Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Evolutionary and compositional analysis of streptokinase including its interaction with plasminogen: An in silico approach
Department of Human Physiology, Vidyasagar University, Midnapore 721102, West Bengal, India.
Department of Human Physiology, Vidyasagar University, Midnapore 721102, West Bengal, India.
Department of Human Physiology, Vidyasagar University, Midnapore 721102, West Bengal, India.
Department of Chemistry, Vidyasagar University, Midnapore 721102, West Bengal, India; Sadhu Ram Chand Murmu University of Jhargram, Jhargram 721507, West Bengal, India.
Show others and affiliations
2022 (English)In: Gene Reports, ISSN 2452-0144, Vol. 29, article id 101689Article in journal (Refereed) Published
Abstract [en]

Due to the accumulation of cholesterol in arterial wall, clot-forming cascade activated in the blood capillaries lead to conditions like myocardial ischemia and heart failure. These clots are dissolved by the enzyme streptokinase (SK), produced by Streptococcus sp., a normal flora in the human body. In the present study, codon-dependent evolution of twenty-three SK from Streptococcus sp. bacteria, isolated from distinct geographical origins were analyzed. Besides, domain variation, compositional analysis, effective number of codons (ENc) plot, codon adaptation index (CAI), and effect of polymorphism on SK interaction with its substrate plasminogen (Plg) were analyzed. Codon usage bias varied within a tiny range. Studies also reveal that AT ending codons are preferred over GC ending codons. Analyses of the other parameters reveal that the mutational pressure is one of the main factors to shape codon usage biasness. Interfacing and polar contact forming amino acid residues of SK with Plg is identical for all Streptococcus dysgalactiae but not for all Streptococcus pyogenes. Changes of those interfacing amino acid sites exhibit a substantial effect on polar interaction between SK and Plg. The present in silico studies are expected to shed further light to characterize and moreover, to understand the various contributing factors to influence SK adaptation that will be fulfilling to develop efficient thrombolytic therapeutics.

Place, publisher, year, edition, pages
Elsevier, 2022. Vol. 29, article id 101689
Keywords [en]
Streptokinase, Plasminogen, Multiple sequence alignment, Phylogenetic tree, Codon usage bias, Molecular docking
National Category
Biochemistry and Molecular Biology
Research subject
Chemistry of Interfaces
Identifiers
URN: urn:nbn:se:ltu:diva-93454DOI: 10.1016/j.genrep.2022.101689ISI: 000869762500005Scopus ID: 2-s2.0-85139297857OAI: oai:DiVA.org:ltu-93454DiVA, id: diva2:1701263
Note

Validerad;2022;Nivå 2;2022-11-10 (hanlid);

Funder: University Grants Commission (UGC), India

Available from: 2022-10-05 Created: 2022-10-05 Last updated: 2022-11-10Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textScopus

Authority records

Patra, Anuttam

Search in DiVA

By author/editor
Patra, Anuttam
By organisation
Chemical Engineering
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 79 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf