The Analysis of OmpA and Rz/Rz1 of Lytic Bacteriophage from Surabaya, Indonesia. (23rd December 2021)
- Record Type:
- Journal Article
- Title:
- The Analysis of OmpA and Rz/Rz1 of Lytic Bacteriophage from Surabaya, Indonesia. (23rd December 2021)
- Main Title:
- The Analysis of OmpA and Rz/Rz1 of Lytic Bacteriophage from Surabaya, Indonesia
- Authors:
- Sjahriani, Tessa
Wasito, Eddy Bagus
Tyasningsih, Wiwiek - Other Names:
- Spilki Fernando Rosado Academic Editor.
- Abstract:
- Abstract : A good strategy to conquer the Escherichia coli -cause food-borne disease could be bacteriophages. Porins are a type of β -barrel proteins with diffuse channels and OmpA, which has a role in hydrophilic transport, is the most frequent porin in E. coli ; it was also chosen as the potential receptor of the phage. And the Rz/Rz1 was engaged in the breakup of the host bacterial external membrane. This study aimed to analyze the amino acid of OmpA and Rz/Rz1 of lytic bacteriophage from Surabaya, Indonesia. This study employed a sample of 8 bacteriophages from the previous study. The OmpA analysis method was mass spectrometry. Rz/Rz1 was analyzed using PCR, DNA sequencing, Expasy Translation, and Expasy ProtParam. The result obtained 10% to 29% sequence coverage of OmpA, carrying the ligand-binding site. The Rz/Rz1 gene shares a high percentage of 97.04% to 98.89% identities with the Siphoviridae isolate ctTwQ4, partial genome, and Myoviridae isolate cthRA4, partial genome. The Mann–Whitney statistical tests indicate the significant differences between Alanine, Aspartate, Glycine, Proline, Serine (p = 0.011 ), Asparagine, Cysteine (p = 0.009 ), Isoleucine (p = 0.043 ), Lysine (p = 0.034 ), Methionine (p = 0.001 ), Threonine (p = 0.018 ), and Tryptophan (p = 0.007 ) of OmpA and Rz/Rz1. The conclusion obtained from this study is the fact that OmpA acts as Phage 1, Phage 2, Phage 3, Phage 5, and Phage 6 receptors for its peptide composition comprising the ligand bindingAbstract : A good strategy to conquer the Escherichia coli -cause food-borne disease could be bacteriophages. Porins are a type of β -barrel proteins with diffuse channels and OmpA, which has a role in hydrophilic transport, is the most frequent porin in E. coli ; it was also chosen as the potential receptor of the phage. And the Rz/Rz1 was engaged in the breakup of the host bacterial external membrane. This study aimed to analyze the amino acid of OmpA and Rz/Rz1 of lytic bacteriophage from Surabaya, Indonesia. This study employed a sample of 8 bacteriophages from the previous study. The OmpA analysis method was mass spectrometry. Rz/Rz1 was analyzed using PCR, DNA sequencing, Expasy Translation, and Expasy ProtParam. The result obtained 10% to 29% sequence coverage of OmpA, carrying the ligand-binding site. The Rz/Rz1 gene shares a high percentage of 97.04% to 98.89% identities with the Siphoviridae isolate ctTwQ4, partial genome, and Myoviridae isolate cthRA4, partial genome. The Mann–Whitney statistical tests indicate the significant differences between Alanine, Aspartate, Glycine, Proline, Serine (p = 0.011 ), Asparagine, Cysteine (p = 0.009 ), Isoleucine (p = 0.043 ), Lysine (p = 0.034 ), Methionine (p = 0.001 ), Threonine (p = 0.018 ), and Tryptophan (p = 0.007 ) of OmpA and Rz/Rz1. The conclusion obtained from this study is the fact that OmpA acts as Phage 1, Phage 2, Phage 3, Phage 5, and Phage 6 receptors for its peptide composition comprising the ligand binding site, and Rz/Rz1 participates in host bacteria lysis. … (more)
- Is Part Of:
- Scientifica. Volume 2021(2021)
- Journal:
- Scientifica
- Issue:
- Volume 2021(2021)
- Issue Display:
- Volume 2021, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 2021
- Issue:
- 2021
- Issue Sort Value:
- 2021-2021-2021-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-12-23
- Subjects:
- Life sciences -- Periodicals
Biology -- Periodicals
Medicine -- Periodicals
Biological Science Disciplines
Medicine
Biology
Life sciences
Medicine
Periodicals
Electronic journals
Periodicals
500 - Journal URLs:
- https://www.hindawi.com/journals/scientifica/ ↗
- DOI:
- 10.1155/2021/7494144 ↗
- Languages:
- English
- ISSNs:
- 2090-908X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library HMNTS - ELD Digital store
- Ingest File:
- 20868.xml