Structural constraints-based evaluation of immunogenic avirulent toxins from Clostridium botulinum C2 and C3 toxins as subunit vaccines

Prisilla, A.; Prathiviraj, R.; Sasikala, R.; Chellapandi, P.

doi:10.1016/j.meegid.2016.06.029

Cited by 12 publications

(5 citation statements)

References 94 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A protein's biophysical properties, such as folding, stability, and functions, are drastically altered by amino acid substitution ( Gromiha et al 2009 ; Prathiviraj et al, 2016 ). Hence, the fluctuation in protein folding leads to replication and multiplication of SARS-CoV-2 in the new environmental niche ( Prisilla et al, 2016 ; Prathiviraj et al, 2016 ; Prathiviraj et al, 2021 ).…”

Section: Discussionmentioning

confidence: 99%

“…The protein folding information plays a key role in the therapeutic intervention of many viral diseases ( Broglia et al 2005 ; Prathiviraj et al, 2021 ). The folding process of a protein determines the structural stability and drug binding specificity ( Prisilla et al, 2016 ; Prathiviraj et al, 2016 ) thus it's most important to identify the folding rate of mutants ( Murugan et al, 2019 ; Prathiviraj et al, 2021 ). Analysis of the genotype and phenotype is essential as it aids in understanding the missense, synonymous, and non-synonymous mutations in the virus.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of genotypic variants and its proteomic mutations of Brazilian SARS-CoV-2 isolates

et al. 2022

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Identification of genotypic variants and its proteomic mutations of Brazilian SARS-CoV-2 isolates

et al. 2022

View full text Add to dashboard Cite

“…The protein folding information plays a key role in the therapeutic intervention of many viral diseases (Broglia et al 2005;Prathiviraj et al, 2021). The folding process of a protein determines the structural stability and drug binding specificity (Prisilla et al, 2016;Prathiviraj et al, 2016) thus it's most important to identify the folding rate of mutants (Murugan et al, 2019;Prathiviraj et al, 2021). The protein folding rate among all the identified mutants was calculated using the FOLD-RATE server (Gromiha et al, 2006).…”

Section: Prediction Of Virulence Mechanism and Protein Folding Ratementioning

confidence: 99%

“…And slow fold rate was identified in other classes (All-α, α+β:α/β and unknown ). Hence, the fluctuation in protein folding leads to replication and multiplication of SARS-CoV-2 in the new environmental niche (Prisilla et al, 2016;Prathiviraj et al, 2016;Prathiviraj et al, 2021).…”

Section: Analysis Of Virulence Mechanism and Protein Folding Statementioning

confidence: 99%

Identification of Genotypic Variants and its Proteomic mutations of Brazilian SARS-CoV-2 Isolates

Prathiviraj

Chellapandi

Kiran

et al. 2021

Preprint

View full text Add to dashboard Cite

The second wave of COVID-19, which is caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), is rapidly spreading over the world. The mechanism behind the escaping from current antivirals is still not clear, due to the occurrence of continuous variants in SARS-CoV-2 genomes. Brazil is the world’s second most COVID-19-affected country. In the present study, we identified the genomic and proteomic variants of Brazilian SARS-CoV-2 isolates. We identified 16 different genotypic variants were found among the 27 isolates. The genotypes of three isolates such as Bra/1236/2021 (G15), Bra/MASP2C844R2/2020 (G11), and Bra/RJ-DCVN5/2020 (G9) have a unique mutant in NSP4 (S184N), 2’O-Mutase (R216N), membrane protein (A2V) and Envelope protein (V5A). A mutation in RdRp of SARS-CoV-2, particularly the change of Pro to Leu at 323 resulted in the stabilization of the structure in BRA/CD1739-P4/2020. NSP4, NSP5 protein mutants are more virulent in Genotype 15 and 16. A fast protein folding rate changes the structural stability and leads to escape for current antivirals. Thus, our findings help researchers to develop the best potent antivirals based on the new mutant of Brazilian isolates.

show abstract

“…Several evolutionary constraints have been identified from the structures and functions of some virulence proteins or protein families (Chellapandi et al 2013(Chellapandi et al , 2018(Chellapandi et al , 2019Prathiviraj et al 2016;Prisilla et al 2016;. A common functional core is conserved and substantially established across unassigned peptidases of microbial pathogens by evolutionary pressure (Barrett and Rawlings 2007).…”

Section: Introductionmentioning

confidence: 99%

Evolutionary genetic analysis of unassigned peptidase clan-associated microbial virulence and pathogenesis

Prathiviraj

Chellapandi

2020

Biologia

Self Cite

View full text Add to dashboard Cite

Peptidase clan is the largest group of proteases with common ancestry as identified by structural homology. A peptidase with unknown catalytic type is referred to as an unassigned peptidase clan, which can be classified into 8 peptidase families (U32, U40, U49, U56, U57, U62, U69, and U72). The members of this clan are widely dispersed in diverse microbial pathogens and their apparent involvement in the microbial virulence is not yet known for antibiotic drug discovery. In the present study, we have analyzed their common structural and functional characteristics using evolutionary genetic analysis. As shown by our analysis, the molecular and functional characteristics of this clan diverged across the microbial pathogens. It also indicates that the members of each family might have evolved independently and a peptidase core converged to interconnect the unassigned peptidase clan. Several evolutionary constraints have been identified as selective measures from this clan that inferred on their functional evolution and divergence. Genetic diversity analysis described that many members of this clan have evolved as new molecular functions across the microbial pathogens by imposing the Darwinian positive selection. Structural analysis of this study indicates that members of this clan have a conserved fold, convergence in functional parts, and divergence in spatial structural arrangements. As the results of our study, the neofunctionalization of several unassigned peptidases provides a full virulence for microbial pathogens occupying at the different pathophysiological niche.

show abstract

Structural constraints-based evaluation of immunogenic avirulent toxins from Clostridium botulinum C2 and C3 toxins as subunit vaccines

Cited by 12 publications

References 94 publications

Identification of genotypic variants and its proteomic mutations of Brazilian SARS-CoV-2 isolates

Identification of genotypic variants and its proteomic mutations of Brazilian SARS-CoV-2 isolates

Identification of Genotypic Variants and its Proteomic mutations of Brazilian SARS-CoV-2 Isolates

Evolutionary genetic analysis of unassigned peptidase clan-associated microbial virulence and pathogenesis

Contact Info

Product

Resources

About