate fructose-1, 6-bisphosphate (FBP) and competitive inhibitor Mannitol-1, 6 bisphosphate (MBP) were docked at known catalytic site of enzyme of interest. The comparative docking analysis shows that enzyme-substrate complex is forming similar Schiff base intermediate and conducts C(3)-C(4) bond cleavage by forming Hydrogen bonding with reaction catalyzing Glu-191, reactive Lys-150, and Schiff base forming Lys-233. On the other hand enzymeinhibitor noncovalent complex is forming cabinolamine precursor and the proton transfer by the formation of hydrogen bond between MBP O(2) with Glu191 enabling stabilization of cabinolamine transition state, which confirms the similar inhibition mechanism. Thus we conclude that Plant Parasitic Nematodes (PPNs) have evolutionary and functional relationship with the class I aldolase enzyme. Hence, FBPA can be targeted to control plant parasitic nematodes.

SUBMITTER: Prasad CS

PROVIDER: S-EPMC3563409 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Evolutionary and functional analysis of fructose bisphosphate aldolase of plant parasitic nematodes.

Prasad Cvs Siva CS Gupta Saurabh S Kumar Himansu H Tiwari Murlidhar M

Bioinformation 20130109 1

The essential and ubiquitous enzyme fructose bisphosphate aldolase (FBPA) has been a good target for controlling the various types of infections caused by pathogens and parasites. The parasitic infections of nematodes are the major concern of scientific community, leading to biochemical characterization of this enzyme. In this work we have developed a small dataset of all types of FBPA sequences collected from publically available databases (EMBL, NCBI and Uni-Port). The Phylogenetic study shows ...[more]

PMID: 23390337

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Project description:Diatoms and other chlorophyll-c containing, or chromalveolate, algae are among the most productive and diverse phytoplankton in the ocean. Evolutionarily, chlorophyll-c algae are linked through common, although not necessarily monophyletic, acquisition of plastid endosymbionts of red as well as most likely green algal origin. There is also strong evidence for a relatively high level of lineage-specific bacterial gene acquisition within chromalveolates. Therefore, analyses of gene content and derivation in chromalveolate taxa have indicated particularly diverse origins of their overall gene repertoire. As a single group of functionally related enzymes spanning two distinct gene families, fructose 1,6-bisphosphate aldolases (FBAs) illustrate the influence on core biochemical pathways of specific evolutionary associations among diatoms and other chromalveolates with various plastid-bearing and bacterial endosymbionts. Protein localization and activity, gene expression, and phylogenetic analyses indicate that the pennate diatom Phaeodactylum tricornutum contains five FBA genes with very little overall functional overlap. Three P. tricornutum FBAs, one class I and two class II, are plastid localized, and each appears to have a distinct evolutionary origin as well as function. Class I plastid FBA appears to have been acquired by chromalveolates from a red algal endosymbiont, whereas one copy of class II plastid FBA is likely to have originated from an ancient green algal endosymbiont. The other copy appears to be the result of a chromalveolate-specific gene duplication. Plastid FBA I and chromalveolate-specific class II plastid FBA are localized in the pyrenoid region of the chloroplast where they are associated with ?-carbonic anhydrase, which is known to play a significant role in regulation of the diatom carbon concentrating mechanism. The two pyrenoid-associated FBAs are distinguished by contrasting gene expression profiles under nutrient limiting compared with optimal CO2 fixation conditions, suggestive of a distinct specialized function for each. Cytosolically localized FBAs in P. tricornutum likely play a role in glycolysis and cytoskeleton function and seem to have originated from the stramenopile host cell and from diatom-specific bacterial gene transfer, respectively.

Project description:BackgroundDespite being important thermal dimorphic fungi causing Paracoccidioidomycosis, the pathogenic mechanisms that underlie the genus Paracoccidioides remain largely unknown. Microbial pathogens express molecules that can interact with human plasminogen, a protein from blood plasma, which presents fibrinolytic activity when activated into plasmin. Additionally, plasmin exhibits the ability of degrading extracellular matrix components, favoring the pathogen spread to deeper tissues. Previous work from our group demonstrated that Paracoccidioides presents enolase, as a protein able to bind and activate plasminogen, increasing the fibrinolytic activity of the pathogen, and the potential for adhesion and invasion of the fungus to host cells. By using proteomic analysis, we aimed to identify other proteins of Paracoccidioides with the ability of binding to plasminogen.ResultsIn the present study, we employed proteomic analysis of the secretome, in order to identify plasminogen-binding proteins of Paracoccidioides, Pb01. Fifteen proteins were present in the fungal secretome, presenting the ability to bind to plasminogen. Those proteins are probable targets of the fungus interaction with the host; thus, they could contribute to the invasiveness of the fungus. For validation tests, we selected the protein fructose 1,6-bisphosphate aldolase (FBA), described in other pathogens as a plasminogen-binding protein. The protein FBA at the fungus surface and the recombinant FBA (rFBA) bound human plasminogen and promoted its conversion to plasmin, potentially increasing the fibrinolytic capacity of the fungus, as demonstrated in fibrin degradation assays. The addition of rFBA or anti-rFBA antibodies was capable of reducing the interaction between macrophages and Paracoccidioides, possibly by blocking the binding sites for FBA. These data reveal the possible participation of the FBA in the processes of cell adhesion and tissue invasion/dissemination of Paracoccidioides.ConclusionsThese data indicate that Paracoccidioides is a pathogen that has several plasminogen-binding proteins that likely play important roles in pathogen-host interaction. In this context, FBA is a protein that might be involved somehow in the processes of invasion and spread of the fungus during infection.

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Evolutionary and functional analysis of fructose bisphosphate aldolase of plant parasitic nematodes.

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Evolutionary and functional analysis of fructose bisphosphate aldolase of plant parasitic nematodes.

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