scholarly journals In-Depth Glyco-Peptidomics Approach Reveals Unexpected Diversity of Glycosylated Peptides and Atypical Post-Translational Modifications in Dendroaspis angusticeps Snake Venom

2017 ◽  
Vol 18 (11) ◽  
pp. 2453 ◽  
Author(s):  
Michel Degueldre ◽  
Julien Echterbille ◽  
Nicolas Smargiasso ◽  
Christian Damblon ◽  
Charlotte Gouin ◽  
...  
Keyword(s):  
Snake Venom ◽  
Post Translational Modifications ◽  
Dendroaspis Angusticeps

Isolation and characterization of Fasciculin II: From Dendroaspis angusticeps snake venom and from chemical synthesis

Toxicon ◽  
2018 ◽  
Vol 149 ◽  
pp. 94-95 ◽  
Author(s):  
Doreen Palud ◽  
Aboudou Soioulata ◽  
Céline Haw ◽  
Laura Mugnier ◽  
Félicité Jarrosson ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Snake Venom ◽  
Dendroaspis Angusticeps ◽  
Isolation And Characterization

The effect of post-translational modifications on the hemorrhagic activity of snake venom metalloproteinases

2004 ◽  
Vol 138 (1) ◽  
pp. 23-32 ◽  
Author(s):  
L.T Garcı́a ◽  
L.T Parreiras e Silva ◽  
O.H.P Ramos ◽  
A.K Carmona ◽  
P.A Bersanetti ◽  
...  
Keyword(s):  
Snake Venom ◽  
Post Translational Modifications ◽  
Hemorrhagic Activity

scholarly journals Snake Venom Metalloproteinases

2016 ◽  
Vol 62 (1) ◽  
pp. 106-111 ◽  
Author(s):  
Şerban Andrei Gâz Florea ◽  
Adriana Gâz Florea ◽  
Hajnal Kelemen ◽  
Daniela-Lucia Muntean
Keyword(s):  
Snake Venom ◽  
Coagulation Factor ◽  
Short Review ◽  
Post Translational Modifications ◽  
Domain Structures ◽  
Factor Ii ◽  
Hemorrhagic Events ◽  
Switch Mechanism ◽  
Fibrinogenolytic Activity ◽  
Apoptotic Activity

AbstractAs more data are generated from proteome and transcriptome analysis revealing that metalloproteinases represent most of the Viperid and Colubrid venom components authors decided to describe in a short review a classification and some of the multiple activities of snake venom metalloproteinases. SVMPs are classified in three major classes (P-I, P-II and P-III classes) based on the presence of various domain structures and according to their domain organization. Furthermore, P-II and P-III classes were separated in subclasses based on distinctive post-translational modifications. SVMPs are synthesized in a latent form, being activated through a Cys-switch mechanism similar to matrix metalloproteinases. Most of the metalloproteinases of the snake venom are responsible for the hemorrhagic events but also have fibrinogenolytic activity, poses apoptotic activity, activate blood coagulation factor II and X, inhibit platelet aggregation, demonstrating that SVMPs have multiple functions in addition to well-known hemorrhagic function.

scholarly journals Enzymatic Activity And Brine Shrimp Lethality Of Venom From The Large Brown Spitting Cobra (Naja Ashei) And Its Neutralization By Antivenom

2020 ◽  
Author(s):  
Mitchel Otieno Okumu ◽  
James Mucunu Mbaria ◽  
Joseph Kangangi Gikunju ◽  
Paul Gichohi Mbuthia ◽  
Vincent Odongo Madadi ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Phospholipase A2 ◽  
Snake Venom ◽  
Brine Shrimp ◽  
Dendroaspis Angusticeps ◽  
Brine Shrimp Lethality ◽  
Brine Shrimp Lethality Assay ◽  
Comparison Results ◽  
Snake Venom Phospholipase ◽  
Naja Haje

Abstract Objective There has been little focus on the enzymatic and lethal activities of Naja ashei venom and their neutralization by antivenom. This study aimed to determine the snake venom phospholipase A2/svPLA2 activity and brine shrimp lethality of N. ashei venom and their neutralization by two antivenoms (I and II). The venom of other snakes in East Africa including the puff adder (Bitis arietans), green mamba (Dendroaspis angusticeps), black mamba (Dendroaspis polylepis), Egyptian cobra (Naja haje), red spitting cobra (Naja pallida), and the Eastern forest cobra (Naja subfulva) were used for comparison. Results: N. subfulva venom had the highest svPLA2 activity while D. angusticeps venom had the least activity. N. subfulva venom was the most toxic in the 24-hour brine shrimp lethality assay (BSLA), while N. ashei venom was the most toxic in the 48 and 72-hour assays. N. haje venom was the least toxic in all assays. One ml of antivenom I neutralized 0.075 µg of svPLA2 in N. ashei venom compared to 0.051 µg by antivenom II. Antivenom I was ineffective in neutralizing N .ashei venom-induced lethality but 1 ml of antivenom II neutralized 0.21 mg of N. ashei venom.

Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

2020 ◽  
Vol 477 (7) ◽  
pp. 1219-1225 ◽  
Author(s):  
Nikolai N. Sluchanko
Keyword(s):  
Protein Function ◽  
Intrinsically Disordered Protein ◽  
Structural Basis ◽  
Major Protein ◽  
Post Translational Modifications ◽  
Protein Protein Interaction ◽  
Intrinsically Disordered ◽  
Biochemical Journal ◽  
Multiple Binding ◽  
And Control

Many major protein–protein interaction networks are maintained by ‘hub’ proteins with multiple binding partners, where interactions are often facilitated by intrinsically disordered protein regions that undergo post-translational modifications, such as phosphorylation. Phosphorylation can directly affect protein function and control recognition by proteins that ‘read’ the phosphorylation code, re-wiring the interactome. The eukaryotic 14-3-3 proteins recognizing multiple phosphoproteins nicely exemplify these concepts. Although recent studies established the biochemical and structural basis for the interaction of the 14-3-3 dimers with several phosphorylated clients, understanding their assembly with partners phosphorylated at multiple sites represents a challenge. Suboptimal sequence context around the phosphorylated residue may reduce binding affinity, resulting in quantitative differences for distinct phosphorylation sites, making hierarchy and priority in their binding rather uncertain. Recently, Stevers et al. [Biochemical Journal (2017) 474: 1273–1287] undertook a remarkable attempt to untangle the mechanism of 14-3-3 dimer binding to leucine-rich repeat kinase 2 (LRRK2) that contains multiple candidate 14-3-3-binding sites and is mutated in Parkinson's disease. By using the protein-peptide binding approach, the authors systematically analyzed affinities for a set of LRRK2 phosphopeptides, alone or in combination, to a 14-3-3 protein and determined crystal structures for 14-3-3 complexes with selected phosphopeptides. This study addresses a long-standing question in the 14-3-3 biology, unearthing a range of important details that are relevant for understanding binding mechanisms of other polyvalent proteins.

Dicarbonyl derived post-translational modifications: chemistry bridging biology and aging-related disease

2020 ◽  
Vol 64 (1) ◽  
pp. 97-110
Author(s):  
Christian Sibbersen ◽  
Mogens Johannsen
Keyword(s):  
Mass Spectrometry ◽  
Future Research ◽  
Amino Acid Residues ◽  
Post Translational Modification ◽  
Dicarbonyl Compounds ◽  
Protein Targets ◽  
Post Translational Modifications ◽  
Reactive Protein ◽  
Glycation End Products ◽  
Direct Mass Spectrometry

Abstract In living systems, nucleophilic amino acid residues are prone to non-enzymatic post-translational modification by electrophiles. α-Dicarbonyl compounds are a special type of electrophiles that can react irreversibly with lysine, arginine, and cysteine residues via complex mechanisms to form post-translational modifications known as advanced glycation end-products (AGEs). Glyoxal, methylglyoxal, and 3-deoxyglucosone are the major endogenous dicarbonyls, with methylglyoxal being the most well-studied. There are several routes that lead to the formation of dicarbonyl compounds, most originating from glucose and glucose metabolism, such as the non-enzymatic decomposition of glycolytic intermediates and fructosyl amines. Although dicarbonyls are removed continuously mainly via the glyoxalase system, several conditions lead to an increase in dicarbonyl concentration and thereby AGE formation. AGEs have been implicated in diabetes and aging-related diseases, and for this reason the elucidation of their structure as well as protein targets is of great interest. Though the dicarbonyls and reactive protein side chains are of relatively simple nature, the structures of the adducts as well as their mechanism of formation are not that trivial. Furthermore, detection of sites of modification can be demanding and current best practices rely on either direct mass spectrometry or various methods of enrichment based on antibodies or click chemistry followed by mass spectrometry. Future research into the structure of these adducts and protein targets of dicarbonyl compounds may improve the understanding of how the mechanisms of diabetes and aging-related physiological damage occur.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

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