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Article ; Online: Aggregation hot spots in the SARS-CoV-2 proteome may constitute potential therapeutic targets for the suppression of the viral replication and multiplication.

Gour, Shalini / Yadav, Jay Kant

2021 Volume 12, Issue 1, Page(s) 1–13

Abstract: The emergence of novel coronavirus SARS-CoV-2 is responsible for causing coronavirus disease-19 (COVID-19) imposing serious threat to global public health. Infection of SARS-CoV-2 to the host cell is characterized by direct translation of positive single ...

Abstract	The emergence of novel coronavirus SARS-CoV-2 is responsible for causing coronavirus disease-19 (COVID-19) imposing serious threat to global public health. Infection of SARS-CoV-2 to the host cell is characterized by direct translation of positive single stranded (+ ss) RNA to form large polyprotein polymerase 1ab (pp1ab), which acts as precursor for a number of nonstructural and structural proteins that play vital roles in replication of viral genome and biosynthesis of new virus particles. The maintenance of viral protein homeostasis is essential for continuation of viral life cycle in the host cell. To test whether the protein homeostasis of SARS-CoV-2 can be disrupted by inducing specific protein aggregation, we made an effort to examine whether the viral proteome contains any aggregation prone regions (APRs) that can be explored for inducing toxic protein aggregation specifically in viral proteins and without affecting the host cell. This curiosity leads to the identification of several (> 70) potential APRs in SARS-CoV-2 proteome. The length of the APRs ranges from 5 to 25 amino acid residues. Nearly 70% of total APRs investigated are relatively smaller and found to be in the range of 5-10 amino acids. The maximum number of ARPs (> 50) was observed in pp1ab. On the other hand, the structural proteins such as, spike (S), nucleoprotein (N), membrane (M) and envelope (E) proteins also possess APRs in their primary structures which altogether constitute 30% of the total APRs identified. Our findings may provide new windows of opportunities to design specific peptide-based, anti-SARS-CoV-2 therapeutic molecules against COVID-19.
Language	English
Publishing date	2021-02-13
Publishing country	Singapore
Document type	Journal Article
ZDB-ID	2890453-9
ISSN	2524-4663 ; 0975-8151
ISSN (online)	2524-4663
ISSN	0975-8151
DOI	10.1007/s42485-021-00057-y
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Article ; Online: Co-morbidities and Complications in COVID-19 Recovered Patients in Bhilwara District, Rajasthan, India

Mahesh Kumar Choudary / Shalini Jain / Surendra Meena / Daulat Meena / Arun Gour / Shalabh Sharma

Journal of Clinical and Diagnostic Research, Vol 16, Iss 3, Pp LC33-LC

A Descriptive Study

2022 Volume 36

Abstract: Introduction: Coronavirus Disease-19 (COVID-19) infection is associated with high rates of pulmonary and extrapulmonary complications that may continue to incur morbidity, disability and delayed mortality in survivors. These include hyperglycaemia, ... ...

Abstract	Introduction: Coronavirus Disease-19 (COVID-19) infection is associated with high rates of pulmonary and extrapulmonary complications that may continue to incur morbidity, disability and delayed mortality in survivors. These include hyperglycaemia, cardiac injury, acute ischaemic or haemorrhagic stroke, neurological deficits, acute kidney injury and liver injury. Aim: To describe symptoms and complications being faced by COVID-19 recovered patients, as well their socio-demographic profile and co-morbidities. Materials and Methods: This was a cross-sectional descriptive study conducted for the period of 12 months from April 2020 to March 2021. Out of nearly 10,000 recovered COVID-19 patients, 1000 patients were selected randomly. The patients were categorised gender-wise (male and female) and locality-wise (urban and rural) and an attempt was made to find if any significant difference exists in the symptoms and complications based on above categorisation. The test used for this purpose was Chi-square test and Fisher’s-exact test. Results: Mean age of participants was 50.2±15.7 years and 43.8% had co-morbidities. Common complications included hyperglycaemia (n=28), acute kidney injury (n=8), acute liver injury (n=5), cardiovascular accident and stroke (n=5), septicaemia (n=8), ischaemic heart disease (n=7), deep vein thrombosis (n=2), cytokine release syndrome (n=10) and post COVID-19 fibrosis (n=3). For septicaemia, a statistically significant difference (p<0.001) was found between urban and rural areas whereas no significant difference in post COVID-19 complications between males and females was observed. Conclusion: The most common co-morbidity was diabetes mellitus and most common complication reported was hyperglycaemia.
Keywords	coronavirus disease-19 ; diabetes ; hypertension ; post covid fibrosis ; septicaemia ; Medicine ; R
Subject code	610
Language	English
Publishing date	2022-03-01T00:00:00Z
Publisher	JCDR Research and Publications Private Limited
Document type	Article ; Online
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Article ; Online: Microalgae mediated bioremediation of polycyclic aromatic hydrocarbons: Strategies, advancement and regulations.

Satpati, Gour Gopal / Gupta, Shalini / Biswas, Rohan Kr / Choudhury, Avik Kumar / Kim, Jung-Wan / Davoodbasha, MubarakAli

Chemosphere

2023 Volume 344, Page(s) 140337

Abstract: Polycyclic aromatic hydrocarbons (PAHs) are pervasive in the atmosphere and are one of the emerging pollutants that cause harmful effects in living systems. There are some natural and anthropogenic sources that can produce PAHs in an uncontrolled way. ... ...

Abstract	Polycyclic aromatic hydrocarbons (PAHs) are pervasive in the atmosphere and are one of the emerging pollutants that cause harmful effects in living systems. There are some natural and anthropogenic sources that can produce PAHs in an uncontrolled way. Several health hazards associated with PAHs like abnormality in the reproductive system, endocrine system as well as immune system have been explained. The mutagenic or carcinogenic effects of hydrocarbons in living systems including algae, vertebrates and invertebrates have been discussed. For controlling PAHs, biodegradation has been suggested as an effective and eco-friendly process. Microalgae-based biosorption and biodegradation resulted in the removal of toxic contaminants. Microalgae both in unialgal form and in consortium (with bacteria or fungi) performed good results in bioaccumulation and biodegradation. In the present review, we highlighted the general information about the PAHs, conventional versus advanced technology for removal. In addition microalgae based removal and toxicity is discussed. Furthermore this work provides an idea on modern scientific applications like genetic and metabolic engineering, nanomaterials-based technologies, artificial neural network (ANN), machine learning (ML) etc. As rapid and effective methods for bioremediation of PAHs. With several pros and cons, biological treatments using microalgae are found to be better for PAH removal than any other conventional technologies.
MeSH term(s)	Animals ; Biodegradation, Environmental ; Microalgae/metabolism ; Polycyclic Aromatic Hydrocarbons/analysis ; Environmental Pollutants/analysis ; Bacteria/metabolism
Chemical Substances	Polycyclic Aromatic Hydrocarbons ; Environmental Pollutants
Language	English
Publishing date	2023-10-03
Publishing country	England
Document type	Review ; Journal Article
ZDB-ID	120089-6
ISSN	1879-1298 ; 0045-6535 ; 0366-7111
ISSN (online)	1879-1298
ISSN	0045-6535 ; 0366-7111
DOI	10.1016/j.chemosphere.2023.140337
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Article ; Online: Pheromone peptide cOB1 from native Enterococcus faecalis forms amyloid-like structures: A new paradigm for peptide pheromones.

Gour, Shalini / Kumar, Vijay / Rana, Monika / Yadav, Jay Kant

Journal of peptide science : an official publication of the European Peptide Society

2019 Volume 25, Issue 8, Page(s) e3178

Abstract: Pheromone peptides are an important component of bacterial quorum-sensing system. The pheromone peptide cOB1 (VAVLVLGA) of native commensal Enterococcus faecalis has also been identified as an antimicrobial peptide (AMP) and reported to kill the ... ...

Abstract	Pheromone peptides are an important component of bacterial quorum-sensing system. The pheromone peptide cOB1 (VAVLVLGA) of native commensal Enterococcus faecalis has also been identified as an antimicrobial peptide (AMP) and reported to kill the prototype clinical isolate strain of E. faecalis V583. In this study, the pheromone peptide cOB1 has shown to form amyloid-like structures, a characteristic which is never reported for a pheromone peptide so far. With in silico analysis, the peptide was predicted to be highly amyloidogenic. Further, under experimental conditions, cOB1 formed aggregates displaying characteristics of amyloid structures such as bathochromic shift in Congo red absorbance, enhancement in thioflavin T fluorescence, and fibrillar morphology under transmission electron microscopy. This novel property of pheromone peptide cOB1 may have some direct effects on the binding of the pheromone to the receptor cells and subsequent conjugative transfer, making this observation more important for the therapeutics, dealing with the generation of virulent and multidrug-resistant pathogenic strains.
MeSH term(s)	Bacterial Proteins/chemical synthesis ; Bacterial Proteins/chemistry ; Enterococcus faecalis/chemistry ; Particle Size ; Protein Aggregates ; Protein Conformation
Chemical Substances	Bacterial Proteins ; Protein Aggregates ; cOB1 protein, Enterococcus faecalis
Language	English
Publishing date	2019-07-22
Publishing country	England
Document type	Journal Article
ZDB-ID	1234416-3
ISSN	1099-1387 ; 1075-2617
ISSN (online)	1099-1387
ISSN	1075-2617
DOI	10.1002/psc.3178
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Article ; Online: Fast and Secure Medical Image Encryption Based on Non Linear 4D Logistic Map and DNA Sequences (NL4DLM_DNA).

Stalin, Shalini / Maheshwary, Priti / Shukla, Piyush Kumar / Maheshwari, Manish / Gour, Bhupesh / Khare, Ankur

Journal of medical systems

2019 Volume 43, Issue 8, Page(s) 267

Abstract: This paper proposes an innovative image cryptosystem algorithm using the properties of the block encryption, 4D logistic map and DNA systems. Multiple key sequences are generated and pixel substitution is performed by using nonlinear 4D logistic map, ... ...

Abstract	This paper proposes an innovative image cryptosystem algorithm using the properties of the block encryption, 4D logistic map and DNA systems. Multiple key sequences are generated and pixel substitution is performed by using nonlinear 4D logistic map, then encryption is performed by using DNA rules to ensure that the different blocks are encrypted securely. The results of the experiment indicate that the proposed Non Linear 4D Logistic Map and DNA (NL4DLM_DNA) sequence based algorithm gives better performance, which is analyzed on the basis of security, quality, attack resilience, diffusion and running time as compared to some previous works.
MeSH term(s)	Algorithms ; Computer Security ; DNA ; Diagnostic Imaging
Chemical Substances	DNA (9007-49-2)
Language	English
Publishing date	2019-07-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	423488-1
ISSN	1573-689X ; 0148-5598
ISSN (online)	1573-689X
ISSN	0148-5598
DOI	10.1007/s10916-019-1389-z
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Article ; Online: Predicted aggregation-prone region (APR) in βB1-crystallin forms the amyloid-like structure and induces aggregation of soluble proteins isolated from human cataractous eye lens.

Harsolia, Ram Swaroop / Kanwar, Ambika / Gour, Shalini / Kumar, Vijay / Kumar, Vikas / Bansal, Rati / Kumar, Suman / Singh, Manish / Yadav, Jay Kant

International journal of biological macromolecules

2020 Volume 163, Page(s) 702–710

Abstract: The aggregation of β-crystallins in the human eye lens constitutes a critical step during the development of cataract. We anticipated that the presence of Aggregation-Prone Regions (APRs) in their primary structure, which might be responsible for ... ...

Abstract	The aggregation of β-crystallins in the human eye lens constitutes a critical step during the development of cataract. We anticipated that the presence of Aggregation-Prone Regions (APRs) in their primary structure, which might be responsible for conformational change required for the self-assembly. To examine the presence of APRs, we systematically analyzed the primary structures of β-crystallins. Out of seven subtypes, the βB1-crystallin found to possess the highest aggregation score with 9 APRs in its primary structure. To confirm the amyloidogenic nature of these newly identified APRs, we further studied the aggregation behavior of one of the APRs spanning from 174 to 180 residues (
MeSH term(s)	Adsorption ; Amyloidogenic Proteins/chemistry ; Amyloidogenic Proteins/isolation & purification ; Amyloidogenic Proteins/metabolism ; Amyloidogenic Proteins/ultrastructure ; Amyloidosis ; Cataract/metabolism ; Chemical Phenomena ; Congo Red/chemistry ; Lens, Crystalline/chemistry ; Lens, Crystalline/metabolism ; Molecular Dynamics Simulation ; Protein Aggregates ; Protein Conformation ; Solubility ; Structure-Activity Relationship ; beta-Crystallin B Chain/chemistry ; beta-Crystallin B Chain/metabolism
Chemical Substances	Amyloidogenic Proteins ; Protein Aggregates ; beta-Crystallin B Chain ; Congo Red (3U05FHG59S)
Language	English
Publishing date	2020-07-08
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2020.07.028
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Article ; Online: Mammalian antimicrobial peptide protegrin-4 self assembles and forms amyloid-like aggregates: Assessment of its functional relevance.

Gour, Shalini / Kumar, Vijay / Singh, Ashutosh / Gadhave, Kundlik / Goyal, Pankaj / Pandey, Janmejay / Giri, Rajanish / Yadav, Jay Kant

Journal of peptide science : an official publication of the European Peptide Society

2019 Volume 25, Issue 3, Page(s) e3151

Abstract: Protegrin-4 (PG-4) is a member of the porcine leukocyte protegrins family of cysteine-rich antimicrobial peptides (AMPs) isolated from Sus scrofa. It consists of 18 amino acid residues and works as a part of innate immune system. In this study, we ... ...

Abstract	Protegrin-4 (PG-4) is a member of the porcine leukocyte protegrins family of cysteine-rich antimicrobial peptides (AMPs) isolated from Sus scrofa. It consists of 18 amino acid residues and works as a part of innate immune system. In this study, we examined the intrinsic aggregation propensity of this AMP using multiple computational algorithms, namely, TANGO, AGGRESCAN, FOLDAMYLOID, AMYLPRED, and ZYGGREGATOR, and found that the peptide is predicted to have a high propensity for the β sheet formation that disposes this peptide to be amyloidogenic. Under in vitro conditions, PG-4 formed visible aggregates and displayed the hallmark properties of typical amyloids such as enhanced binding of Congo red, increased fluorescence with Thioflavin-T, and fibrillar morphology under transmission electron microscopy. Then we examined its antimicrobial activity against Bacillus subtilis and found that the aggregated peptide retained its antimicrobial activity. Additionally, the aggregates remain non-toxic to the HEK293 and Caco2 cells. Our study suggests that the inherent aggregation properties of AMP can rationally be explored as a potential source of peptide-based antimicrobials with enhanced stability.
MeSH term(s)	Animals ; Antimicrobial Cationic Peptides/chemistry ; Antimicrobial Cationic Peptides/metabolism ; Antimicrobial Cationic Peptides/pharmacology ; Bacillus subtilis/cytology ; Bacillus subtilis/drug effects ; Caco-2 Cells ; Dose-Response Relationship, Drug ; HEK293 Cells ; Humans ; Microbial Sensitivity Tests ; Microbial Viability/drug effects ; Protein Aggregates ; Protein Aggregation, Pathological ; Sus scrofa
Chemical Substances	Antimicrobial Cationic Peptides ; Protein Aggregates ; protegrin-4 (157214-61-4)
Language	English
Publishing date	2019-02-03
Publishing country	England
Document type	Journal Article
ZDB-ID	1234416-3
ISSN	1099-1387 ; 1075-2617
ISSN (online)	1099-1387
ISSN	1075-2617
DOI	10.1002/psc.3151
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Article ; Online: The mechanism of phosphatidylcholine-induced interference of PAP (248-286) aggregation.

Kumar, Vijay / Gour, Shalini / Verma, Nidhi / Kumar, Suman / Gadhave, Kundlik / Mishra, Pushpendra Mani / Goyal, Pankaj / Pandey, Janmejay / Giri, Rajanish / Yadav, Jay Kant

Journal of peptide science : an official publication of the European Peptide Society

2019 Volume 25, Issue 4, Page(s) e3152

Abstract: Seminal amyloids are well known for their role in enhancing HIV infection. Among all the amyloidogenic peptides identified in human semen, ... ...

Abstract	Seminal amyloids are well known for their role in enhancing HIV infection. Among all the amyloidogenic peptides identified in human semen, PAP
MeSH term(s)	Humans ; Kinetics ; Peptides/antagonists & inhibitors ; Phosphatidylcholines/chemistry ; Phosphatidylcholines/pharmacology ; Protein Aggregates/drug effects ; Semen/chemistry
Chemical Substances	Peptides ; Phosphatidylcholines ; Protein Aggregates ; 1,2-oleoylphosphatidylcholine (EDS2L3ODLV)
Language	English
Publishing date	2019-02-19
Publishing country	England
Document type	Journal Article
ZDB-ID	1234416-3
ISSN	1099-1387 ; 1075-2617
ISSN (online)	1099-1387
ISSN	1075-2617
DOI	10.1002/psc.3152
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Article ; Online: Antimicrobial peptide (Cn-AMP2) from liquid endosperm of Cocos nucifera forms amyloid-like fibrillar structure.

Gour, Shalini / Kaushik, Vibha / Kumar, Vijay / Bhat, Priyanka / Yadav, Subhash C / Yadav, Jay K

Journal of peptide science : an official publication of the European Peptide Society

2016 Volume 22, Issue 4, Page(s) 201–207

Abstract: Cn-AMP2 is an antimicrobial peptide derived from liquid endosperm of coconut (Cocos nucifera). It consists of 11 amino acid residues and predicted to have high propensity for β-sheet formation that disposes this peptide to be amyloidogenic. In the ... ...

Abstract	Cn-AMP2 is an antimicrobial peptide derived from liquid endosperm of coconut (Cocos nucifera). It consists of 11 amino acid residues and predicted to have high propensity for β-sheet formation that disposes this peptide to be amyloidogenic. In the present study, we have examined the amyloidogenic propensities of Cn-AMP2 in silico and then tested the predictions under in vitro conditions. The in silico study revealed that the peptide possesses high amyloidogenic propensity comparable with Aβ. Upon solubilisation and agitation in aqueous buffer, Cn-AMP2 forms visible aggregates that display bathochromic shift in the Congo red absorbance spectra, strong increase in thioflavin T fluorescence and fibrillar morphology under transmission electron microscopy. All these properties are typical of an amyloid fibril derived from various proteins/peptides including Aβ.
MeSH term(s)	Amyloid/chemistry ; Amyloid/ultrastructure ; Anti-Infective Agents/chemistry ; Antimicrobial Cationic Peptides/chemistry ; Cocos/chemistry ; Endosperm/chemistry ; Plant Proteins/chemistry ; Protein Aggregates ; Protein Structure, Quaternary ; Protein Structure, Secondary
Chemical Substances	Amyloid ; Anti-Infective Agents ; Antimicrobial Cationic Peptides ; Plant Proteins ; Protein Aggregates
Language	English
Publishing date	2016-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1234416-3
ISSN	1099-1387 ; 1075-2617
ISSN (online)	1099-1387
ISSN	1075-2617
DOI	10.1002/psc.2860
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Article: Predicted aggregation-prone region (APR) in βB1-crystallin forms the amyloid-like structure and induces aggregation of soluble proteins isolated from human cataractous eye lens

Harsolia, Ram Swaroop / Kanwar, Ambika / Gour, Shalini / Kumar, Vijay / Kumar, Vikas / Bansal, Rati / Kumar, Suman / Singh, Manish / Yadav, Jay Kant

International journal of biological macromolecules. 2020 Nov. 15, v. 163

2020

Abstract	The aggregation of β-crystallins in the human eye lens constitutes a critical step during the development of cataract. We anticipated that the presence of Aggregation-Prone Regions (APRs) in their primary structure, which might be responsible for conformational change required for the self-assembly. To examine the presence of APRs, we systematically analyzed the primary structures of β-crystallins. Out of seven subtypes, the βB1-crystallin found to possess the highest aggregation score with 9 APRs in its primary structure. To confirm the amyloidogenic nature of these newly identified APRs, we further studied the aggregation behavior of one of the APRs spanning from 174 to 180 residues (¹⁷⁴LWVYGFS¹⁸⁰) of βB1-crystallin, which is referred as βB1₍₁₇₄₋₁₈₀₎. Under in vitro conditions, the synthetic analogue of βB1₍₁₇₄₋₁₈₀₎ peptide formed visible aggregates and displayed high Congo red (CR) bathochromic shift, Thioflavin T (ThT) binding and fibrilar morphology under transmission electron microscopy, which are the typical characteristics of amyloids. Further, the aggregated βB1₍₁₇₄₋₁₈₀₎ was found to induce aggregation of the soluble fraction of proteins isolated from the human cataractous lens. This observation suggests that the presence of APRs in βB1-crystallin might be serving as one of the intrinsic supplementary factors responsible for constitutive aggregation behavior of βB1-crystallin and development of cataract.
Keywords	aggregation behavior ; amyloid ; cataract ; eye lens ; humans ; peptides ; transmission electron microscopy
Language	English
Dates of publication	2020-1115
Size	p. 702-710.
Publishing place	Elsevier B.V.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2020.07.028
Database	NAL-Catalogue (AGRICOLA)

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