ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships

Cavada, Benildo S.; Pinto-Junior, Vanir Reis; Osterne, Vinicius Jose Da Silva; Nascimento, Kyria S.

doi:10.3390/ijms20010030

Cited by 51 publications

(40 citation statements)

References 136 publications

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“…It is well known the ability of ConA‐like lectins in recognize mannosides and derived glycoconjugates 22,23 . With CaBo, the results of lectin specificity studies confirm this main characteristic of this group.…”

Section: Resultssupporting

confidence: 52%

“…It is well known the ability of ConA-like lectins in recognize mannosides and derived glycoconjugates. 22,23 24 Thus, it seems that the lectin presents similar behavior as carrageenan. In respect to the lack of a second maximum at the lectin lower concentrations, it could mean that the lectin response is not only dose-dependent, but also time-dependent.…”

Section: Prediction Of Binding Specificity Of Cabomentioning

confidence: 96%

“…In the paw edema test, the α-methyl-mannoside reversal assay ( Figure 4C The results presented in this paper are consistent with those shown in other works described for ConA-like lectins, in particular those describing the proinflammatory effect of lectins isolated from the Diocleineae subtribe, as reported also for the lectins from Dioclea lasiophylla and Canavalia virosa. 23,34,35 Thus, it is notorious that, even working with a group of lectins of high structural similarity and of the same specificity, the results of biological activity vary in terms of the potency of the biological effect, which justifies all the more acute tests regarding the fine specificity of these proteins.…”

Section: Relationship Between In Silico Analysis and Biological Actmentioning

confidence: 99%

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Exploring the carbohydrate‐binding ability of Canavalia bonariensis lectin in inflammation models

Cavada

Silva

Osterne

et al. 2020

J of Molecular Recognition

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Lectins are a group of proteins of non-immune origin recognized for their ability to bind reversibly to carbohydrates. Researchers have been intrigued by oligosaccharides and glycoconjugates for their involvement as mediators of complex cellular events and then many biotechnological applications of lectins are based on glycocode decoding and their activities. Here, we report a structural and biological study of a ConA-like mannose/glucose-specific lectin from Canavalia bonariensis seeds, CaBo. More specifically, we evaluate the binding of CaBo with α-methyl-D-mannoside (MMA) and mannose-1,3-α-D-mannose (M13) and the resultant in vivo effects on a rat model of acute inflammation. A virtual screening was also carried out to cover a larger number of possible bindings of CaBo. In silico analysis demonstrated the stability of CaBo interaction with mannose-type ligands, and the lectin was able to induce acute inflammation in rats with the participation of the carbohydrate recognition domain (CRD) and histamine release. These results confirm the ability of CaBo to interact with hybrid and high-mannose N-glycans, supporting the hypothesis that CaBo's biological activity occurs primarily through its interaction with cell surface glycosylated receptors.

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Section: Resultssupporting

confidence: 52%

Section: Prediction Of Binding Specificity Of Cabomentioning

confidence: 96%

Section: Relationship Between In Silico Analysis and Biological Actmentioning

confidence: 99%

See 1 more Smart Citation

Exploring the carbohydrate‐binding ability of Canavalia bonariensis lectin in inflammation models

Cavada

Silva

Osterne

et al. 2020

J of Molecular Recognition

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“…Carbohydrate moieties of glycoproteins act as mediators for interactions between host cell membrane and the virus fusion and take part in the viral infections. Lectin-dependent therapy, based on protein-carbohydrate interactions, can be used as a substitute to effectively tackle microbial diseases in the future [143][144][145][146][147][148][149][150].…”

Section: Viral Glycoproteins As Targets For Plant Lectinsmentioning

confidence: 99%

Status of mannose-binding lectin (MBL) and complement system in COVID-19 patients and therapeutic applications of antiviral plant MBLs

Gupta

2021

Mol Cell Biochem

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Coronavirus disease 2019 (COVID-19) is an infectious disease caused by a virus called "Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2)." In the majority of patients, infection with COVID-19 may be asymptomatic or may cause only mild symptoms. However, in some patients, there can also be immunological problems, such as macrophage activation syndrome (CSS) that results in cytokine storm syndrome (CSS) and acute respiratory distress syndrome (ARDS). Comprehension of host-microbe communications is the critical aspect in the advancement of new therapeutics against infectious illnesses. Endogenous animal lectins, a class of proteins, may perceive non-self glycans found on microorganisms. Serum mannose-binding lectin (sMBL), as a part of the innate immune framework, recognizes a wide range of microbial microorganisms and activates complement cascade via an antibody-independent pathway. Although the molecular basis for the intensity of SARS-CoV-2 infection is not generally understood, scientific literature indicates that COVID-19 is correlated with unregulated activation of the complement in terms of disease severity. Disseminated intravascular coagulation (DIC), inflammation, and immune paralysis contribute to unregulated complement activation. Pre-existing genetic defects in MBL and their association with complement play a major role in immune response dysregulation caused by SARS-CoV-2. In order to generate anti-complement-based therapies in Covid-19, an understanding of sMBL in immune response to SARS-CoV-2 and complement is therefore essential. This review highlights the role of endogenous sMBL and complement activation during SARS-CoV-2 infection and their therapeutic management by various agents, mainly plant lectins, since antiviral mannose-binding plant lectins (pMBLs) offer potential applications in the prevention and control of viral infections.

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“…Many more examples of circularly permuted proteins have since been discovered, but all of these natural examples, like the artificial circular permutations, are made at the genetic level. ConA and the closely-related conA-like lectins in the Diocleinae subtribe of plants remain the only proteins observed to undergo post-translational circular permutation (Cavada et al, 2018). The functional purpose for conA circular permutation remains elusive as few biochemical studies have been performed with purified pro-conA.…”

Section: Introductionmentioning

confidence: 99%

Structural basis for a natural circular permutation in proteins

Nonis

Haywood

et al. 2020

Preprint

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Over 30 years ago, an intriguing post-translational modification was discovered to be responsible for creating concanavalin A (conA), a carbohydrate-binding protein found in the seeds of jack bean (Canavalia ensiformis) and commercially used for carbohydrate chromatography. Biosynthesis of conA involves what was then an unprecedented rearrangement in amino acid sequence, whereby the N-terminal half of the gene-encoded conA precursor is swapped to become the C-terminal half of conA. The cysteine protease, asparaginyl endopeptidase (AEP), was shown to be involved, but its mechanism was not fully elucidated. To understand the structural basis and consequences of conA circular permutation, we generated a recombinant jack bean conA precursor (pro-conA) plus jack bean AEP (CeAEP1) and solved crystal structures for each to 2.1 Å and 2.7 Å respectively. By reconstituting the biosynthesis of conA in vitro, we prove CeAEP1 alone can perform both the cleavage and cleavage-coupled transpeptidation to form conA. CeAEP1 structural analysis reveals how it is capable of carrying out both these reactions. Biophysical assays illustrated that conA is more thermally and pH stable than pro-conA, consistent with fewer intermolecular interactions between subunits in the pro-conA crystal structure. These findings elucidate the consequences of circular permutation in the only post-translation example known to occur in nature.

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ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships

Cited by 51 publications

References 136 publications

Exploring the carbohydrate‐binding ability of Canavalia bonariensis lectin in inflammation models

Exploring the carbohydrate‐binding ability of Canavalia bonariensis lectin in inflammation models

Status of mannose-binding lectin (MBL) and complement system in COVID-19 patients and therapeutic applications of antiviral plant MBLs

Structural basis for a natural circular permutation in proteins

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